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dc.contributor.authorWang, Zhiyu
dc.contributor.authorIorio, Ronald M.
dc.date2022-08-11T08:09:31.000
dc.date.accessioned2022-08-23T16:33:50Z
dc.date.available2022-08-23T16:33:50Z
dc.date.issued1999-03-26
dc.date.submitted2008-10-31
dc.identifier.citation<p>J Gen Virol. 1999 Mar;80 ( Pt 3):749-53.</p>
dc.identifier.issn0022-1317 (Print)
dc.identifier.doi10.1099/0022-1317-80-3-749
dc.identifier.pmid10092015
dc.identifier.urihttp://hdl.handle.net/20.500.14038/38193
dc.description.abstractThe 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.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=10092015&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttps://doi.org/10.1099/0022-1317-80-3-749
dc.subjectAdsorption
dc.subjectAmino Acid Sequence
dc.subject*Amino Acid Substitution
dc.subjectAnimals
dc.subjectAntibodies, Monoclonal
dc.subjectCell Line
dc.subjectConserved Sequence
dc.subjectEpitopes
dc.subjectErythrocytes
dc.subjectGuinea Pigs
dc.subjectHN Protein
dc.subjectHumans
dc.subjectLactose
dc.subjectLeucine Zippers
dc.subjectMolecular Sequence Data
dc.subjectNeuraminidase
dc.subjectNewcastle Disease
dc.subjectNewcastle disease virus
dc.subjectProtein Conformation
dc.subjectSialic Acids
dc.subjectTransfection
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleAmino 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
dc.typeJournal Article
dc.source.journaltitleThe Journal of general virology
dc.source.volume80 ( Pt 3)
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/1073
dc.identifier.contextkey659262
html.description.abstract<p>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.</p>
dc.identifier.submissionpathoapubs/1073
dc.contributor.departmentDepartment of Molecular Genetics and Microbiology
dc.source.pages749-53


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