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3. Fungal Planet description sheets:1182-1283

Author

Crous, P. W., Cowan, D. A., Maggs-Kölling, G., Yilmaz, N., Thangavel, R., Wingfield, M. J., Noordeloos, M. E., Dima, B., Brandrud, T. E., Jansen, G. M., Morozova, O. V., Vila, J., Shivas, R. G., Tan, Y. P., Bishop-Hurley, S., Lacey, E., Marney, T. S., Larsson, E., Le Floch, G., Lombard, L., Nodet, P., Hubka, V., Alvarado, P., Berraf-Tebbal, A., Reyes, J. D., Delgado, G., Eichmeier, A., Jordal, J. B., Kachalkin, A. V., Kubatova, A., Maciá-Vicente, J. G., Malysheva, E. F., Papp, V., Rajeshkumar, K. C., Sharma, A., Spetik, M., Szabóová, D., Tomashevskaya, M. A., Abad, J. A., Abad, Z. G., Alexandrova, A. V., Anand, G., Arenas, F., Ashtekar, N., Balashov, S., Bañares, Á., Baroncelli, R., Bera, I, Biketova, A. Yu., Blomquist, C. L., Boekhout, T., Boertmann, D., Bulyonkova, T. M., Burgess, T. I., Carnegie, A. J., Cobo-Diaz, J. F., Corriol, G., Cunnington, J. H., da Cruz, M. O., Damm, U., Davoodian, N., Santiago, A. L. C. M. de A., Dearnaley, J., de Freitas, L. W. S., Dhileepan, K., Dimitrov, R., Di Piazza, S., Fatima, S., Fuljer, F., Galera, H., Ghosh, A., Giraldo, A., Glushakova, A. M., Gorczak, M., Gouliamova, D. E., Gramaje, D., Groenewald, M., Gunsch, C. K., Gutiérrez, A., Holdom, D., Houbraken, J., Ismailov, A. B., Istel, L., Iturriaga, T., Jeppson, M., Jurjevic, Z., Kalinina, L. B., Kapitonov, V. I., Kautmanová, I., Khalid, A. N., Kiran, M., Kiss, L., Kovács, Á., Kurose, D., Kusan, I., Lad, S., Læssøe, T., Lee, H. B., Luangsa-ard, J. J., Lynch, M., Mahamedi, A. E., Malysheva, V. F., Mateos, A., Matocec, N., Mesic, A., Miller, A. N., Mongkolsamrit, S., Moreno, G., Morte, A., Mostowfizadeh-Ghalamfarsa, R., Naseer, A., Navarro-Rodenas, A., Nguyen, T. T. T., Noisripoom, W., Ntandu, J. E., Nuytinck, J., Ostrý, V., Pankratov, T. A., Pawlowska, J., Pecenka, J., Pham, T. H. G., Polhorsky, A., Posta, A., Raudabaugh, D. B., Reschke, K., Rodriguez, A., Romero, M., Rooney-Latham, S., Roux, J., Sandoval-Denis, M., Smith, M. Th., Steinrucken, T. V., Svetasheva, T. Y., van der Linde, E. J., Vegte, M. v.d., Vauras, J., Verbeken, A., Visagie, C. M., Vitelli, J. S., Volobuev, S. V., Weill, A., Wrzosek, M., Zmitrovich, I. V., Zvyagina, E. A., Groenewald, J. Z., Crous, P. W., Cowan, D. A., Maggs-Kölling, G., Yilmaz, N., Thangavel, R., Wingfield, M. J., Noordeloos, M. E., Dima, B., Brandrud, T. E., Jansen, G. M., Morozova, O. V., Vila, J., Shivas, R. G., Tan, Y. P., Bishop-Hurley, S., Lacey, E., Marney, T. S., Larsson, E., Le Floch, G., Lombard, L., Nodet, P., Hubka, V., Alvarado, P., Berraf-Tebbal, A., Reyes, J. D., Delgado, G., Eichmeier, A., Jordal, J. B., Kachalkin, A. V., Kubatova, A., Maciá-Vicente, J. G., Malysheva, E. F., Papp, V., Rajeshkumar, K. C., Sharma, A., Spetik, M., Szabóová, D., Tomashevskaya, M. A., Abad, J. A., Abad, Z. G., Alexandrova, A. V., Anand, G., Arenas, F., Ashtekar, N., Balashov, S., Bañares, Á., Baroncelli, R., Bera, I, Biketova, A. Yu., Blomquist, C. L., Boekhout, T., Boertmann, D., Bulyonkova, T. M., Burgess, T. I., Carnegie, A. J., Cobo-Diaz, J. F., Corriol, G., Cunnington, J. H., da Cruz, M. O., Damm, U., Davoodian, N., Santiago, A. L. C. M. de A., Dearnaley, J., de Freitas, L. W. S., Dhileepan, K., Dimitrov, R., Di Piazza, S., Fatima, S., Fuljer, F., Galera, H., Ghosh, A., Giraldo, A., Glushakova, A. M., Gorczak, M., Gouliamova, D. E., Gramaje, D., Groenewald, M., Gunsch, C. K., Gutiérrez, A., Holdom, D., Houbraken, J., Ismailov, A. B., Istel, L., Iturriaga, T., Jeppson, M., Jurjevic, Z., Kalinina, L. B., Kapitonov, V. I., Kautmanová, I., Khalid, A. N., Kiran, M., Kiss, L., Kovács, Á., Kurose, D., Kusan, I., Lad, S., Læssøe, T., Lee, H. B., Luangsa-ard, J. J., Lynch, M., Mahamedi, A. E., Malysheva, V. F., Mateos, A., Matocec, N., Mesic, A., Miller, A. N., Mongkolsamrit, S., Moreno, G., Morte, A., Mostowfizadeh-Ghalamfarsa, R., Naseer, A., Navarro-Rodenas, A., Nguyen, T. T. T., Noisripoom, W., Ntandu, J. E., Nuytinck, J., Ostrý, V., Pankratov, T. A., Pawlowska, J., Pecenka, J., Pham, T. H. G., Polhorsky, A., Posta, A., Raudabaugh, D. B., Reschke, K., Rodriguez, A., Romero, M., Rooney-Latham, S., Roux, J., Sandoval-Denis, M., Smith, M. Th., Steinrucken, T. V., Svetasheva, T. Y., van der Linde, E. J., Vegte, M. v.d., Vauras, J., Verbeken, A., Visagie, C. M., Vitelli, J. S., Volobuev, S. V., Weill, A., Wrzosek, M., Zmitrovich, I. V., Zvyagina, E. A., and Groenewald, J. Z.

Abstract

Novel species of fungi described in this study include those from various countries as follows: Algeria, Phaeoacremonium adelophialidum from Vitis vinifera. Antarctica, Comoclathris antarctica from soil. Australia, Coniochaeta salicifolia as endophyte from healthy leaves of Geijera salicifolia, Eremothecium peggii in fruit of Citrus australis, Microdochium ratticaudae from stem of Sporobolus natalensis, Neocelosporium corymbiae on stems of Corymbia variegata, Phytophthora kelmanii from rhizosphere soil of Ptilotus pyramidatus, Pseudosydowia backhousiae on living leaves of Backhousia citriodora, Pseudosydowia indooroopillyensis, Pseudosydowia louisecottisiae and Pseudosydowia queenslandica on living leaves of Eucalyptus sp. Brazil, Absidia montepascoalis from soil. Chile, Ilyonectria zarorii from soil under Maytenus boaria. Costa Rica, Colletotrichum filicis from an unidentified fern. Croatia, Mollisia endogranulata on deteriorated hardwood. Czech Republic, Arcopilus navicularis from tea bag with fruit tea, Neosetophoma buxi as endophyte from Buxus sempervirens, Xerochrysium bohemicum on surface of biscuits with chocolate glaze and filled with jam. France, Entoloma cyaneobasale on basic to calcareous soil, Fusarium aconidiale from Triticum aestivum, Fusarium juglandicola from buds of Juglans regia. Germany, Tetraploa endophytica as endophyte from Microthlaspi perfoliatum roots. India, Castanediella ambae on leaves of Mangifera indica, Lactifluus kanadii on soil under Castanopsis sp., Penicillium uttarakhandense from soil. Italy, Penicillium ferraniaense from compost. Namibia, Bezerromyces gobabebensis on leaves of unidentified succulent, Cladosporium stipagrostidicola on leaves of Stipagrostis sp., Cymostachys euphorbiae on leaves of Euphorbia sp., Deniquelata hypolithi from hypolith under a rock, Hysterobrevium walvisbayicola on leaves of unidentified tree, Knufia hypolithi and Knufia walvisbayicola from hypolith under a rock, Lapidomyces stipagrostidicola on lea

Published
2021

4. Fungal Planet description sheets: 1182-1283

Author

Conselho Nacional de Desenvolvimento Científico e Tecnológico (Brasil), Fundação de Amparo à Ciência e Tecnologia do Estado de Pernambuco, Russian Foundation for Basic Research, Russian Academy of Sciences, Swedish Taxonomy Initiative, German Research Foundation, LOEWE Center for Insect Biotechnology & Bioresources, Russian Government, Lomonosov Moscow State University, Ministry of Science and Higher Education of the Russian Federation, University of Warsaw, European Commission, Hemvati Nandan Bahuguna Garhwal University, Russian Science Foundation, Rural Industries Research and Development Corporation (Australia), Department of Agriculture and Water Resources (Australia), Croatian Science Foundation, Department of Science and Technology (India), International Centre for Genetic Engineering and Biotechnology, Bulgarian National Science Fund, Universidad de Alcalá, Charles University (Czech Republic), Ministry of Agriculture of the Czech Republic, Ministry of Innovation and Technology (Hungary), National Research, Development and Innovation Office (Hungary), Norwegian Biodiversity Information Centre, University of Oslo, Ministerio de Economía y Competitividad (España), Fundación Séneca, Ministry of Health of the Czech Republic, Crous, P. W., Cowan, D. A., Maggs-Kölling, G., Yilmaz, N., Thangavel, R., Wingfield, M. J., Noordeloos, M. E., Dima, B., Brandrud, T. E., Jansen, G. M., Morozova, O. V., Cunnington, J. H., Biketova, A. Yu., Blomquist, C. L., Boekhout, T., Boertmann, D., Bulyonkova, T. M., Burgess, T. I., Cruz, M. O. da, Damm, U., Davoodian, N., Matočec, N., Santiago, A. L. C. M. de A., Dearnaley, J., Freitas, L. W. S., Mahamedi, A. E., Dhileepan, K., Dimitrov, R., Di Piazza, S., Fatima, S., Fuljer, F., Galera, H., Kušan, I., Ghosh, A., Giraldo, A., Glushakova, A. M., Gorczak, M., Malysheva, V. F, Gouliamova, D. E., Gramaje, David, Groenewald, M., Gunsch, C. K., Gutierrez-Aguirregabiria, A., Lad, S., Holdom, D., Houbraken, J., Ismailov, A. B., Istel, Ł., Iturriaga, T., Mateos, A., Jeppson, M., Jurjević, Željko, Kalinina, L. B., Kapitonov, V. I., Læssøe, T., Kautmanová, I., Khalid, Abdul Nasir, Kiran, M., Kiss, L., Kovács, A., Kurose, D., Lee, H. B., Luangsa-Ard, J. J., Lynch, M., Mešić, A., Miller, A. N., Mongkolsamrit, S., Bishop-Hurley, S., Moreno, G., Morte, A., Mostowfizadeh-Ghalamfarsa, R., Vila, J., Naseer, Arooj, Navarro-Ródenas, A., Nguyen, T. T. T., Noisripoom, W., Ntandu, J. E., Nuytinck, J., Volobuev, S. V., Ostrý, V., Pankratov, T. A., Pawłowska, J., Pečenka, Jakub, Shivas, R. G., Pham, T. H. G., Polhorský, A., Pošta, A., Raudabaugh, D. B., Reschke, K., Weill, A., Rodríguez, A., Romero, M., Rooney-Latham, S., Roux, J., Sandoval-Denis, M., Tan, Y. P., Smith, M. Th., Steinrucken, T. V., Svetasheva, T. Y., Tkalčec, Z., Wrzosek, M., Linde, E. J. van der, Vegte, M., Vauras, J., Verbeken, A., Visagie, C. M., Vitelli, J. S., Zmitrovich, I. V., Zvyagina, E. A., Groenewald, J. Z., Lacey, E., Marney, T. S., Larsson, K.-H., Carnegie, A. J., Le Floch, G, Lombard, L., Nodet, P., Hubka, V., Alvarado, P., Berraf-Tebbal, Akila, Reyes, J. D., Delgado, Gregorio, Eichmeier, Ales, Jordal, J. B., Cobo-Díaz, José F., Kachalkin, A.V., Kubátová, A., Maciá-Vicente, José G., Malysheva, E. F., Papp, V., Rajeshkumar, Kunhiraman C., Sharma, A., Spetik, M., Szabóová, D., Tomashevskaya, M. A., Corriol, G., Abad, J. A., Abad, Z. G., Alexandrova, A. V., Anand, G., Arenas, F., Ashtekar, N., Balashov, S., Bañares, Ángel, Baroncelli, R., Bera, I., Conselho Nacional de Desenvolvimento Científico e Tecnológico (Brasil), Fundação de Amparo à Ciência e Tecnologia do Estado de Pernambuco, Russian Foundation for Basic Research, Russian Academy of Sciences, Swedish Taxonomy Initiative, German Research Foundation, LOEWE Center for Insect Biotechnology & Bioresources, Russian Government, Lomonosov Moscow State University, Ministry of Science and Higher Education of the Russian Federation, University of Warsaw, European Commission, Hemvati Nandan Bahuguna Garhwal University, Russian Science Foundation, Rural Industries Research and Development Corporation (Australia), Department of Agriculture and Water Resources (Australia), Croatian Science Foundation, Department of Science and Technology (India), International Centre for Genetic Engineering and Biotechnology, Bulgarian National Science Fund, Universidad de Alcalá, Charles University (Czech Republic), Ministry of Agriculture of the Czech Republic, Ministry of Innovation and Technology (Hungary), National Research, Development and Innovation Office (Hungary), Norwegian Biodiversity Information Centre, University of Oslo, Ministerio de Economía y Competitividad (España), Fundación Séneca, Ministry of Health of the Czech Republic, Crous, P. W., Cowan, D. A., Maggs-Kölling, G., Yilmaz, N., Thangavel, R., Wingfield, M. J., Noordeloos, M. E., Dima, B., Brandrud, T. E., Jansen, G. M., Morozova, O. V., Cunnington, J. H., Biketova, A. Yu., Blomquist, C. L., Boekhout, T., Boertmann, D., Bulyonkova, T. M., Burgess, T. I., Cruz, M. O. da, Damm, U., Davoodian, N., Matočec, N., Santiago, A. L. C. M. de A., Dearnaley, J., Freitas, L. W. S., Mahamedi, A. E., Dhileepan, K., Dimitrov, R., Di Piazza, S., Fatima, S., Fuljer, F., Galera, H., Kušan, I., Ghosh, A., Giraldo, A., Glushakova, A. M., Gorczak, M., Malysheva, V. F, Gouliamova, D. E., Gramaje, David, Groenewald, M., Gunsch, C. K., Gutierrez-Aguirregabiria, A., Lad, S., Holdom, D., Houbraken, J., Ismailov, A. B., Istel, Ł., Iturriaga, T., Mateos, A., Jeppson, M., Jurjević, Željko, Kalinina, L. B., Kapitonov, V. I., Læssøe, T., Kautmanová, I., Khalid, Abdul Nasir, Kiran, M., Kiss, L., Kovács, A., Kurose, D., Lee, H. B., Luangsa-Ard, J. J., Lynch, M., Mešić, A., Miller, A. N., Mongkolsamrit, S., Bishop-Hurley, S., Moreno, G., Morte, A., Mostowfizadeh-Ghalamfarsa, R., Vila, J., Naseer, Arooj, Navarro-Ródenas, A., Nguyen, T. T. T., Noisripoom, W., Ntandu, J. E., Nuytinck, J., Volobuev, S. V., Ostrý, V., Pankratov, T. A., Pawłowska, J., Pečenka, Jakub, Shivas, R. G., Pham, T. H. G., Polhorský, A., Pošta, A., Raudabaugh, D. B., Reschke, K., Weill, A., Rodríguez, A., Romero, M., Rooney-Latham, S., Roux, J., Sandoval-Denis, M., Tan, Y. P., Smith, M. Th., Steinrucken, T. V., Svetasheva, T. Y., Tkalčec, Z., Wrzosek, M., Linde, E. J. van der, Vegte, M., Vauras, J., Verbeken, A., Visagie, C. M., Vitelli, J. S., Zmitrovich, I. V., Zvyagina, E. A., Groenewald, J. Z., Lacey, E., Marney, T. S., Larsson, K.-H., Carnegie, A. J., Le Floch, G, Lombard, L., Nodet, P., Hubka, V., Alvarado, P., Berraf-Tebbal, Akila, Reyes, J. D., Delgado, Gregorio, Eichmeier, Ales, Jordal, J. B., Cobo-Díaz, José F., Kachalkin, A.V., Kubátová, A., Maciá-Vicente, José G., Malysheva, E. F., Papp, V., Rajeshkumar, Kunhiraman C., Sharma, A., Spetik, M., Szabóová, D., Tomashevskaya, M. A., Corriol, G., Abad, J. A., Abad, Z. G., Alexandrova, A. V., Anand, G., Arenas, F., Ashtekar, N., Balashov, S., Bañares, Ángel, Baroncelli, R., and Bera, I.

Abstract

Novel species of fungi described in this study include those from various countries as follows: Algeria, Phaeoacremonium adelophialidum from Vitis vinifera. Antarctica, Comoclathris antarctica from soil. Australia, Coniochaeta salicifolia as endophyte from healthy leaves of Geijera salicifolia, Eremothecium peggii in fruit of Citrus australis, Microdochium ratticaudae from stem of Sporobolus natalensis, Neocelosporium corymbiae on stems of Corymbia variegata, Phytophthora kelmanii from rhizosphere soil of Ptilotus pyramidatus, Pseudosydowia backhousiae on living leaves of Backhousia citriodora, Pseudosydowia indoor oopillyensis, Pseudosydowia louisecottisiae and Pseudosydowia queenslandica on living leaves of Eucalyptus sp. Brazil, Absidia montepascoalis from soil. Chile, Ilyonectria zarorii from soil under Maytenus boaria. Costa Rica, Colletotrichum filicis from an unidentified fern. Croatia, Mollisia endogranulata on deteriorated hardwood. Czech Republic, Arcopilus navicularis from tea bag with fruit tea, Neosetophoma buxi as endophyte from Buxus sempervirens, Xerochrysium bohemicum on surface of biscuits with chocolate glaze and filled with jam. France, Entoloma cyaneobasale on basic to calcareous soil, Fusarium aconidiale from Triticum aestivum, Fusarium juglandicola from buds of Juglans regia. Germany, Tetraploa endophytica as endophyte from Microthlaspi perfoliatum roots. India, Castanediella ambae on leaves of Mangifera indica, Lactifluus kanadii on soil under Castanopsis sp., Penicillium uttarakhandense from soil. Italy, Penicillium ferraniaense from compost. Namibia, Bezerromyces gobabebensis on leaves of unidentified succulent, Cladosporium stipagrostidicola on leaves of Stipagrostis sp., Cymostachys euphorbiae on leaves of Euphorbia sp., Deniquelata hypolithi from hypolith under a rock, Hysterobrevium walvisbayicola on leaves of unidentified tree, Knufia hypolithi and Knufia walvisbayicola from hypolith under a rock, Lapidomyces stipagrostidicola on leave

Published
2021

5. Cross-Linked Collagen Triple Helices by Oxime Ligation

Author

Nina B. Hentzen, Linde E. J. Smeenk, Sereina Riniker, Helma Wennemers, and Jagna Witek

Subjects
chemistry.chemical_classification, Protein Stability, 010405 organic chemistry, Stereochemistry, General Chemistry, 010402 general chemistry, Oxime, 01 natural sciences, Biochemistry, Catalysis, 0104 chemical sciences, Amino acid, Folding (chemistry), chemistry.chemical_compound, Colloid and Surface Chemistry, chemistry, Covalent bond, Oximes, Collagen, Proline, Ligation, Triple helix, Cysteine
Abstract

Covalent cross-links are crucial for the folding and stability of triple-helical collagen, the most abundant protein in nature. Cross-linking is also an attractive strategy for the development of synthetic collagen-based biocompatible materials. Nature uses interchain disulfide bridges to stabilize collagen trimers. However, their implementation into synthetic collagen is difficult and requires the replacement of the canonical amino acids (4R)-hydroxyproline and proline by cysteine or homocysteine, which reduces the preorganization and thereby stability of collagen triple helices. We therefore explored alternative covalent cross-links that allow for connecting triple-helical collagen via proline residues. Here, we present collagen model peptides that are cross-linked by oxime bonds between 4-aminooxyproline (Aop) and 4-oxoacetamidoproline placed in coplanar Xaa and Yaa positions of neighboring strands. The covalently connected strands folded into hyperstable collagen triple helices (Tm ≈ 80 °C). The desig...

Published
2017
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6. Reconstructing the Discontinuous and Conformational β1/β 3-Loop Binding Site on hFSH/hCG by Using Highly Constrained Multicyclic Peptides

Author

Joris J. Benschop, Wouter Cornelis Puijk, Drohpatie Timmers‐Parohi, Peter Timmerman, Henk Hiemstra, Linde E. J. Smeenk, Jan H. van Maarseveen, and Synthetic Organic Chemistry (HIMS, FNWI)

Subjects
Models, Molecular, Antigen-Antibody Complex, Stereochemistry, Molecular Sequence Data, Peptide, Plasma protein binding, Biochemistry, Chorionic Gonadotropin, Peptides, Cyclic, Catalysis, Protein Structure, Secondary, chemistry.chemical_compound, Biomimetic Materials, Oximes, Side chain, Humans, Amino Acid Sequence, Disulfides, Binding site, Molecular Biology, Peptide sequence, chemistry.chemical_classification, Binding Sites, Organic Chemistry, Antibodies, Monoclonal, Oxime, Kinetics, chemistry, Covalent bond, Cyclization, Molecular Medicine, Follicle Stimulating Hormone, Protein Binding
Abstract

Making peptide-based molecules that mimic functional interaction sites on proteins remains a challenge in biomedical sciences. Here, we present a robust technology for the covalent assembly of highly constrained and discontinuous binding site mimics, the potential of which is exemplified for structurally complex binding sites on the "Cys-knot" proteins hFSH and hCG. Peptidic structures were assembled by Ar(CH2Br)(2)-promoted peptide cyclizations, combined with oxime ligation and disulfide formation. The technology allows unprotected side chain groups and is applicable to peptides of different lengths and nature. A tetracyclic FSH mimic was constructed, showing >600-fold improved binding compared to linear or monocyclic controls. Binding of a tricyclic hCG mimic to anti-hCG mAb 8G5 was identical to hCG itself (IC50= 260 vs. 470 pm), whereas this mimic displayed an IC50 value of 149 nm for mAb 3468, an hCG-neutralizing antibody with undetectable binding to either linear or monocyclic controls.

Published
2015

7. Folding Dynamics of the Trp-Cage Miniprotein: Evidence for a Native-Like Intermediate from Combined Time-Resolved Vibrational Spectroscopy and Molecular Dynamics Simulations

Author

Kristen A. Marino, Albert J Kettelarij, Matthijs R. Panman, Heleen Meuzelaar, Linde E. J. Smeenk, Peter Timmerman, Adriana Huerta-Viga, Jan H. van Maarseveen, Peter G. Bolhuis, Sander Woutersen, Synthetic Organic Chemistry (HIMS, FNWI), Simulation of Biomolecular Systems (HIMS, FNWI), and Molecular Spectroscopy (HIMS, FNWI)

Subjects
Protein Folding, Time Factors, Protein Conformation, Phi value analysis, Molecular Dynamics Simulation, 010402 general chemistry, Vibration, 01 natural sciences, Protein Structure, Secondary, Absorption, 03 medical and health sciences, Molecular dynamics, Protein structure, Spectroscopy, Fourier Transform Infrared, Materials Chemistry, Transition Temperature, Folding funnel, Physical and Theoretical Chemistry, 030304 developmental biology, Quantitative Biology::Biomolecules, 0303 health sciences, Chemistry, Lasers, Spectrum Analysis, Temperature, Contact order, Protein Structure, Tertiary, 0104 chemical sciences, Surfaces, Coatings and Films, Folding (chemistry), Kinetics, Crystallography, Protein folding, Downhill folding, Peptides, Hydrophobic and Hydrophilic Interactions
Abstract

Trp-cage is a synthetic 20-residue miniprotein which folds rapidly and spontaneously to a well-defined globular structure more typical of larger proteins. Due to its small size and fast folding, it is an ideal model system for experimental and theoretical investigations of protein folding mechanisms. However, Trp-cage's exact folding mechanism is still a matter of debate.,Here we investigate Trp-cage's relaxation dynamics in the amide I' spectral region (1530- 1700 cm(-1)) using time-resolved infrared spectroscopy. Residue-specific information was obtained by incorporating an isotopic label (C-13=O-18) into the amide carbonyl group of residue Gly11, thereby spectrally isolating an individual 3(10)-helical residue. The folding unfolding equilibrium is perturbed using a nanosecond temperature jump (T jump), and the subsequent re-equilibration is probed by observing the time dependent vibrational response in the amide I' region. We observe bimodal relaxation kinetics with time constants of 100 +/- 10 and 770 +/- 40 ns at 322 K, suggesting that the folding involves an intermediate state, the character of which can be determined from the time and frequency resolved data We find that the relaxation dynamics close to the melting temperature involve fast fluctuations in the polyproline II region, whereas the slower process can be attributed to conformational rearrangements due to the global (un)folding transition of the protein. Combined analysis of our T-jump data and molecular dynamics simulations indicates that the formation of a well-defined alpha-helix precedes the rapid formation of the hydrophobic cage structure, implying a native like folding intermediate, that Mainly differs from the folded conformation in the orientation of the C-terminal polyproline II helix relative to the N-terminal part of the backbone., We find that the main free energy barrier is positioned between the folding intermediate and the unfolded state ensemble, and that it involves the formation of the alpha-helix, the 3(10)-helix, and the Asp9- Arg16 salt bridge. Our results suggest that at low temperature (T << T-m) a folding path via formation of alpha-helical contacts followed by hydrophobic clustering becomes more important.

Published
2013
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8. Selective enrichment of azide-containing peptides from complex mixtures

Author

Leo J. de Koning, Luitzen de Jong, Jeremy M. Baskin, Chris G. de Koster, Linde E. J. Smeenk, JaapWillem Back, Gert Jan Kramer, Jan H. van Maarseveen, Merel A. Nessen, Henk Hiemstra, Carolyn R. Bertozzi, Synthetic Organic Chemistry (HIMS, FNWI), Faculteit der Geneeskunde, Mass Spectrometry of Biomacromolecules (SILS, FNWI), and Medical Biochemistry

Subjects
Proteomics, Azides, Proteome, Molecular Sequence Data, Peptide, Biochemistry, Article, Mass Spectrometry, Glutarates, chemistry.chemical_compound, Methionine, Cations, Amino Acid Sequence, Peptide sequence, Alanine, chemistry.chemical_classification, biology, Cytochrome c, Cytochromes c, General Chemistry, Chromatography, Ion Exchange, Combinatorial chemistry, Amino acid, Kinetics, Cross-Linking Reagents, chemistry, Covalent bond, biology.protein, Azide, Peptides
Abstract

A general method is described to sequester peptides containing azides from complex peptide mixtures, aimed at facilitating mass spectrometric analysis to study different aspects of proteome dynamics. The enrichment method is based on covalent capture of azide-containing peptides by the azide-reactive cyclooctyne (ARCO) resin and is demonstrated for two different applications. Enrichment of peptides derived from cytochrome c treated with the azide-containing cross-linker bis(succinimidyl)-3-azidomethyl glutarate (BAMG) shows several cross-link containing peptides. Sequestration of peptides derived from an Escherichia coli proteome, pulse labeled with the bio-orthogonal amino acid azidohomoalanine as substitute for methionine, allows identification of numerous newly synthesized proteins. Furthermore, the method is found to be very specific, as after enrichment over 87% of all peptides contain (modified) azidohomoalanine.

Published
2009
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10. Genera of phytopathogenic fungi: GOPHY 1

Author

Marin-Felix, Y., Groenewald, J. Z., Cai, L., Chen, Q., Marincowitz, S., Barnes, I., Bensch, K., Braun, U., Camporesi, E., Damm, U., de Beer, Z. W., Dissanayake, A., Edwards, J., Giraldo, A., Hernández-Restrepo, M., Hyde, K. D., Jayawardena, R. S., Lombard, L., Luangsa-ard, J., McTaggart, A. R., Rossman, A. Y., Sandoval-Denis, M., Shen, M., Shivas, R. G., Tan, Y. P., van der Linde, E. J., Wingfield, M. J., Wood, A. R., Zhang, J. Q., Zhang, Y., Crous, P. W., Marin-Felix, Y., Groenewald, J. Z., Cai, L., Chen, Q., Marincowitz, S., Barnes, I., Bensch, K., Braun, U., Camporesi, E., Damm, U., de Beer, Z. W., Dissanayake, A., Edwards, J., Giraldo, A., Hernández-Restrepo, M., Hyde, K. D., Jayawardena, R. S., Lombard, L., Luangsa-ard, J., McTaggart, A. R., Rossman, A. Y., Sandoval-Denis, M., Shen, M., Shivas, R. G., Tan, Y. P., van der Linde, E. J., Wingfield, M. J., Wood, A. R., Zhang, J. Q., Zhang, Y., and Crous, P. W.

Abstract

Genera of Phytopathogenic Fungi (GOPHY) is introduced as a new series of publications in order to provide a stable platform for the taxonomy of phytopathogenic fungi. This first paper focuses on 21 genera of phytopathogenic fungi: Bipolaris, Boeremia, Calonectria, Ceratocystis, Cladosporium, Colletotrichum, Coniella, Curvularia, Monilinia, Neofabraea, Neofusicoccum, Pilidium, Pleiochaeta, Plenodomus, Protostegia, Pseudopyricularia, Puccinia, Saccharata, Thyrostroma, Venturia and Wilsonomyces. For each genus, a morphological description and information about its pathology, distribution, hosts and disease symptoms are provided. In addition, this information is linked to primary and secondary DNA barcodes of the presently accepted species, and relevant literature. Moreover, several novelties are introduced, i.e. new genera, species and combinations, and neo-, lecto- and epitypes designated to provide a stable taxonomy. This first paper includes one new genus, 26 new species, ten new combinations, and four typifications of older names.

Published
2017

11. Synthesis of water-soluble scaffolds for peptide cyclization, labeling, and ligation

Author

Nicolas Dailly, Henk Hiemstra, Jan H. van Maarseveen, Linde E. J. Smeenk, Peter Timmerman, and Synthetic Organic Chemistry (HIMS, FNWI)

Subjects
chemistry.chemical_classification, Azides, Molecular Structure, Organic Chemistry, Water, Peptide, Oxime, Biochemistry, Combinatorial chemistry, Peptides, Cyclic, Cycloaddition, chemistry.chemical_compound, Kinetics, Water soluble, chemistry, Solubility, Cyclization, Alkynes, Oximes, Side chain, Organic chemistry, Reactivity (chemistry), Chemical ligation, Physical and Theoretical Chemistry, Ligation
Abstract

The synthesis and applications of water-soluble scaffolds that conformationally constrain side chain unprotected linear peptides containing two cysteines are described. These scaffolds contain a functionality with orthogonal reactivity to be used for labeling and ligation. This is illustrated by the chemical ligation of two dissimilar constrained peptides via oxime ligation or strain-promoted azide–alkyne cycloaddition in aqueous media.

Published
2012

12. Folding Dynamics of the Trp-Cage Miniprotein: Evidence for a Native-Like Intermediate from Combined Time-Resolved Vibrational Spectroscopy and Molecular Dynamics Simulations

Author

Meuzelaar, Heleen, Marino, Kristen A., Huerta-Viga, Adriana, Panman, Matthijs R., Smeenk, Linde E. J., Kettelarij, Albert J., van Maarseveen, Jan H., Timmerman, Peter, Bolhuis, Peter G., and Woutersen, Sander

Abstract

Trp-cage is a synthetic 20-residue miniprotein which folds rapidly and spontaneously to a well-defined globular structure more typical of larger proteins. Due to its small size and fast folding, it is an ideal model system for experimental and theoretical investigations of protein folding mechanisms. However, Trp-cage’s exact folding mechanism is still a matter of debate. Here we investigate Trp-cage’s relaxation dynamics in the amide I′ spectral region (1530–1700 cm–1) using time-resolved infrared spectroscopy. Residue-specific information was obtained by incorporating an isotopic label (13C18O) into the amide carbonyl group of residue Gly11, thereby spectrally isolating an individual 310-helical residue. The folding–unfolding equilibrium is perturbed using a nanosecond temperature-jump (T-jump), and the subsequent re-equilibration is probed by observing the time-dependent vibrational response in the amide I′ region. We observe bimodal relaxation kinetics with time constants of 100 ± 10 and 770 ± 40 ns at 322 K, suggesting that the folding involves an intermediate state, the character of which can be determined from the time- and frequency-resolved data. We find that the relaxation dynamics close to the melting temperature involve fast fluctuations in the polyproline II region, whereas the slower process can be attributed to conformational rearrangements due to the global (un)folding transition of the protein. Combined analysis of our T-jump data and molecular dynamics simulations indicates that the formation of a well-defined α-helix precedes the rapid formation of the hydrophobic cage structure, implying a native-like folding intermediate, that mainly differs from the folded conformation in the orientation of the C-terminal polyproline II helix relative to the N-terminal part of the backbone. We find that the main free-energy barrier is positioned between the folding intermediate and the unfolded state ensemble, and that it involves the formation of the α-helix, the 310-helix, and the Asp9–Arg16 salt bridge. Our results suggest that at low temperature (T≪ Tm) a folding path via formation of α-helical contacts followed by hydrophobic clustering becomes more important.

Published
2024
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15. Cover Picture: Reconstructing the Discontinuous and Conformational β1/β3-Loop Binding Site on hFSH/hCG by Using Highly Constrained Multicyclic Peptides (ChemBioChem 1/2015)

Author

Drohpatie Timmers‐Parohi, Linde E. J. Smeenk, Joris J. Benschop, Wouter Cornelis Puijk, Henk Hiemstra, Jan H. van Maarseveen, and Peter Timmerman

Subjects
Loop (topology), Organic Chemistry, Biophysics, Molecular Medicine, Cover (algebra), Discontinuous epitope, Biology, Binding site, Molecular Biology, Biochemistry, Combinatorial chemistry
Published
2014
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16. Folding Dynamics of the Trp-Cage Miniprotein: Evidence for a Native-Like Intermediate from Combined Time-Resolved Vibrational Spectroscopy and Molecular Dynamics Simulations

Author

Meuzelaar, Heleen, primary, Marino, Kristen A., additional, Huerta-Viga, Adriana, additional, Panman, Matthijs R., additional, Smeenk, Linde E. J., additional, Kettelarij, Albert J., additional, van Maarseveen, Jan H., additional, Timmerman, Peter, additional, Bolhuis, Peter G., additional, and Woutersen, Sander, additional

Published
2013
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17. Finding the missing link: Resolving the Coryneliomycetidae within Eurotiomycetes.

Author

Wood, A. R., Damm, U., van der Linde, E. J., Groenewald, J. Z., Cheewangkoon, R., and Crous, P. W.

Subjects
EUROTIOMYCETES, PODOCARPACEAE, MOLECULAR phylogeny, PODOCARPUS, GENOMICS
Abstract

Species belonging to the Coryneliaceae and parasitizing Podocarpaceae hosts were collected from different locations in South Africa and studied morphologically by light microscopy and molecularly by obtaining partial nrDNA (ITS-1/5.8S/ITS-2, 18S and 28S) gene sequences. The position of the Coryneliaceae within the Eurotiomycetidae was not confirmed and a new subclass, Coryneliomycetidae, was introduced. While Eurotiomycetidae usually form cleistothecia/gymnothecia with evanescent, unitunicate asci, and Chaetothyriomycetidae mostly perithecia with bitunicate/fissitunicate to evanescent asci, Coryneliomycetidae form pseudothecial mazaedial ascomata, initially with double-walled asci with the outer layer deliquescing, resulting in passive ascospore release. The Coryneliomycetidae thus occupies a unique position in the Eurotiomycetes. Furthermore, epitypes were designated for Corynelia uberata, the type species of Corynelia (type genus of the family, order and subclass), Lagenulopsis bispora, the type species of Lagenulopsis, and Tripospora tripos the type species of Tripospora, with Lagenulopsis and Tripospora confirmed as belonging to the Coryneliaceae. Corynelia uberata resolved into three clades, one on Afrocarpus (= Podocarpus) falcatus and A. gracilior, and two clades occurring on P. latifolius, herein described as C. africana and C. fructigena. Morphologically these three species are not readily distinguishable, although they differ in spore dimensions, ascomata shape, ornamentation and DNA phylogeny. It is likely that several more species from other parts of the world are currently erroneously placed in C. uberata. [ABSTRACT FROM AUTHOR]

Published
2017
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20. Selective Enrichment of Azide-Containing Peptides from Complex Mixtures

Author

Nessen, Merel A., primary, Kramer, Gertjan, additional, Back, JaapWillem, additional, Baskin, Jeremy M., additional, Smeenk, Linde E. J., additional, de Koning, Leo J., additional, van Maarseveen, Jan H., additional, de Jong, Luitzen, additional, Bertozzi, Carolyn R., additional, Hiemstra, Henk, additional, and de Koster, Chris G., additional

Published
2009
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26. New and interesting records of South African fungi, XV. Two new Laboulbeniales records from...

Author

van der Linde, E. J and Rong, I.H.

Subjects
*LABOULBENIALES
Abstract

Reports that Laboulbeniales are predominately parasites of true insects which infest mostly Coleoptera. Reference to two members of the Laboulbeniales being reported from South Africa for the first time; Names of these members; Provision of illustration of both fungi; Information on the distribution, morphology, host specificity and nutrition.

Published
1997
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27. Fungal Planet description sheets: 1182-1283.

Author

Crous PW, Cowan DA, Maggs-Kölling G, Yilmaz N, Thangavel R, Wingfield MJ, Noordeloos ME, Dima B, Brandrud TE, Jansen GM, Morozova OV, Vila J, Shivas RG, Tan YP, Bishop-Hurley S, Lacey E, Marney TS, Larsson E, Le Floch G, Lombard L, Nodet P, Hubka V, Alvarado P, Berraf-Tebbal A, Reyes JD, Delgado G, Eichmeier A, Jordal JB, Kachalkin AV, Kubátová A, Maciá-Vicente JG, Malysheva EF, Papp V, Rajeshkumar KC, Sharma A, Spetik M, Szabóová D, Tomashevskaya MA, Abad JA, Abad ZG, Alexandrova AV, Anand G, Arenas F, Ashtekar N, Balashov S, Bañares Á, Baroncelli R, Bera I, Biketova AY, Blomquist CL, Boekhout T, Boertmann D, Bulyonkova TM, Burgess TI, Carnegie AJ, Cobo-Diaz JF, Corriol G, Cunnington JH, da Cruz MO, Damm U, Davoodian N, de A Santiago ALCM, Dearnaley J, de Freitas LWS, Dhileepan K, Dimitrov R, Di Piazza S, Fatima S, Fuljer F, Galera H, Ghosh A, Giraldo A, Glushakova AM, Gorczak M, Gouliamova DE, Gramaje D, Groenewald M, Gunsch CK, Gutiérrez A, Holdom D, Houbraken J, Ismailov AB, Istel Ł, Iturriaga T, Jeppson M, Jurjević Ž, Kalinina LB, Kapitonov VI, Kautmanová I, Khalid AN, Kiran M, Kiss L, Kovács Á, Kurose D, Kušan I, Lad S, Læssøe T, Lee HB, Luangsa-Ard JJ, Lynch M, Mahamedi AE, Malysheva VF, Mateos A, Matočec N, Mešić A, Miller AN, Mongkolsamrit S, Moreno G, Morte A, Mostowfizadeh-Ghalamfarsa R, Naseer A, Navarro-Ródenas A, Nguyen TTT, Noisripoom W, Ntandu JE, Nuytinck J, Ostrý V, Pankratov TA, Pawłowska J, Pecenka J, Pham THG, Polhorský A, Pošta A, Raudabaugh DB, Reschke K, Rodríguez A, Romero M, Rooney-Latham S, Roux J, Sandoval-Denis M, Smith MT, Steinrucken TV, Svetasheva TY, Tkalčec Z, van der Linde EJ, V D Vegte M, Vauras J, Verbeken A, Visagie CM, Vitelli JS, Volobuev SV, Weill A, Wrzosek M, Zmitrovich IV, Zvyagina EA, and Groenewald JZ

Abstract

Novel species of fungi described in this study include those from various countries as follows: Algeria , Phaeoacremonium adelophialidum from Vitis vinifera. Antarctica , Comoclathris antarctica from soil. Australia , Coniochaeta salicifolia as endophyte from healthy leaves of Geijera salicifolia , Eremothecium peggii in fruit of Citrus australis , Microdochium ratticaudae from stem of Sporobolus natalensis , Neocelosporium corymbiae on stems of Corymbia variegata , Phytophthora kelmanii from rhizosphere soil of Ptilotus pyramidatus , Pseudosydowia backhousiae on living leaves of Backhousia citriodora , Pseudosydowia indooroopillyensis , Pseudosydowia louisecottisiae and Pseudosydowia queenslandica on living leaves of Eucalyptus sp. Brazil , Absidia montepascoalis from soil. Chile , Ilyonectria zarorii from soil under Maytenus boaria. Costa Rica , Colletotrichum filicis from an unidentified fern. Croatia , Mollisia endogranulata on deteriorated hardwood. Czech Republic , Arcopilus navicularis from tea bag with fruit tea, Neosetophoma buxi as endophyte from Buxus sempervirens , Xerochrysium bohemicum on surface of biscuits with chocolate glaze and filled with jam. France , Entoloma cyaneobasale on basic to calcareous soil, Fusarium aconidiale from Triticum aestivum , Fusarium juglandicola from buds of Juglans regia. Germany , Tetraploa endophytica as endophyte from Microthlaspi perfoliatum roots . India , Castanediella ambae on leaves of Mangifera indica , Lactifluus kanadii on soil under Castanopsis sp., Penicillium uttarakhandense from soil. Italy , Penicillium ferraniaense from compost. Namibia , Bezerromyces gobabebensis on leaves of unidentified succulent, Cladosporium stipagrostidicola on leaves of Stipagrostis sp., Cymostachys euphorbiae on leaves of Euphorbia sp., Deniquelata hypolithi from hypolith under a rock, Hysterobrevium walvisbayicola on leaves of unidentified tree, Knufia hypolithi and Knufia walvisbayicola from hypolith under a rock, Lapidomyces stipagrostidicola on leaves of Stipagrostis sp., Nothophaeotheca mirabibensis (incl. Nothophaeotheca gen. nov.) on persistent inflorescence remains of Blepharis obmitrata , Paramyrothecium salvadorae on twigs of Salvadora persica , Preussia procaviicola on dung of Procavia sp., Sordaria equicola on zebra dung, Volutella salvadorae on stems of Salvadora persica . Netherlands , Entoloma ammophilum on sandy soil, Entoloma pseudocruentatum on nutrient poor (acid) soil, Entoloma pudens on plant debris, amongst grasses. New Zealand , Amorocoelophoma neoregeliae from leaf spots of Neoregelia sp., Aquilomyces metrosideri and Septoriella callistemonis from stem discolouration and leaf spots of Metrosideros sp., Cadophora neoregeliae from leaf spots of Neoregelia sp., Flexuomyces asteliae (incl. Flexuomyces gen. nov.) and Mollisia asteliae from leaf spots of Astelia chathamica , Ophioceras freycinetiae from leaf spots of Freycinetia banksii , Phaeosphaeria caricis-sectae from leaf spots of Carex secta. Norway , Cuphophyllus flavipesoides on soil in semi-natural grassland, Entoloma coracis on soil in calcareous Pinus and Tilia forests, Entoloma cyaneolilacinum on soil semi-natural grasslands, Inocybe norvegica on gravelly soil. Pakistan , Butyriboletus parachinarensis on soil in association with Quercus baloot. Poland , Hyalodendriella bialowiezensis on debris beneath fallen bark of Norway spruce Picea abies. Russia , Bolbitius sibiricus on à moss covered rotting trunk of Populus tremula , Crepidotus wasseri on debris of Populus tremula , Entoloma isborscanum on soil on calcareous grasslands, Entoloma subcoracis on soil in subalpine grasslands, Hydropus lecythiocystis on rotted wood of Betula pendula , Meruliopsis faginea on fallen dead branches of Fagus orientalis , Metschnikowia taurica from fruits of Ziziphus jujube , Suillus praetermissus on soil, Teunia lichenophila as endophyte from Cladonia rangiferina. Slovakia , Hygrocybe fulgens on mowed grassland, Pleuroflammula pannonica from corticated branches of Quercus sp. South Africa , Acrodontium burrowsianum on leaves of unidentified Poaceae , Castanediella senegaliae on dead pods of Senegalia ataxacantha , Cladophialophora behniae on leaves of Behnia sp., Colletotrichum cliviigenum on leaves of Clivia sp., Diatrype dalbergiae on bark of Dalbergia armata , Falcocladium heteropyxidicola on leaves of Heteropyxis canescens , Lapidomyces aloidendricola as epiphyte on brown stem of Aloidendron dichotomum , Lasionectria sansevieriae and Phaeosphaeriopsis sansevieriae on leaves of Sansevieria hyacinthoides , Lylea dalbergiae on Diatrype dalbergiae on bark of Dalbergia armata , Neochaetothyrina syzygii (incl. Neochaetothyrina gen. nov.) on leaves of Syzygium chordatum , Nothophaeomoniella ekebergiae (incl. Nothophaeomoniella gen. nov.) on leaves of Ekebergia pterophylla , Paracymostachys euphorbiae (incl. Paracymostachys gen. nov.) on leaf litter of Euphorbia ingens , Paramycosphaerella pterocarpi on leaves of Pterocarpus angolensis , Paramycosphaerella syzygii on leaf litter of Syzygium chordatum , Parateichospora phoenicicola (incl. Parateichospora gen. nov.) on leaves of Phoenix reclinata , Seiridium syzygii on twigs of Syzygium chordatum , Setophoma syzygii on leaves of Syzygium sp., Starmerella xylocopis from larval feed of an Afrotropical bee Xylocopa caffra , Teratosphaeria combreti on leaf litter of Combretum kraussii , Teratosphaericola leucadendri on leaves of Leucadendron sp., Toxicocladosporium pterocarpi on pods of Pterocarpus angolensis. Spain , Cortinarius bonachei with Quercus ilex in calcareus soils, Cortinarius brunneovolvatus under Quercus ilex subsp . ballota in calcareous soil, Extremopsis radicicola (incl. Extremopsis gen. nov.) from root-associated soil in a wet heathland, Russula quintanensis on acidic soils, Tubaria vulcanica on volcanic lapilii material, Tuber zambonelliae in calcareus soil. Sweden , Elaphomyces borealis on soil under Pinus sylvestris and Betula pubescens. Tanzania , Curvularia tanzanica on inflorescence of Cyperus aromaticus. Thailand , Simplicillium niveum on Ophiocordyceps camponoti-leonardi on underside of unidentified dicotyledonous leaf. USA , Calonectria californiensis on leaves of Umbellularia californica , Exophiala spartinae from surface sterilised roots of Spartina alterniflora , Neophaeococcomyces oklahomaensis from outside wall of alcohol distillery. Vietnam , Fistulinella aurantioflava on soil. Morphological and culture characteristics are supported by DNA barcodes. Citation : Crous PW, Cowan DA, Maggs-Kölling, et al. 2021. Fungal Planet description sheets: 1182-1283. Persoonia 46: 313-528. https://doi.org/10.3767/persoonia.2021.46.11., (© 2021 Naturalis Biodiversity Center & Westerdijk Fungal Biodiversity Institute.)

Published
2021
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28. Genera of phytopathogenic fungi: GOPHY 1.

Author

Marin-Felix Y, Groenewald JZ, Cai L, Chen Q, Marincowitz S, Barnes I, Bensch K, Braun U, Camporesi E, Damm U, de Beer ZW, Dissanayake A, Edwards J, Giraldo A, Hernández-Restrepo M, Hyde KD, Jayawardena RS, Lombard L, Luangsa-Ard J, McTaggart AR, Rossman AY, Sandoval-Denis M, Shen M, Shivas RG, Tan YP, van der Linde EJ, Wingfield MJ, Wood AR, Zhang JQ, Zhang Y, and Crous PW

Abstract

Genera of Phytopathogenic Fungi (GOPHY) is introduced as a new series of publications in order to provide a stable platform for the taxonomy of phytopathogenic fungi. This first paper focuses on 21 genera of phytopathogenic fungi: Bipolaris , Boeremia , Calonectria , Ceratocystis , Cladosporium , Colletotrichum , Coniella , Curvularia , Monilinia , Neofabraea , Neofusicoccum , Pilidium , Pleiochaeta , Plenodomus , Protostegia , Pseudopyricularia , Puccinia , Saccharata , Thyrostroma , Venturia and Wilsonomyces . For each genus, a morphological description and information about its pathology, distribution, hosts and disease symptoms are provided. In addition, this information is linked to primary and secondary DNA barcodes of the presently accepted species, and relevant literature. Moreover, several novelties are introduced, i.e. new genera, species and combinations, and neo-, lecto- and epitypes designated to provide a stable taxonomy. This first paper includes one new genus, 26 new species, ten new combinations, and four typifications of older names.

Published
2017
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29. Claviceps cyperi, a new cause of severe ergotism in dairy cattle consuming maize silage and teff hay contaminated with ergotised Cyperus esculentus (nut sedge) on the Highveld of South Africa.

Author

Naudè TW, Botha CJ, Vorster JH, Roux C, Van der Linde EJ, Van der Walt SI, Rottinghaus GE, Van Jaarsveld L, and Lawrence AN

Subjects
Animal Feed, Animals, Cattle, Cattle Diseases epidemiology, Cattle Diseases pathology, Cattle Diseases physiopathology, Claviceps growth & development, Cyperus microbiology, Disease Outbreaks veterinary, Eragrostis chemistry, Eragrostis microbiology, Ergotism epidemiology, Ergotism etiology, Ergotism pathology, Female, Fever etiology, Fever pathology, Fever veterinary, Lactation drug effects, South Africa epidemiology, Zea mays chemistry, Zea mays microbiology, Cattle Diseases etiology, Claviceps pathogenicity, Ergot Alkaloids isolation & purification, Ergotism veterinary, Food Contamination analysis, Silage microbiology
Abstract

During December/January 1996/97 typical summer syndrome (hyperthermia and a 30% drop in milk yield) occurred in succession in two Holstein dairy herds (n=240 and n=150 milking cows, respectively) on the South African Highveld. These farms are situated in the midst of the prime maize and dairy farming areas of South Africa where this condition had never been diagnosed before. The individual components of the concentrate on both farms were negative for ergot alkaloids. Endophytic fungi and/or ergot infestation of teff and other grasses fed to the cows were then suspected of being involved, but neither endophytes nor ergot alkaloids could be implicated from these sources. By measuring the serum prolactin levels of groups of sheep (n=5) fed the first farm's total mixed ration (TMR) or its three individual fibre components for a period of 11 days, the source of the ergot alkaloids was identified. A statistically significant decrease in the level of this hormone occurred only in the group on maize silage (which constituted 28% on dry matter base of the TMR). The involvement of the maize silage was further chemically confirmed by the high levels of total ergot alkaloids, predominantly ergocryptine, found by LC-MS in the silage as well as in the TMR (115-975 ppb and 65-300 ppb, respectively). The ergot alkaloid content (mainly ergocryptine) of the maize silage on the second affected farm was 875 ppb. Withdrawal of contaminated silage resulted in gradual recovery of stock on both farms. Nut sedge (Cyperus esculentus and Cyperus rotundus of the family Cyperaceae) has a world-wide distribution and is a common weed in annual crops, and can be parasitized by Claviceps cyperi. Careful examination of the maize silage from both farms revealed that it was heavily contaminated with nut sedge and that it contained minute sclerotia, identified as those of Claviceps cyperi, originating from the latter. Nut sedge was abundant on both farms and it is believed that late seasonal rain had resulted in mature, heavily ergotised nut sedge being cut with the silage. Claviceps cyperi sclerotia, collected on the affected fields in the following autumn contained 3600-4000 ppm ergocryptine. That the dominant alkaloid produced by this particular fungus was indeed ergocryptine, was confirmed by negative ion chemical ionization MS/MS. In one further outbreak in another Holstein herd, teff hay contaminated with ergotised nut sedge and containing 1200 ppb alkaloids, was incriminated as the cause of the condition. This is the first report of bovine ergotism not associated with the Poaceae infected with Claviceps purpureum or endophytes but with the family Cyperaceae and this particular fungal phytopathogen.

Published
2005
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30. Pain, thermal sensation and cooling rates of hands while touching cold materials.

Author

Havenith G, van de Linde EJ, and Heus R

Subjects
Adolescent, Adult, Exercise physiology, Female, Humans, Male, Pain Measurement, Sensory Thresholds, Body Temperature Regulation physiology, Cold Temperature adverse effects, Hand physiology, Pain physiopathology, Thermosensing physiology
Abstract

Hand cooling and resulting comfort and pain were studied in 12 subjects, while touching six different materials (polyurethane foam, wood, nylon, rustproof steel, aluminium, and temperature-controlled metal) which were initially at ambient temperature. This was done for three ambient temperatures (-10 degrees, 0 degree and 10 degrees C), after pre-exposure exercise or rest, with bare hands or while wearing gloves. The observed cooling curves were analysed as Newtonian cooling curves. The observed time constants appeared to be significantly related to the materials' contact coefficients, the presence of hand protection, the preceding activity, and the interaction between contact coefficient and the presence of hand protection. These parameters also allowed a good description of the time constant (r2 = 0.8) of the related cooling curves. Thermal and pain sensation could be described in terms of the local skin temperature, ambient temperature and hand protection. Equal pain and thermal levels were associated with lower temperatures of the back of the hand than of the contact side. The slightly painful condition was associated with a skin temperature of 16 degrees C for the back and 19 degrees C for the palm of the hand. The pain level appeared to be inversely related to cooling speed. Skin freezing occurred at higher skin temperatures when touching cold objects than when exposed to cold air as a result of reduced supercooling. The regression equations determined allowed calculations to be made of safety limits for hand cooling while in contact with a wide range of materials.

Published
1992
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