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Rhabdovirus matrix protein structures reveal a novel mode of self-association

Abstract:

The matrix (M) proteins of rhabdoviruses are multifunctional proteins essential for virus maturation and budding that also regulate the expression of viral and host proteins. We have solved the structures of M from the vesicular stomatitis virus serotype New Jersey (genus: Vesiculovirus) and from Lagos bat virus (genus: Lyssavirus), revealing that both share a common fold despite sharing no identifiable sequence homology. Strikingly, in both structures a stretch of residues from the otherwise...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1371/journal.ppat.1000251

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Institution:
University of Oxford
Department:
Oxford Protein Production Facility
Role:
Author
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Institution:
University of Oxford
Department:
Oxford Protein Production Facility
Role:
Author
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Institution:
Institut Pasteur, Paris, France
Department:
UPRE Lyssavirus Dynamics and Host Adaptation,WHO Collaborating Centre for Reference and Research on Rabies
Role:
Author
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Institution:
University of Oxford
Department:
Oxford Protein Production Facility
Role:
Author
More by this author
Institution:
Institut Pasteur, Paris, France
Department:
UPRE Lyssavirus Dynamics and Host Adaptation,WHO Collaborating Centre for Reference and Research on Rabies
Role:
Author
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Contributors

Institution:
Wake Forest University School of Medicine
Role:
Editor
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Grant:
"LSHG-CT-2004-511960", "LSHG-CT-2006-031220"
Biotechnology and Biological Sciences Research Council More from this funder
Medical Research Council More from this funder
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Funding agency for:
Grimes, J
Publisher:
Public Library of Science Publisher's website
Journal:
PLoS Pathogens Journal website
Volume:
4
Issue:
12
Article number:
e1000251
Publication date:
2008-12-01
DOI:
EISSN:
1553-7374
ISSN:
1553-7366
Language:
English
Keywords:
Subjects:
UUID:
uuid:655cffee-628f-4711-b164-4fc18aa98fa5
Local pid:
ora:2806
Deposit date:
2009-06-04

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