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38 results on '"Moncrieffe, Martin C."'

7. The dominantly expressed class II molecule from a resistant MHC haplotype presents only a few Marek’s disease virus peptides by using an unprecedented binding motif

Author

Halabi, Samer, primary, Ghosh, Michael, additional, Stevanović, Stefan, additional, Rammensee, Hans-Georg, additional, Bertzbach, Luca D., additional, Kaufer, Benedikt B., additional, Moncrieffe, Martin C., additional, Kaspers, Bernd, additional, Härtle, Sonja, additional, and Kaufman, Jim, additional

Published
2021
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8. Differential host response to a herpesvirus: Marek’s disease virus peptides on chicken MHC class II molecules are derived from only a few genes and illustrate a new mode of peptide binding

Author

Halabi, Samer, primary, Ghosh, Michael, additional, Stevanović, Stefan, additional, Rammensee, Hans-Georg, additional, Bertzbach, Luca D., additional, Kaufer, Benedikt B., additional, Moncrieffe, Martin C., additional, Kaspers, Bernd, additional, Härtle, Sonja, additional, and Kaufman, Jim, additional

Published
2020
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16. Quaternary structure and catalytic activity of the Escherichia coli ribonuclease E amino-terminal catalytic domain

Author

Callaghan, Anastasia J., Grossmann, J. Gunter, Redko, Yulia U., Ilag, Leopold L., Moncrieffe, Martin C., Symmons, Martyn F., Robinson, Carol V., McDowall, Kenneth J., and Luisi, Ben F.

Subjects
Binding proteins -- Analysis, Catalysis -- Analysis, Ribonuclease -- Research, Structure-activity relationships (Biochemistry) -- Analysis, Biological sciences, Chemistry
Abstract

The processing activity of the endoribonuclease, RNase E, is mediated by a conserved catalytic domain, which is a homotetramer. Results show that the tetramer binds up to four molecules of specific RNA substrate analogue and that the tetramer possesss D(sub)2 dihedral symmetry. Data point out that the S1-RNA binding domains of RNase E lies on the periphery of the tetramer.

Published
2003

17. Structural dependencies of (super h3)J(sub NC') scalar coupling in protein H-bond chains

Author

Juranic, Nenad, Moncrieffe, Martin C., Likic, Vladimir A., Prendergast, Franklyn G., and Macura, Slobodan

Subjects
Proteins -- Research, Electron configuration -- Research, Hydrogen bonding -- Observations, Chemistry
Abstract

The H-bond ((super h3)J(sub NC') and peptide bond scalar couplings establish connectivity of the electronic structure in the H-bond chains of proteins. The electronic structure of the H-bond chains can affect (super h3)J(sub NC') in a manner that is independent of the local H-bond geometry.

Published
2002

31. Optical spectroscopic characterization of single tryptophan mutants of chicken skeletal troponin C: evidence of interdomain interaction

Author

Moncrieffe, Martin C., Venyaminov, Sergei Yu., Miller, Todd E., Guzman, Georgiana, Potter, James D., and Prendergast, Franklyn G.

Subjects
Calcium-binding proteins -- Research, Carrier proteins -- Research, Chickens -- Usage, Tryptophan -- Research, Biological sciences, Chemistry
Abstract

An examination of the effects of metal ion binding on the optical spectroscopic characteristics and temperature stability of two single tryptophan mutants of chicken skeletal troponin C (TnC) has been conducted. Temperature stability measurements indicate that events that occur in the N-terminal domain have a corresponding effect in the C-terminal domain's stability. These information, coupled with the titration results, indicate an interaction between the TnC's N- and C-terminal domains.

Published
1999

35. Structural Dependencies of [sup h3] J[sub NC′] Scalar Coupling in Protein H-Bond Chains.

Author

Juranić, Nenad, Moncrieffe, Martin C., Likić, Vladimir A., Prendergast, Franklyn G., and Macura, Slobodan

Subjects
*HYDROGEN bonding, *PROTEINS
Abstract

The H-bond ([sup h3]J[sub NC']) and peptide bond (¹J[sub NC']) scalar couplings establish connectivity of the electronic structure in the H-bond chains of proteins. The correlated changes of [sup h3]J[sub NC'] and ¹J[sub NC'] couplings extend over several peptide groups in the chains. Consequently, the electronic structure of the H-bond chains can affect [sup h3]J[sub NC'] in a manner that is independent of the local H-bond geometry. By taking this into account, and by using a more complete set of H-bond geometry parameters, we have predicted [sup h3]J[sub NC'] couplings in the H-bond chains with deviations commensurate to the standard deviations of the experimentally determined values. We have created a comprehensive database of [sup h3]J[sub NC'] and ¹J[sub NC'] couplings by measuring the coupling constants in ubiquitin (αβ-fold) intestinal fatty acid binding protein (β-barrel) and carp panralbumin (α-helical). [ABSTRACT FROM AUTHOR]

Published
2002
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36. The dominantly expressed class II molecule from a resistant MHC haplotype presents only a few Marek's disease virus peptides by using an unprecedented binding motif

Author

Halabi, Samer, Ghosh, Michael, Stevanović, Stefan, Rammensee, Hans-Georg, Bertzbach, Luca D, Kaufer, Benedikt B, Moncrieffe, Martin C, Kaspers, Bernd, Härtle, Sonja, and Kaufman, Jim

Subjects
Models, Molecular, Antigen Presentation, B-Lymphocytes, Immunodominant Epitopes, Histocompatibility Antigens Class II, 3. Good health, Viral Proteins, Bursa of Fabricius, Haplotypes, Marek Disease, Animals, Peptides, Chickens, Herpesvirus 2, Gallid, Cells, Cultured, Poultry Diseases, Disease Resistance
Abstract

Funder: Deutschen Konsortium für Translationale Krebsforschung; funder-id: http://dx.doi.org/10.13039/501100012353, Funder: Natural and Medical Sciences Institute (D), Viral diseases pose major threats to humans and other animals, including the billions of chickens that are an important food source as well as a public health concern due to zoonotic pathogens. Unlike humans and other typical mammals, the major histocompatibility complex (MHC) of chickens can confer decisive resistance or susceptibility to many viral diseases. An iconic example is Marek's disease, caused by an oncogenic herpesvirus with over 100 genes. Classical MHC class I and class II molecules present antigenic peptides to T lymphocytes, and it has been hard to understand how such MHC molecules could be involved in susceptibility to Marek's disease, given the potential number of peptides from over 100 genes. We used a new in vitro infection system and immunopeptidomics to determine peptide motifs for the 2 class II molecules expressed by the MHC haplotype B2, which is known to confer resistance to Marek's disease. Surprisingly, we found that the vast majority of viral peptide epitopes presented by chicken class II molecules arise from only 4 viral genes, nearly all having the peptide motif for BL2*02, the dominantly expressed class II molecule in chickens. We expressed BL2*02 linked to several Marek's disease virus (MDV) peptides and determined one X-ray crystal structure, showing how a single small amino acid in the binding site causes a crinkle in the peptide, leading to a core binding peptide of 10 amino acids, compared to the 9 amino acids in all other reported class II molecules. The limited number of potential T cell epitopes from such a complex virus can explain the differential MHC-determined resistance to MDV, but raises questions of mechanism and opportunities for vaccine targets in this important food species, as well as providing a basis for understanding class II molecules in other species including humans.

37. The dominantly expressed class II molecule from a resistant MHC haplotype presents only a few Marek’s disease virus peptides by using an unprecedented binding motif

Author

Halabi, Samer, Ghosh, Michael, Stevanović, Stefan, Rammensee, Hans-Georg, Bertzbach, Luca D., Kaufer, Benedikt B., Moncrieffe, Martin C., Kaspers, Bernd, Härtle, Sonja, and Kaufman, Jim

Subjects
B cells, 600 Technik, Medizin, angewandte Wissenschaften::630 Landwirtschaft::630 Landwirtschaft und verwandte Bereiche, Major histocompatibility complex, Chickens, 3. Good health
Abstract

Viral diseases pose major threats to humans and other animals, including the billions of chickens that are an important food source as well as a public health concern due to zoonotic pathogens. Unlike humans and other typical mammals, the major histocompatibility complex (MHC) of chickens can confer decisive resistance or susceptibility to many viral diseases. An iconic example is Marek’s disease, caused by an oncogenic herpesvirus with over 100 genes. Classical MHC class I and class II molecules present antigenic peptides to T lymphocytes, and it has been hard to understand how such MHC molecules could be involved in susceptibility to Marek’s disease, given the potential number of peptides from over 100 genes. We used a new in vitro infection system and immunopeptidomics to determine peptide motifs for the 2 class II molecules expressed by the MHC haplotype B2, which is known to confer resistance to Marek’s disease. Surprisingly, we found that the vast majority of viral peptide epitopes presented by chicken class II molecules arise from only 4 viral genes, nearly all having the peptide motif for BL2*02, the dominantly expressed class II molecule in chickens. We expressed BL2*02 linked to several Marek’s disease virus (MDV) peptides and determined one X-ray crystal structure, showing how a single small amino acid in the binding site causes a crinkle in the peptide, leading to a core binding peptide of 10 amino acids, compared to the 9 amino acids in all other reported class II molecules. The limited number of potential T cell epitopes from such a complex virus can explain the differential MHC-determined resistance to MDV, but raises questions of mechanism and opportunities for vaccine targets in this important food species, as well as providing a basis for understanding class II molecules in other species including humans.

38. Characterization of Symmetric Complexes of Nerve Growth Factor and the Ectodomain of the Pan-neurotrophin Receptor, p75NTR.

Author

Aurikko, Jukka P., Ruotolo, Brandon T., Grossmann, J. Günter, Moncrieffe, Martin C., Stephens, Elaine, Leppänen, Veli-Matti, Robinson, Carol V., Saarma, Mart, Bradshaw, Ralph A., and Blundell, Tom L.

Subjects
*NERVE growth factor, *CELLS, *NEURONS, *PROTEINS, *TRICHOPLUSIA, *MASS spectrometry, *X-ray scattering
Abstract

Nerve growth factor (NGF) is the ligand for two unrelated cellular receptors, TrkA and p75NTR, and acts as a mediator in the development and maintenance of the mammalian nervous system. Signaling through TrkA kinase domains promotes neuronal survival, whereas activation of the p75NTR ‘death domains’ induces apoptosis under correct physiological conditions. However, co-expression of these receptors leads to enhanced neuronal survival upon NGF stimulation, possibly through a ternary p75NTR·NGF·TrkA complex. We have expressed human p75NTR ligand binding domain as a secreted glycosylated protein in Trichoplusia ni cells. Following assembly and purification of soluble p75NTR·NGF complexes, mass spectrometry, analytical ultracentrifugation, and solution x-ray scattering measurements are indicative of 2:2 stoichiometry, which implies a symmetric complex. Molecular models of the 2:2 p75NTR·NGF complex based on these data are not consistent with the further assembly of either symmetric (2:2:2) or asymmetric (2:2:1) ternary p75NTR·NGF·TrkA complexes. [ABSTRACT FROM AUTHOR]

Published
2005
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