Cooperative Neuraminidase Activity in a Paramyxovirus

Paramyxoviruses possess neuraminidase (NA) activity, i.e., the ability to cleave sialic acid from membrane-bound and soluble glycoconjugates. The activity is associated with a homotetrameric, surface glycoprotein spike, called the hemagglutinin-neuraminidase. This structure also mediates viral attac...

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Bibliographic Details
Published in:Virology (New York, N.Y.) N.Y.), 1995-10, Vol.213 (1), p.241-244
Main Authors: Mahon, Paul J., Deng, Ruitang, Mirza, Anne M., Iorio, Ronald M.
Format: Article
Language:English
Subjects:
Antibodies, Monoclonal
HN Protein - metabolism
Influenza A virus - enzymology
Kinetics
Neuraminidase - metabolism
Newcastle disease virus
Newcastle disease virus - enzymology
Parainfluenza Virus 1, Human - enzymology
Substrate Specificity
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Summary:Paramyxoviruses possess neuraminidase (NA) activity, i.e., the ability to cleave sialic acid from membrane-bound and soluble glycoconjugates. The activity is associated with a homotetrameric, surface glycoprotein spike, called the hemagglutinin-neuraminidase. This structure also mediates viral attachment to sialic acid-containing receptors and constitutes the major neutralizing antigen for the virus. Cooperativity has been demonstrated for the NA activity of an isolate of one of the paramyxoviruses, Newcastle disease virus. Although all known viral NA proteins are homooligomeric, this is the first demonstration of cooperativity in this family of proteins. A variant virus, selected by escape from neutralization by a monoclonal antibody thought to bind close to the NA active site, has lost cooperativity. Conversion to the noncooperative state correlates with increases in both avidity for cellular receptors and fusogenic activity.
ISSN:0042-6822
1096-0341
DOI:10.1006/viro.1995.1564