NDLI: Efficient replication of a paramyxovirus independent of full zippering of the fusion protein six-helix bundle domain

Content Provider	PubMed Central
Author	Brindley, Melinda A. Philippe, Plattet Karl, Plemper Richard
Abstract	Protein-mediated membrane fusion is essential for eukaryotic cell biology. In several major human viral pathogens the full closure of a six-helix bundle (6HB) fusion core structure is considered imperative for the opening of a productive fusion pore. We tested this paradigm by engineering covalently restricted paramyxovirus fusion proteins that are incapable of full 6HB zippering. These proteins remained fusion competent without disruption of the restricting bonds, although fusion activity was reduced. Recombinant virions harboring the engineered fusion proteins confirmed efficient, 6HB closure-independent paramyxovirus entry. We demonstrate that full 6HB zippering does not govern paramyxovirus entry. Our results may extend to other viruses using related fusiogenic glycoproteins and affect the design of antiparamyxovirus strategies targeting virus entry.
Related Links	http://dx.doi.org/10.1073/pnas.1403609111
Starting Page	3795
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	36
Volume Number	111
Language	English
Publisher	National Academy of Sciences
Publisher Date	2014-09-09
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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Efficient replication of a paramyxovirus independent of full zippering of the fusion protein six-helix bundle domain