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Research Article

Rhabdovirus Matrix Protein Structures Reveal a Novel Mode of Self-Association

  • Stephen C. Graham,

    Affiliation: Division of Structural Biology and Oxford Protein Production Facility, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, United Kingdom

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  • René Assenberg equal contributor,

    equal contributor Contributed equally to this work with: René Assenberg, Olivier Delmas

    Affiliation: Division of Structural Biology and Oxford Protein Production Facility, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, United Kingdom

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  • Olivier Delmas equal contributor,

    equal contributor Contributed equally to this work with: René Assenberg, Olivier Delmas

    Affiliation: UPRE Lyssavirus Dynamics and Host Adaptation, WHO Collaborating Centre for Reference and Research on Rabies, Institut Pasteur, Paris, France

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  • Anil Verma,

    Affiliation: Division of Structural Biology and Oxford Protein Production Facility, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, United Kingdom

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  • Alireza Gholami,

    Affiliation: UPRE Lyssavirus Dynamics and Host Adaptation, WHO Collaborating Centre for Reference and Research on Rabies, Institut Pasteur, Paris, France

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  • Chiraz Talbi,

    Affiliation: UPRE Lyssavirus Dynamics and Host Adaptation, WHO Collaborating Centre for Reference and Research on Rabies, Institut Pasteur, Paris, France

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  • Raymond J. Owens,

    Affiliation: Division of Structural Biology and Oxford Protein Production Facility, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, United Kingdom

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  • David I. Stuart,

    Affiliation: Division of Structural Biology and Oxford Protein Production Facility, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, United Kingdom

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  • Jonathan M. Grimes mail,

    jonathan@strubi.ox.ac.uk (JMG); hbourhy@pasteur.fr (HB)

    Affiliation: Division of Structural Biology and Oxford Protein Production Facility, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, United Kingdom

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  • Hervé Bourhy mail

    jonathan@strubi.ox.ac.uk (JMG); hbourhy@pasteur.fr (HB)

    Affiliation: UPRE Lyssavirus Dynamics and Host Adaptation, WHO Collaborating Centre for Reference and Research on Rabies, Institut Pasteur, Paris, France

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  • Published: December 26, 2008
  • DOI: 10.1371/journal.ppat.1000251

About the Authors

Stephen C. Graham, René Assenberg, Anil Verma, Raymond J. Owens, David I. Stuart, Jonathan M. Grimes
Division of Structural Biology and Oxford Protein Production Facility, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, United Kingdom
Olivier Delmas, Alireza Gholami, Chiraz Talbi, Hervé Bourhy
UPRE Lyssavirus Dynamics and Host Adaptation, WHO Collaborating Centre for Reference and Research on Rabies, Institut Pasteur, Paris, France

Corresponding Authors

Competing Interests

The authors have declared that no competing interests exist.

Author Contributions

Wrote the paper: SCG. Collected diffraction data, solved and refined the structures, and performed analytical gel filtration: SCG. Expressed, purified and crystallized LBV and VSVNJ M, and subcloned LBV M: RA. Cloned LBV and VSVNJ M: OD. Purified LBV M: AV. Cloned truncated LBV M: AG. Sequenced lyssavirus M genes: CT. Designed the experiments, interpreted the results and revised the manuscript: SCG RA OD AV AG CT RJO DIS JMG HB.