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4. Shapeshifting bullvalene-linked vancomycin dimers as effective antibiotics against multidrug-resistant gram-positive bacteria

Author

Ottonello, Alessandra, primary, Wyllie, Jessica A., additional, Yahiaoui, Oussama, additional, Sun, Shoujun, additional, Koelln, Rebecca A., additional, Homer, Joshua A., additional, Johnson, Robert M., additional, Murray, Ewan, additional, Williams, Paul, additional, Bolla, Jani R., additional, Robinson, Carol V., additional, Fallon, Thomas, additional, Soares da Costa, Tatiana P., additional, and Moses, John E., additional

Published
2023
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5. A 4-cyano-3-methylisoquinoline inhibitor of Plasmodium falciparum growth targets the sodium efflux pump PfATP4

Author

Gilson, Paul R., Kumarasingha, Rasika, Thompson, Jennifer, Zhang, Xinxin, Penington, Jocelyn Sietsma, Kalhor, Robabeh, Bullen, Hayley E., Lehane, Adele M., Dans, Madeline G., de Koning-Ward, Tania F., Holien, Jessica K., Soares da Costa, Tatiana P., Hulett, Mark D., Buskes, Melissa J., Crabb, Brendan S., Kirk, Kiaran, Papenfuss, Anthony T., Cowman, Alan F., and Abbott, Belinda M.

Published
2019
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11. Structural insight into the Scribble PDZ domains interaction with the oncogenic Human T‐cell lymphotrophic virus‐1 (HTLV‐1) Tax1 PBM.

Author

Javorsky, Airah, Maddumage, Janesha C., Mackie, Emily R. R., Soares da Costa, Tatiana P., Humbert, Patrick O., and Kvansakul, Marc

Subjects
CELL polarity, ISOTHERMAL titration calorimetry, T cells, CELL migration, ONCOGENIC proteins, CELL cycle regulation
Abstract

Scribble (Scrib) is a highly conserved cell polarity regulator that harbours potent tumour suppressor activity and plays an important role in cell migration. Dysregulation of polarity is associated with poor prognosis during viral infections. Human T‐cell lymphotrophic virus‐1 (HTLV‐1) encodes for the oncogenic Tax1 protein, a modulator of the transcription of viral and human proteins that can cause cell cycle dysregulation as well as a loss of genomic integrity. Previous studies established that Scribble interacts with Tax1 via its C‐terminal PDZ‐binding motif (PBM), leading to aggregation of polarity regulators and subsequent perturbation of host cell adhesion, proliferation, and signalling. Using isothermal titration calorimetry, we now show that all four PDZ domains of Scribble bind to Tax1 PBM. We then determined crystal structures of Scribble PDZ1, PDZ2 and PDZ3 domains bound to Tax1 PBM. Our findings establish a structural basis for Tax1‐mediated subversion of Scribble‐mediated cell polarity signalling and provide the platform for mechanistic studies to examine Tax1 induced mislocalization of Scribble and the associated changes in cellular architecture and subsequent tumorigenesis. [ABSTRACT FROM AUTHOR]

Published
2023
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13. Structural characterisation of a MAPR‐related archaeal cytochrome b5M protein.

Author

Teakel, Sarah, Marama, Michealla, Aragão, David, Tsimbalyuk, Sofiya, Mackie, Emily R. R., Soares da Costa, Tatiana P., Forwood, Jade K., and Cahill, Michael A.

Subjects
PROGESTERONE receptors, PROTEIN domains, PROTEINS, PROTEIN structure, CRYSTAL structure, CYTOCHROME c
Abstract

We recently reported that the membrane‐associated progesterone receptor (MAPR) protein family (mammalian members: PGRMC1, PGRMC2, NEUFC and NENF) originated from a new class of prokaryotic cytochrome b5 (cytb5) domain proteins, called cytb5M (MAPR‐like). Relative to classical cytb5 proteins, MAPR and ctyb5M proteins shared unique sequence elements and a distinct heme‐binding orientation at an approximately 90° rotation relative to classical cytb5, as demonstrated in the archetypal crystal structure of a cytb5M protein (PDB accession number 6NZX). Here, we present the crystal structure of an archaeal cytb5M domain (Methanococcoides burtoniiWP_011499504.1, PDB:6VZ6). It exhibits similar heme binding to the 6NZX cytb5M, supporting the deduction that MAPR‐like heme orientation was inherited from the prokaryotic ancestor of the original eukaryotic MAPR gene. [ABSTRACT FROM AUTHOR]

Published
2022
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19. CCDC 2026570: Experimental Crystal Structure Determination

Author

Li, Suhua, Li, Gencheng, Gao, Bing, Pujari, Sidharam P., Chen, Xiaoyan, Kim, Hyunseok, Zhou, Feng, Klivansky, Liana M., Liu, Yi, Driss, Hafedh, Impey, Rachael E., Soares da Costa, Tatiana P., Liang, Dong Dong, Lu, Jianmei, Wu, Peng, Zuilhof, Han, Moses, John, Sharpless, Barry, Li, Suhua, Li, Gencheng, Gao, Bing, Pujari, Sidharam P., Chen, Xiaoyan, Kim, Hyunseok, Zhou, Feng, Klivansky, Liana M., Liu, Yi, Driss, Hafedh, Impey, Rachael E., Soares da Costa, Tatiana P., Liang, Dong Dong, Lu, Jianmei, Wu, Peng, Zuilhof, Han, Moses, John, and Sharpless, Barry

Abstract

DUTLAI : [1,1'-biphenyl]-4-yl (4-ethynylphenyl)sulfurofluoridimidate, Related Article: Suhua Li, Gencheng Li, Bing Gao, Sidharam P. Pujari, Xiaoyan Chen, Hyunseok Kim, Feng Zhou, Liana M. Klivansky, Yi Liu, Hafedh Driss, Dong-Dong Liang, Jianmei Lu, Peng Wu, Han Zuilhof, John Moses, K. Barry Sharpless|2021|Nature Chemistry|13|858|doi:10.1038/s41557-021-00726-x

Published
2020

25. Structural insights into BCL2 pro-survival protein interactions with the key autophagy regulator BECN1 following phosphorylation by STK4/MST1

Author

Lee, Erinna F., primary, Smith, Nicholas A., additional, Soares da Costa, Tatiana P., additional, Meftahi, Nastaran, additional, Yao, Shenggen, additional, Harris, Tiffany J., additional, Tran, Sharon, additional, Pettikiriarachchi, Anne, additional, Perugini, Matthew A., additional, Keizer, David W., additional, Evangelista, Marco, additional, Smith, Brian J., additional, and Fairlie, W. Douglas, additional

Published
2019
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27. Defining the distinct, intrinsic properties of the novel type I interferon, IFNϵ

Author

Stifter, Sebastian A, Matthews, Antony Y, Mangan, Niamh E, Fung, Ka Yee, Drew, Alexander, Tate, Michelle D, Soares da Costa, Tatiana P, Hampsey, Daniel, Mayall, Jemma, Hansbro, Phil M, Garcia Minambres, Albert, Eid, Sahar G, Mak, Johnson, Scoble, Judy, Lovrecz, George, deWeerd, Nicole A, Hertzog, Paul J, Stifter, Sebastian A, Matthews, Antony Y, Mangan, Niamh E, Fung, Ka Yee, Drew, Alexander, Tate, Michelle D, Soares da Costa, Tatiana P, Hampsey, Daniel, Mayall, Jemma, Hansbro, Phil M, Garcia Minambres, Albert, Eid, Sahar G, Mak, Johnson, Scoble, Judy, Lovrecz, George, deWeerd, Nicole A, and Hertzog, Paul J

Published
2018

28. Identification of two dihydrodipicolinate synthase isoforms from Pseudomonas aeruginosa that differ in allosteric regulation.

Author

Impey, Rachael E., Panjikar, Santosh, Hall, Cody J., Bock, Lucy J., Sutton, J. Mark, Perugini, Matthew A., and Soares da Costa, Tatiana P.

Subjects
ALLOSTERIC regulation, PSEUDOMONAS aeruginosa, BACTERIAL cell walls, NOSOCOMIAL infections, BIOSYNTHESIS, AMINO acids, DRUG resistance
Abstract

Pseudomonas aeruginosa is one of the leading causes of nosocomial infections, accounting for 10% of all hospital‐acquired infections. Current antibiotics against P. aeruginosa are becoming increasingly ineffective due to the exponential rise in drug resistance. Thus, there is an urgent need to validate and characterize novel drug targets to guide the development of new classes of antibiotics against this pathogen. One such target is the diaminopimelate (DAP) pathway, which is responsible for the biosynthesis of bacterial cell wall and protein building blocks, namely meso‐DAP and lysine. The rate‐limiting step of this pathway is catalysed by the enzyme dihydrodipicolinate synthase (DHDPS), typically encoded for in bacteria by a single dapA gene. Here, we show that P. aeruginosa encodes two functional DHDPS enzymes, PaDHDPS1 and PaDHDPS2. Although these isoforms have similar catalytic activities (kcat = 29 s−1 and 44 s−1 for PaDHDPS1 and PaDHDPS2, respectively), they are differentially allosterically regulated by lysine, with only PaDHDPS2 showing inhibition by the end product of the DAP pathway (IC50 = 130 μm). The differences in allostery are attributed to a single amino acid difference in the allosteric binding pocket at position 56. This is the first example of a bacterium that contains multiple bona fide DHDPS enzymes, which differ in allosteric regulation. We speculate that the presence of the two isoforms allows an increase in the metabolic flux through the DAP pathway when required in this clinically important pathogen. Databases: PDB ID: 6P90. [ABSTRACT FROM AUTHOR]

Published
2020
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29. The Sodium Sialic Acid Symporter From Staphylococcus aureus Has Altered Substrate Specificity

Author

North, Rachel A., primary, Wahlgren, Weixiao Y., additional, Remus, Daniela M., additional, Scalise, Mariafrancesca, additional, Kessans, Sarah A., additional, Dunevall, Elin, additional, Claesson, Elin, additional, Soares da Costa, Tatiana P., additional, Perugini, Matthew A., additional, Ramaswamy, S., additional, Allison, Jane R., additional, Indiveri, Cesare, additional, Friemann, Rosmarie, additional, and Dobson, Renwick C. J., additional

Published
2018
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31. Defining the distinct, intrinsic properties of the novel type I interferon, IFNϵ

Author

Stifter, Sebastian A., primary, Matthews, Antony Y., additional, Mangan, Niamh E., additional, Fung, Ka Yee, additional, Drew, Alexander, additional, Tate, Michelle D., additional, Soares da Costa, Tatiana P., additional, Hampsey, Daniel, additional, Mayall, Jemma, additional, Hansbro, Phil M., additional, Garcia Minambres, Albert, additional, Eid, Sahar G., additional, Mak, Johnson, additional, Scoble, Judy, additional, Lovrecz, George, additional, deWeerd, Nicole A., additional, and Hertzog, Paul J., additional

Published
2018
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35. Structural Determinants Defining the Allosteric Inhibition of an Essential Antibiotic Target

Author

Soares da Costa, Tatiana P., primary, Desbois, Sebastien, additional, Dogovski, Con, additional, Gorman, Michael A., additional, Ketaren, Natalia E., additional, Paxman, Jason J., additional, Siddiqui, Tanzeela, additional, Zammit, Leanne M., additional, Abbott, Belinda M., additional, Robins-Browne, Roy M., additional, Parker, Michael W., additional, Jameson, Geoffrey B., additional, Hall, Nathan E., additional, Panjikar, Santosh, additional, and Perugini, Matthew A., additional

Published
2016
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37. Improved Synthesis of Biotinol-5′-AMP: Implications for Antibacterial Discovery

Author

Tieu, William, primary, Polyak, Steven W., additional, Paparella, Ashleigh S., additional, Yap, Min Y., additional, Soares da Costa, Tatiana P., additional, Ng, Belinda, additional, Wang, Geqing, additional, Lumb, Richard, additional, Bell, Jan M., additional, Turnidge, John D., additional, Wilce, Matthew C. J., additional, Booker, Grant W., additional, and Abell, Andrew D., additional

Published
2014
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40. Selective inhibition of Biotin Protein Ligase from Staphylococcus aureus

Author

Soares da Costa, Tatiana P., primary, Tieu, William, additional, Yap, Min Y., additional, Pendini, Nicole R., additional, Polyak, Steven W., additional, Sejer Pedersen, Daniel, additional, Morona, Renato, additional, Turnidge, John D., additional, Wallace, John C., additional, Wilce, Matthew C.J., additional, Booker, Grant W., additional, and Abell, Andrew D., additional

Published
2012
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42. Improved synthesis of biotinol-5'-AMP: implications for antibacterial discovery

Author

Jan M. Bell, Richard S Lumb, Min Y. Yap, Andrew D. Abell, John D. Turnidge, William Tieu, Belinda Ng, Matthew C.J. Wilce, Tatiana P. Soares da Costa, Geqing Wang, Ashleigh S. Paparella, Steven W. Polyak, Grant W. Booker, Tieu, William, Polyak, Steven W, Paparella, Ashleigh S, Yap, Min Y, Soares Da Costa, Tatiana P, Ng, Belinda, Wang, Geqing, Lumb, Richard, Bell, Jan M, Turnidge, John D, Wilce, Matthew CJ, Booker, Grant W, and Abell, Andrew D

Subjects
biology, medicine.drug_class, drug design, enzyme inhibitors, Organic Chemistry, Antibiotics, biology.organism_classification, medicine.disease_cause, Biochemistry, Chemical synthesis, Microbiology, Mycobacterium tuberculosis, chemistry.chemical_compound, Biotin, chemistry, Staphylococcus aureus, Drug Discovery, medicine, biotin protein ligase, Cytotoxicity, Antibacterial activity, Bacteria, chemical synthesis
Abstract

An improved synthesis of biotinol-5′-AMP, an acyl-AMP mimic of the natural reaction intermediate of biotin protein ligase (BPL), is reported. This compound was shown to be a pan inhibitor of BPLs from a series of clinically important bacteria, particularly Staphylococcus aureus and Mycobacterium tuberculosis, and kinetic analysis revealed it to be competitive against the substrate biotin. Biotinol-5′-AMP also exhibits antibacterial activity against a panel of clinical isolates of S. aureus and M. tuberculosis with MIC values of 1-8 and 0.5-2.5 μg/mL, respectively, while being devoid of cytotoxicity to human HepG2 cells. Refereed/Peer-reviewed

Published
2015

43. Optimising in situ click chemistry: the screening and identification of biotin protein ligase inhibitors

Author

Steven W. Polyak, Kelly L. Keeling, William Tieu, Matthew C.J. Wilce, Tatiana P. Soares da Costa, Min Yin Yap, Grant W. Booker, John C. Wallace, Andrew D. Abell, Tieu, William, Soares Da Costa, Tatiana P, Yap, Min Y, Keeling, Kelly L, Wilce, Matthew CJ, Wallace, John C, Booker, Grant W, Polyak, Steven W, and Abell, Andrew D

Subjects
chemistry.chemical_classification, DNA ligase, Staphylococcus aureus biotin protein ligase, Triazole, Alkyne, General Chemistry, Ligand (biochemistry), chemistry.chemical_compound, Enzyme, chemistry, Biochemistry, Biotin, triazole-based inhibitor, Click chemistry, ligand optimisation, Azide
Abstract

A 'leaky mutant' (SaBPL-R122G) of Staphylococcus aureus biotin protein ligase (SaBPL) is used to enhance the turnover rate for the reaction of biotin alkyne with an azide to give a triazole. This allows the enzyme to select the optimum triazole-based inhibitor using a library of such azides in a single experiment with greatly improved efficiency and sensitivity of detection, difficulties that can restrict the general utility of a multi-component in situ click approach to ligand optimisation. Refereed/Peer-reviewed

Published
2013

44. Biotin analogues with antibacterial activity are potent inhibitors of biotin protein ligase

Author

John C. Wallace, Andrew D. Abell, Grant W. Booker, Min Y. Yap, Jan M. Bell, Ondrej Zvarec, Steven W. Polyak, Matthew C.J. Wilce, William Tieu, Tatiana P. Soares da Costa, John D. Turnidge, Soares Da Costa, Tatiana P, Tieu, William, Yap, Min Y, Zvarec, Ondrej, Bell, Jan M, Turnidge, John D, Wallace, John C, Booker, Grant W, Wilce, Matthew C J, Abell, Andrew D, Polyak, Steven W, and School of Materials Science & Engineering

Subjects
chemistry.chemical_classification, DNA ligase, biology, Organic Chemistry, enzyme inhibitor, medicine.disease_cause, Biochemistry, chemistry.chemical_compound, enzyme, Enzyme, Biotin, chemistry, Enzyme inhibitor, Staphylococcus aureus, antibiotic, medicinal chemistry, Drug Discovery, biology.protein, medicine, biotin protein ligase, Mode of action, Antibacterial activity, Escherichia coli
Abstract

There is a desperate need to develop new antibiotic agents to combat the rise of drug-resistant bacteria, such as clinically important Staphylococcus aureus. The essential multifunctional enzyme, biotin protein ligase (BPL), is one potential drug target for new antibiotics. We report the synthesis and characterization of a series of biotin analogues with activity against BPLs from S. aureus, Escherichia coli, and Homo sapiens. Two potent inhibitors with K i < 100 nM were identified with antibacterial activity against a panel of clinical isolates of S. aureus (MIC 2-16 μg/mL). Compounds with high ligand efficiency and >20-fold selectivity between the isozymes were identified and characterized. The antibacterial mode of action was shown to be via inhibition of BPL. The bimolecular interactions between the BPL and the inhibitors were defined by surface plasmon resonance studies and X-ray crystallography. These findings pave the way for second-generation inhibitors and antibiotics with greater potency and selectivity. © 2012 American Chemical Society. Refereed/Peer-reviewed

Published
2012

45. Selective inhibition of biotin protein ligase from Staphylococcus aureus

Author

Grant W. Booker, Matthew C.J. Wilce, Min Y. Yap, Steven W. Polyak, Nicole R. Pendini, Andrew D. Abell, Renato Morona, Daniel Sejer Pedersen, William Tieu, Tatiana P. Soares da Costa, John D. Turnidge, John C. Wallace, Soares Da Costa, Tatiana P, Tieu, William, Yap, Min Y, Pendini, Nicole R, Polyak, Steven W, Pedersen, Daniel Sejer, Morona, Renato, Turnidge, John D, Wallace, John C, Wilce, Matthew C J, Booker, Grant W, and Abell, Andrew D

Subjects
Staphylococcus aureus, enzyme inhibitors, Biotin, Plasma protein binding, Drug resistance, Biology, Crystallography, X-Ray, medicine.disease_cause, Biochemistry, antibiotics, Cell Line, Microbiology, Ligases, chemistry.chemical_compound, Antibiotic resistance, Bacterial Proteins, biotin, medicinal chemistry, Drug Resistance, Bacterial, medicine, Humans, biotin protein ligase, Enzyme Inhibitors, Molecular Biology, x-ray crystallography, chemistry.chemical_classification, DNA ligase, Cell Biology, Triazoles, Enzyme, chemistry, Enzymology, Click Chemistry, Pharmacophore, Protein Binding
Abstract

There is a well documented need to replenish the antibiotic pipeline with new agents to combat the rise of drug resistant bacteria. One strategy to combat resistance is to discover new chemical classes immune to current resistance mechanisms that inhibit essential metabolic enzymes. Many of the obvious drug targets that have no homologous isozyme in the human host have now been investigated. Bacterial drug targets that have a closely related human homologue represent a new frontier in antibiotic discovery. However, to avoid potential toxicity to the host, these inhibitors must have very high selectivity for the bacterial enzyme over the human homolog. We have demonstrated that the essential enzyme biotin protein ligase (BPL) from the clinically important pathogen Staphylococcus aureus could be selectively inhibited. Linking biotin to adenosine via a 1,2,3 triazole yielded the first BPL inhibitor selective for S. aureus BPL over the human equivalent. The synthesis of new biotin 1,2,3- triazole analogues using click chemistry yielded our most potent structure (Ki 90 nM) with a >1100-fold selectivity for the S. aureus BPL over the human homologue. X-ray crystallography confirmed the mechanism of inhibitor binding. Importantly, the inhibitor showed cytotoxicity against S. aureus but not cultured mammalian cells. The biotin 1,2,3-triazole provides a novel pharmacophore for future medicinal chemistry programs to develop this new antibiotic class. Refereed/Peer-reviewed

Published
2012

46. Structural characterisation of a MAPR-related archaeal cytochrome b 5M protein.

Author

Teakel S, Marama M, Aragão D, Tsimbalyuk S, Mackie ERR, Soares da Costa TP, Forwood JK, and Cahill MA

Subjects
Animals, Archaea genetics, Archaea metabolism, Cytochromes b5 genetics, Heme metabolism, Mammals, Protein Binding, Cytochromes b genetics, Cytochromes b metabolism, Receptors, Progesterone genetics
Abstract

We recently reported that the membrane-associated progesterone receptor (MAPR) protein family (mammalian members: PGRMC1, PGRMC2, NEUFC and NENF) originated from a new class of prokaryotic cytochrome b 5 (cytb 5 ) domain proteins, called cytb 5M (MAPR-like). Relative to classical cytb 5 proteins, MAPR and ctyb 5M proteins shared unique sequence elements and a distinct heme-binding orientation at an approximately 90° rotation relative to classical cytb 5 , as demonstrated in the archetypal crystal structure of a cytb 5M protein (PDB accession number 6NZX). Here, we present the crystal structure of an archaeal cytb 5M domain (Methanococcoides burtonii WP&#95;011499504.1, PDB:6VZ6). It exhibits similar heme binding to the 6NZX cytb 5M , supporting the deduction that MAPR-like heme orientation was inherited from the prokaryotic ancestor of the original eukaryotic MAPR gene., (© 2022 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.)

Published
2022
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