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Shared paramyxoviral glycoprotein architecture is adapted for diverse attachment strategies

Shared paramyxoviral glycoprotein architecture is adapted for diverse attachment strategies
Shared paramyxoviral glycoprotein architecture is adapted for diverse attachment strategies

Members within the paramyxovirus subfamily Paramyxovirinae constitute a large number of highly virulent human and animal pathogens. The glycoproteins present on these viruses are responsible for mediating host cell attachment and fusion and are key targets for the design of antiviral entry inhibitors. In the present review, we discuss recent structural studies which have led to a better understanding of the various mechanisms by which different paramyxoviruses use their attachment glycoproteins to hijack specific protein and glycan cell-surface receptors to facilitate viral entry. It is observed that the paramyxovirus attachment glycoprotein consists of a conserved overall structure which includes an N-terminal six-bladed β-propeller domain which is responsible for cell receptor binding. Crystal structures of this domain from different biomedically important paramyxoviruses, including measles, Nipah, Hendra, Newcastle disease and parainfluenza viruses, alone and in complex with their functional cell-surface receptors, demonstrate three contrasting mechanisms of receptor engagement that paramyxoviruses have evolved to confer discreet protein- and glycan-receptor specificity. This structural information highlights the adaptability of the paramyxovirus attachment glycoprotein surface and the potential for the emergence of new and potentially harmful viruses in human hosts.

Paramyxovirus, Protein crystallography, Structural virology, Viral glycoprotein, Virus entry
0300-5127
1349-1355
Bowden, Thomas A.
4b17a588-ac01-4112-807a-8b99a6c20d0f
Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9
Jones, E. Yvonne
6b9004c9-137b-4f43-8a14-c7c83bcaa4be
Stuart, David I.
2751c230-9d4c-4981-aeb7-cafb51ed749d
Bowden, Thomas A.
4b17a588-ac01-4112-807a-8b99a6c20d0f
Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9
Jones, E. Yvonne
6b9004c9-137b-4f43-8a14-c7c83bcaa4be
Stuart, David I.
2751c230-9d4c-4981-aeb7-cafb51ed749d

Bowden, Thomas A., Crispin, Max, Jones, E. Yvonne and Stuart, David I. (2010) Shared paramyxoviral glycoprotein architecture is adapted for diverse attachment strategies. Biochemical Society Transactions, 38 (5), 1349-1355. (doi:10.1042/BST0381349).

Record type: Review

Abstract

Members within the paramyxovirus subfamily Paramyxovirinae constitute a large number of highly virulent human and animal pathogens. The glycoproteins present on these viruses are responsible for mediating host cell attachment and fusion and are key targets for the design of antiviral entry inhibitors. In the present review, we discuss recent structural studies which have led to a better understanding of the various mechanisms by which different paramyxoviruses use their attachment glycoproteins to hijack specific protein and glycan cell-surface receptors to facilitate viral entry. It is observed that the paramyxovirus attachment glycoprotein consists of a conserved overall structure which includes an N-terminal six-bladed β-propeller domain which is responsible for cell receptor binding. Crystal structures of this domain from different biomedically important paramyxoviruses, including measles, Nipah, Hendra, Newcastle disease and parainfluenza viruses, alone and in complex with their functional cell-surface receptors, demonstrate three contrasting mechanisms of receptor engagement that paramyxoviruses have evolved to confer discreet protein- and glycan-receptor specificity. This structural information highlights the adaptability of the paramyxovirus attachment glycoprotein surface and the potential for the emergence of new and potentially harmful viruses in human hosts.

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More information

Published date: October 2010
Keywords: Paramyxovirus, Protein crystallography, Structural virology, Viral glycoprotein, Virus entry

Identifiers

Local EPrints ID: 414591
URI: https://eprints.soton.ac.uk/id/eprint/414591
ISSN: 0300-5127
PURE UUID: af508fe2-8047-4b1f-830e-9c9437deb661
ORCID for Max Crispin: ORCID iD orcid.org/0000-0002-1072-2694

Catalogue record

Date deposited: 04 Oct 2017 16:30
Last modified: 16 Jul 2019 00:26

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