Modes of paramyxovirus fusion: a Henipavirus perspective |
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| Authors: | Lee Benhur Ataman Zeynep Akyol |
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| Affiliation: | 1 Department of Microbiology, Immunology and Molecular Genetics, University of California, Los Angeles, David Geffen School of Medicine, 615 Charles E. Young Drive East, Los Angeles, CA 90095, USA
2 Department of Pathology and Laboratory Medicine, University of California, Los Angeles, David Geffen School of Medicine, 615 Charles E. Young Drive East, Los Angeles, CA 90095, USA |
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| Abstract: | Henipavirus is a new genus of Paramyxoviridae that uses protein-based receptors (ephrinB2 and ephrinB3) for virus entry. Paramyxovirus entry requires the coordinated action of the fusion (F) and attachment viral envelope glycoproteins. Receptor binding to the attachment protein triggers F to undergo a conformational cascade that results in membrane fusion. The accumulation of structural and functional studies on many paramyxoviral fusion and attachment proteins, including the recent elucidation of structures of Nipah virus (NiV) and Hendra virus (HeV) G glycoproteins bound and unbound to cognate ephrinB receptors, indicate that henipavirus entry and fusion could differ mechanistically from paramyxoviruses that use glycan-based receptors. |
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