Peter Colman

Last updated

Peter Colman

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 79) [1]
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 AC FRS FAA FTSE (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 Macfarlane Burnet Medal and Lecture in 1995. [24]

Related Research Articles

<span class="mw-page-title-main">Antiviral drug</span> Medication used to treat a viral infection

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 one 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.

<span class="mw-page-title-main">Hemagglutinin (influenza)</span> Hemagglutinin of influenza virus

Influenza hemagglutinin (HA) or haemagglutinin[p] is a homotrimeric glycoprotein found on the surface of influenza viruses and is integral to its infectivity.

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

Zanamivir is a medication used to treat and prevent influenza caused by influenza A and influenza B viruses. It is a neuraminidase inhibitor and was developed by the Australian biotech firm Biota Holdings. It was licensed to Glaxo in 1990 and approved in the US in 1999, only for use as a treatment for influenza. In 2006, it was approved for prevention of influenza A and B. Zanamivir was the first neuraminidase inhibitor commercially developed. It is marketed by GlaxoSmithKline under the trade name Relenza as a powder for oral inhalation.

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

Exo-α-sialidase is a glycoside hydrolase that cleaves the glycosidic linkages of neuraminic acids:

Virus-like particles (VLPs) are molecules that closely resemble viruses, but are non-infectious because they contain no viral genetic material. They can be naturally occurring or synthesized through the individual expression of viral structural proteins, which can then self assemble into the virus-like structure. Combinations of structural capsid proteins from different viruses can be used to create recombinant VLPs. Both in-vivo assembly and in-vitro assembly have been successfully shown to form virus-like particles. VLPs derived from the Hepatitis B virus (HBV) and composed of the small HBV derived surface antigen (HBsAg) were described in 1968 from patient sera. VLPs have been produced from components of a wide variety of virus families including Parvoviridae, Retroviridae, Flaviviridae, Paramyxoviridae and bacteriophages. VLPs can be produced in multiple cell culture systems including bacteria, mammalian cell lines, insect cell lines, yeast and plant cells.

<span class="mw-page-title-main">Gregory Winter</span> English biochemist (born 1951)

Sir Gregory Paul Winter is a Nobel Prize-winning English molecular biologist best known for his work on the therapeutic use of monoclonal antibodies. His research career has been based almost entirely at the MRC Laboratory of Molecular Biology and the MRC Centre for Protein Engineering, in Cambridge, England.

<span class="mw-page-title-main">Nucleoprotein</span> Type of protein

Nucleoproteins are proteins conjugated with nucleic acids. Typical nucleoproteins include ribosomes, nucleosomes and viral nucleocapsid proteins.

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.

<i>Enterovirus E</i> Species of virus

Enterovirus E is a picornavirus of the genus Enterovirus. The virus may also be referred to as enteric cytopathic bovine orphan virus (ECBO). It is endemic in cattle populations worldwide, and although normally fairly nonpathogenic, it can cause reproductive, respiratory, or enteric disease – particularly when the animal is concurrently infected with another pathogen.

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

Viral neuraminidase is a type of neuraminidase found on the surface of influenza viruses that enables the virus to be released from the host cell. Neuraminidases are enzymes that cleave sialic acid groups from glycoproteins. Neuraminidase inhibitors are antiviral agents that inhibit influenza viral neuraminidase activity and are of major importance in the control of influenza.

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

In molecular biology, hemagglutinins are receptor-binding membrane fusion glycoproteins produced by viruses in the Paramyxoviridae family. Hemagglutinins are responsible for binding to receptors on red blood cells to initiate viral attachment and infection. The agglutination of red cells occurs when antibodies on one cell bind to those on others, causing amorphous aggregates of clumped cells.

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

Hemagglutinin-neuraminidase refers to a single viral protein that has both hemagglutinin and (endo) neuraminidase EC 3.2.1.18 activity. This is in contrast to the proteins found in influenza, where both functions exist but in two separate proteins. Its neuraminidase domain has the CAZy designation glycoside hydrolase family 83 (GH83).

A heavy-chain antibody is an antibody which consists only of two heavy chains and lacks the two light chains usually found in antibodies.

<span class="mw-page-title-main">Peter Palese</span> American microbiologist and virologist

Peter Palese is a United States microbiologist, researcher, inventor and the Horace W. Goldsmith Professor in the Department of Microbiology at the Icahn School of Medicine at Mount Sinai in New York City, and an expert in the field of RNA viruses.

<span class="mw-page-title-main">George Hirst (virologist)</span> American virologist and science administrator

George Keble Hirst, M.D. was an American virologist and science administrator who was among the first to study the molecular biology and genetics of animal viruses, especially influenza virus. He directed the Public Health Research Institute in New York City (1956–1981), and was also the founding editor-in-chief of Virology, the first English-language journal to focus on viruses. He is particularly known for inventing the hemagglutination assay, a simple method for quantifying viruses, and adapting it into the hemagglutination inhibition assay, which measures virus-specific antibodies in serum. He was the first to discover that viruses can contain enzymes, and the first to propose that virus genomes can consist of discontinuous segments. The New York Times described him as "a pioneer in molecular virology."

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.

<span class="mw-page-title-main">Universal flu vaccine</span> Vaccine that prevents infection from all strains of the flu

A universal flu vaccine is a flu vaccine that is effective against all influenza strains regardless of the virus sub type, antigenic drift or antigenic shift. Hence it should not require modification from year to year. As of 2021 no universal flu vaccine had been approved for general use, several were in development, and one was in clinical trial.

<i>Influenza D virus</i> Species of virus

Influenza D virus is a species in the virus genus Deltainfluenzavirus, in the family Orthomyxoviridae, that causes influenza.

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. "Macfarlane Burnet Medal and Lecture". Australian Academy of Science. Retrieved 22 February 2017.

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