Journal
JOURNAL OF VIROLOGY
Volume 78, Issue 7, Pages 3733-3741Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.78.7.3733-3741.2004
Keywords
-
Categories
Funding
- NIAID NIH HHS [AI-11949, R01 AI038956, AI-38956] Funding Source: Medline
Ask authors/readers for more resources
Paramyxoviruses are the leading cause of respiratory disease in children. Several paramyxoviruses possess a surface glycoprotein, the hemagglutinin-neuraminidase (HN), that is involved in attachment to sialic acid receptors, promotion of fusion, and removal of sialic acid from infected cells and progeny virions. Previously we showed that Newcastle disease virus (NDV) HN contained a pliable sialic acid recognition site that could take two states, a binding state and a catalytic state. Here we present evidence for a second sialic acid binding site at the dimer interface of HN and present a model for its involvement in cell fusion. Three different crystal forms of NDV HN now reveal identical tetrameric arrangements of HN monomers, perhaps indicative of the tetramer association found on the viral surface.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available