Peter Colman

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Peter Colman
AC FRS FAA FTSE
Professor Peter Colman FRS.jpg
Peter Colman at the Royal Society admissions day in 2014
Born
Peter Malcolm Colman

(1944-04-03) 3 April 1944 (age 80) [1]
Adelaide [2]
Alma mater
Known for
Awards
Scientific career
Fields
Institutions
Thesis The physical structure of two parabanic acid complexes and an investigation of short intermolecular carbon-oxygen contacts  (1969)
Doctoral advisor Harry Medlin [6]
Website www.wehi.edu.au/people/peter-colman

Peter Malcolm Colman (born 1944) [1] is the head of the structural biology division at the Walter and Eliza Hall Institute of Medical Research in Melbourne, Australia. [7]

Contents

Education

Colman was educated at the University of Adelaide, where he received a Bachelor of Science degree in physics in 1966 [1] and a PhD in 1969 for research on the chemical structure of parabanic acid complexes supervised by Harry Medlin. [6]

Research and career

Colman's research interests are in structural biology, [8] [9] [10] especially of human B-cell lymphoma 2 (BCL-2). [11] [12] [13] [14] Colman determined the three-dimensional structure of the influenza virus neuraminidase and, in one of the earliest cases of structure-based drug design, discovered zanamivir, the first-in-class neuraminidase inhibitor for influenza. [15] His subsequent structural studies on resistance to this drug class suggested how to design drugs against moving targets. [15] His discoveries underpin drug stockpiling for pandemic preparedness. [15] He has made seminal contributions to structural studies of antibodies and antibody-antigen complexes. [15] Recent[ when? ] work on apoptosis solves the long-standing problem of how pro-apoptotic Bax changes conformation to dimerise and then oligomerise and permeabilise the mitochondrial membrane, an essential step in the intrinsic cell-death pathway. [15]

His work has been published in leading peer reviewed scientific journals including Nature , [8] [16] [17] [18] [19] [20] the Journal of Molecular Biology , [21] and Nature Reviews Molecular Cell Biology . [22]

Awards and honours

Peter Colman, showing his flu protein (neuraminidase) model to Frank Macfarlane Burnet . CSIRO ScienceImage 2005 Peter Colman and Frank Macfarlane Burnet.jpg
Peter Colman, showing his flu protein (neuraminidase) model to Frank Macfarlane Burnet .

In the Queen's 2017 Birthday Honours Colman was appointed a Companion of the Order of Australia (AC), Australia's highest civilian honour, "for eminent service to medical research, particularly in the fields of structural biology and medicinal chemistry, as a leader in the commercial translation of scientific discoveries, to professional organisations, and as a mentor of young scientists". [23]

Colman was elected a Fellow of the Royal Society (FRS) in 2014. [15] In 2001 he was awarded a Centenary Medal "For service to Australian society and science in structural biology". [5] Colman was also elected a Fellow of the Australian Academy of Science in 1989 and a Fellow of the Australian Academy of Technological Sciences and Engineering in 1997. [1] He was awarded the Lemberg Medal in 1988 [24] and the Macfarlane Burnet Medal and Lecture in 1995. [25]

Related Research Articles

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Antiviral drugs are a class of medication used for treating viral infections. Most antivirals target specific viruses, while a broad-spectrum antiviral is effective against a wide range of viruses. Antiviral drugs are a class of antimicrobials, a larger group which also includes antibiotic, antifungal and antiparasitic drugs, or antiviral drugs based on monoclonal antibodies. Most antivirals are considered relatively harmless to the host, and therefore can be used to treat infections. They should be distinguished from virucides, which are not medication but deactivate or destroy virus particles, either inside or outside the body. Natural virucides are produced by some plants such as eucalyptus and Australian tea trees.

<span class="mw-page-title-main">Antigenic shift</span> Process by which two or more different strains of a virus combine to form a new subtype

Antigenic shift is the process by which two or more different strains of a virus, or strains of two or more different viruses, combine to form a new subtype having a mixture of the surface antigens of the two or more original strains. The term is often applied specifically to influenza, as that is the best-known example, but the process is also known to occur with other viruses, such as visna virus in sheep. Antigenic shift is a specific case of reassortment or viral shift that confers a phenotypic change.

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Antigenic drift is a kind of genetic variation in viruses, arising from the accumulation of mutations in the virus genes that code for virus-surface proteins that host antibodies recognize. This results in a new strain of virus particles that is not effectively inhibited by the antibodies that prevented infection by previous strains. This makes it easier for the changed virus to spread throughout a partially immune population. Antigenic drift occurs in both influenza A and influenza B viruses.

<span class="mw-page-title-main">Zanamivir</span> Influenza medication

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<span class="mw-page-title-main">Neuraminidase</span> Glycoside hydrolase enzymes that cleave the glycosidic linkages of neuraminic acids

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Neuraminidase inhibitors (NAIs) are a class of drugs which block the neuraminidase enzyme. They are a commonly used antiviral drug type against influenza. Viral neuraminidases are essential for influenza reproduction, facilitating viral budding from the host cell. Oseltamivir (Tamiflu), zanamivir (Relenza), laninamivir (Inavir), and peramivir belong to this class. Unlike the M2 inhibitors, which work only against the influenza A virus, NAIs act against both influenza A and influenza B.

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<span class="mw-page-title-main">Hemagglutinin-neuraminidase</span>

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Neuraminidase inhibitors inhibit enzymatic activity of the enzyme neuraminidase (sialidase). These type of inhibitors have been introduced as anti-influenza drugs as they prevent the virus from exiting infected cells and thus stop further spreading of the virus. Neuraminidase inhibitors for human neuraminidase (hNEU) have the potential to be useful drugs as the enzyme plays a role in several signaling pathways in cells and is implicated in diseases such as diabetes and cancer.

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References

  1. 1 2 3 4 Anon (2014). "Colman, Dr Peter Malcolm" . Who's Who (online Oxford University Press  ed.). A & C Black. doi:10.1093/ww/9780199540884.013.U23546.(Subscription or UK public library membership required.)
  2. 1 2 Peter Malcolm Colman, CSIROpedia, Commonwealth Scientific and Industrial Research Organisation
  3. ↑ Colman, P. M. (1994). "Influenza virus neuraminidase: Structure, antibodies, and inhibitors". Protein Science. 3 (10): 1687–96. doi:10.1002/pro.5560031007. PMC   2142611 . PMID   7849585.
  4. ↑ "Professor Peter Colman". aips.net. Australian Institute of Policy and Science.
  5. 1 2 COLMAN, Peter Malcolm - Centenary Medal, 1 January 2001, It's an Honour.
  6. 1 2 Colman, Peter Malcolm (1969). The physical structure of two parabanic acid complexes and an investigation of short intermolecular carbon-oxygen contacts. trove.nla.gov.au (PhD thesis). University of Adelaide. hdl:2440/19998. OCLC   222734513. Lock-green.svg
  7. ↑ Peter Colman publications indexed by the Scopus bibliographic database. (subscription required)
  8. 1 2 Huber, R.; Deisenhofer, J.; Colman, P. M.; Matsushima, M.; Palm, W. (1976). "Crystallographic structure studies of an IgG molecule and an Fc fragment". Nature. 264 (5585): 415–20. Bibcode:1976Natur.264..415H. doi:10.1038/264415a0. PMID   1004567. S2CID   4193312.
  9. ↑ Colman, P. M. (1994). "Effects of amino acid sequence changes on antibody-antigen interactions". Research in Immunology. 145 (1): 33–6. doi:10.1016/S0923-2494(94)80039-1. PMID   7516563.
  10. ↑ Type 1 Diabetes Research Update – with Professor Peter Colman on YouTube
  11. ↑ Lessene, G.; Czabotar, P. E.; Colman, P. M. (2008). "BCL-2 family antagonists for cancer therapy". Nature Reviews Drug Discovery. 7 (12): 989–1000. doi:10.1038/nrd2658. PMID   19043450. S2CID   7385925.
  12. ↑ Brady, R. M.; Vom, A.; Roy, M. J.; Toovey, N.; Smith, B. J.; Moss, R. M.; Hatzis, E.; Huang, D. C. S.; Parisot, J. P.; Yang, H.; Street, I. P.; Colman, P. M.; Czabotar, P. E.; Baell, J. B.; Lessene, G. (2014). "De-Novo Designed Library of Benzoylureas as Inhibitors of BCL-XL: Synthesis, Structural and Biochemical Characterization". Journal of Medicinal Chemistry. 57 (4): 1323–43. doi:10.1021/jm401948b. PMID   24456288.
  13. ↑ Koehler, M. F. T.; Bergeron, P.; Choo, E. F.; Lau, K.; Ndubaku, C.; Dudley, D.; Gibbons, P.; Sleebs, B. E.; Rye, C. S.; Nikolakopoulos, G.; Bui, C.; Kulasegaram, S.; Kersten, W. J. A.; Smith, B. J.; Czabotar, P. E.; Colman, P. M.; Huang, D. C. S.; Baell, J. B.; Watson, K. G.; Hasvold, L.; Tao, Z. F.; Wang, L.; Souers, A. J.; Elmore, S. W.; Flygare, J. A.; Fairbrother, W. J.; Lessene, G. (2014). "Structure-Guided Rescaffolding of Selective Antagonists of BCL-XL". ACS Medicinal Chemistry Letters. 5 (6): 662–7. doi:10.1021/ml500030p. PMC   4060937 . PMID   24944740.
  14. ↑ Chen, L.; Willis, S. N.; Wei, A.; Smith, B. J.; Fletcher, J. I.; Hinds, M. G.; Colman, P. M.; Day, C. L.; Adams, J. M.; Huang, D. C. S. (2005). "Differential Targeting of Prosurvival Bcl-2 Proteins by Their BH3-Only Ligands Allows Complementary Apoptotic Function". Molecular Cell. 17 (3): 393–403. doi: 10.1016/j.molcel.2004.12.030 . PMID   15694340.
  15. 1 2 3 4 5 6 Anon (2014). "Professor Peter Colman FRS". royalsociety.org. London: Royal Society. Archived from the original on 5 May 2015. One or more of the preceding sentences incorporates text from the royalsociety.org website where:
    “All text published under the heading 'Biography' on Fellow profile pages is available under Creative Commons Attribution 4.0 International License.” --Royal Society Terms, conditions and policies at the Wayback Machine (archived 2016-11-11)
  16. ↑ von Itzstein, M.; Wu, W. Y.; Kok, G. B.; Pegg, M. S.; Dyason, J. C.; Jin, B.; Phan, T. V.; Smythe, M. L.; White, H. F.; Oliver, S. W.; Colman, P. M.; Varghese, J. N.; Ryan, D. M.; Woods, J. M.; Bethell, R. C.; Hotham, V. J.; Cameron, J. M.; Penn, C. R. (1993). "Rational design of potent sialidase-based inhibitors of influenza virus replication". Nature. 363 (6428): 418–23. Bibcode:1993Natur.363..418V. doi:10.1038/363418a0. PMID   8502295. S2CID   4359333.
  17. ↑ Chothia, C.; Lesk, A. M.; Tramontano, A.; Levitt, M.; Smith-Gill, S. J.; Air, G.; Sheriff, S.; Padlan, E. A.; Davies, D.; Tulip, W. R.; Colman, P. M.; Spinelli, S.; Alzari, P. M.; Poljak, R. J. (1989). "Conformations of immunoglobulin hypervariable regions". Nature. 342 (6252): 877–883. Bibcode:1989Natur.342..877C. doi:10.1038/342877a0. PMID   2687698. S2CID   4241051.
  18. ↑ Varghese, J. N.; Laver, W. G.; Colman, P. M. (1983). "Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 Å resolution". Nature. 303 (5912): 35–40. Bibcode:1983Natur.303...35V. doi:10.1038/303035a0. PMID   6843658. S2CID   4363648.
  19. ↑ Colman, P. M.; Laver, W. G.; Varghese, J. N.; Baker, A. T.; Tulloch, P. A.; Air, G. M.; Webster, R. G. (1987). "Three-dimensional structure of a complex of antibody with influenza virus neuraminidase". Nature. 326 (6111): 358–63. Bibcode:1987Natur.326..358C. doi:10.1038/326358a0. PMID   2436051. S2CID   4239913.
  20. ↑ Colman, P. M.; Varghese, J. N.; Laver, W. G. (1983). "Structure of the catalytic and antigenic sites in influenza virus neuraminidase". Nature. 303 (5912): 41–4. Bibcode:1983Natur.303...41C. doi:10.1038/303041a0. PMID   6188957. S2CID   4325977.
  21. ↑ Lawrence, M. C.; Colman, P. M. (1993). "Shape Complementarity at Protein/Protein Interfaces". Journal of Molecular Biology. 234 (4): 946–50. doi:10.1006/jmbi.1993.1648. PMID   8263940.
  22. ↑ Colman, P. M.; Lawrence, M. C. (2003). "The structural biology of type I viral membrane fusion". Nature Reviews Molecular Cell Biology. 4 (4): 309–19. doi:10.1038/nrm1076. PMID   12671653. S2CID   31703688.
  23. ↑ Companion (AC) in the General Division of the Order of Australia Archived 22 March 2018 at the Wayback Machine , Media Notes, Queen's Birthday 2017, www.gg.gov.au
  24. ↑ "Lemberg Medal Winners". Australian Society for Biochemistry and Molecular Biology. Retrieved 31 January 2024.
  25. ↑ "Macfarlane Burnet Medal and Lecture". Australian Academy of Science. Retrieved 22 February 2017.

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