Abstract:
:The Paramyxoviridae family of enveloped viruses enters cells through the concerted action of two viral glycoproteins. The receptor-binding protein, hemagglutinin-neuraminidase (HN), H, or G, binds its cellular receptor and activates the fusion protein, F, which, through an extensive refolding event, brings viral and cellular membranes together, mediating virus-cell fusion. However, the underlying mechanism of F activation on receptor engagement remains unclear. Current hypotheses propose conformational changes in HN, H, or G propagating from the receptor-binding site in the HN, H, or G globular head to the F-interacting stalk region. We provide evidence that the receptor-binding globular head domain of the paramyxovirus parainfluenza virus 5 HN protein is entirely dispensable for F activation. Considering together the crystal structures of HN from different paramyxoviruses, varying energy requirements for fusion activation, F activation involving the parainfluenza virus 5 HN stalk domain, and properties of a chimeric paramyxovirus HN protein, we propose a simple model for the activation of paramyxovirus fusion.
journal_name
Proc Natl Acad Sci U S Aauthors
Bose S,Zokarkar A,Welch BD,Leser GP,Jardetzky TS,Lamb RAdoi
10.1073/pnas.1213813109subject
Has Abstractpub_date
2012-09-25 00:00:00pages
E2625-34issue
39eissn
0027-8424issn
1091-6490pii
1213813109journal_volume
109pub_type
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