2004
DOI: 10.1128/jvi.78.23.13351-13355.2004
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Biological Significance of the Second Receptor Binding Site of Newcastle Disease Virus Hemagglutinin-Neuraminidase Protein

Abstract: The paramyxovirus hemagglutinin-neuraminidase (HN) is a multifunctional protein responsible for attachment to receptors containing sialic acid, neuraminidase (NA) activity, and the promotion of membrane fusion, which is induced by the fusion protein. Analysis of the three-dimensional structure of Newcastle disease virus (NDV) HN protein revealed the presence of a large pocket, which mediates both receptor binding and NA activities. Recently, a second sialic acid binding site on HN was revealed by cocrystalliza… Show more

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Cited by 39 publications
(48 citation statements)
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“…The NDV HN protein forms tetramers on the virion, and similar to the PIV5 HN, the isolated head NA domains exist primarily as monomers (4)(5)(6)(16)(17)(18). The HN stalk provides a significant driving force for oligomerization, but the TM domains are also thought to play a role (19).…”
Section: Resultsmentioning
confidence: 99%
“…The NDV HN protein forms tetramers on the virion, and similar to the PIV5 HN, the isolated head NA domains exist primarily as monomers (4)(5)(6)(16)(17)(18). The HN stalk provides a significant driving force for oligomerization, but the TM domains are also thought to play a role (19).…”
Section: Resultsmentioning
confidence: 99%
“…On the side of the helix at which N-glycan addition decreases HAd, the N-glycan may be disrupting HNЈs second sialic acid binding site formed by the dimeric interface, thereby decreasing HNЈs receptor binding avidity. This idea is based on the demonstrated role of the second sialic acid binding site in attachment (3). N-glycan addition to the other side of the HR2 helix increases receptor binding avidity and may do so by stabilizing the receptor-binding structure of HN, resulting in a more efficient interaction with receptors.…”
Section: Discussionmentioning
confidence: 99%
“…For the HN glycoproteins both receptor binding activity and the neuraminidase active site are localized to the globular head domain, as with human parainfluenza virus 3 (hPIV-3) and NDV HN (10,16,30,52). In addition to receptor binding and specificity, the attachment glycoproteins also possess the fusion promotion activity and specificity for the F glycoprotein.…”
mentioning
confidence: 99%