Amino acid substitutions in a conserved region in the stalk of the Newcastle disease virus HN glycoprotein spike impair its neuraminidase activity in the globular domain
UMass Chan Affiliations
Department of Molecular Genetics and MicrobiologyDocument Type
Journal ArticlePublication Date
1999-03-26Keywords
AdsorptionAmino Acid Sequence
*Amino Acid Substitution
Animals
Antibodies, Monoclonal
Cell Line
Conserved Sequence
Epitopes
Erythrocytes
Guinea Pigs
HN Protein
Humans
Lactose
Leucine Zippers
Molecular Sequence Data
Neuraminidase
Newcastle Disease
Newcastle disease virus
Protein Conformation
Sialic Acids
Transfection
Life Sciences
Medicine and Health Sciences
Metadata
Show full item recordAbstract
The ectodomain of the paramyxovirus haemagglutinin-neuraminidase (HN) glycoprotein spike can be divided into two regions: a membrane-proximal, stalk-like structure and a terminal globular domain. The latter contains all the antibody recognition sites of the protein, as well as its receptor recognition and neuraminidase (NA) active sites. These two activities of the protein can be separated by monoclonal antibody functional inhibition studies and mutations in the globular domain. Herein, we show that mutation of several conserved residues in the stalk of the Newcastle disease virus HN protein markedly decrease its NA activity without a significant effect on receptor recognition. Thus, mutations in the stalk, distant from the NA active site in the globular domain, can also separate attachment and NA. These results add to an increasing body of evidence that the NA activity of this protein is dependent on an intact stalk structure.Source
J Gen Virol. 1999 Mar;80 ( Pt 3):749-53.
DOI
10.1099/0022-1317-80-3-749Permanent Link to this Item
http://hdl.handle.net/20.500.14038/38193PubMed ID
10092015Related Resources
ae974a485f413a2113503eed53cd6c53
10.1099/0022-1317-80-3-749