Journal
JOURNAL OF VIROLOGY
Volume 85, Issue 22, Pages 12079-12082Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.05679-11
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Funding
- National Institutes of Health [AI-49268]
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Newcastle disease virus (NDV)-induced membrane fusion requires an interaction between the hemagglutinin-neuraminidase (HN) attachment and the fusion (F) proteins, triggered by HN's binding to receptors. NDV HN has two sialic acid binding sites: site I, which also mediates neuraminidase activity, and site II, which straddles the membrane-distal end of the dimer interface. By characterizing the effect on receptor binding avidity and F-interactive capability of HN dimer interface mutations, we present evidence consistent with (i) receptor engagement by site I triggering the interaction with F and (ii) site II functioning to maintain high-avidity receptor binding during the fusion process.
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