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dc.contributor.authorAlamares, Judith G.
dc.contributor.authorLi, Jianrong
dc.contributor.authorIorio, Ronald M.
dc.date2022-08-11T08:08:57.000
dc.date.accessioned2022-08-23T16:13:55Z
dc.date.available2022-08-23T16:13:55Z
dc.date.issued2005-08-06
dc.date.submitted2008-06-23
dc.identifier.citationJ Clin Microbiol. 2005 Aug;43(8):4229-33. <a href="http://dx.doi.org/10.1128/JCM.43.8.4229-4233.2005">Link to article on publisher's site</a>
dc.identifier.issn0095-1137 (Print)
dc.identifier.doi10.1128/JCM.43.8.4229-4233.2005
dc.identifier.pmid16081986
dc.identifier.urihttp://hdl.handle.net/20.500.14038/33737
dc.description.abstractNewcastle disease virus (NDV) strains are classified as having high (velogenic), intermediate (mesogenic), or low (lentogenic) pathogenesis and virulence in chickens. Recent studies have established that the hemagglutinin-neuraminidase (HN) protein plays an important role in viral tropism and virulence. A monoclonal antibody (AVS-I) has previously been shown to be specific for lentogenic strains of NDV (Srinivasappa et al., Avian Dis. 30:562-567, 1986) and is routinely used to identify these strains. We have used competition antibody binding assays with a previously characterized panel of monoclonal antibodies, binding to chimeric HN proteins, and the characterization of an escape mutant to localize the binding site of AVS-I to the extreme carboxy terminus of the protein. In addition, we have shown that AVS-I does recognize at least one mesogenic strain and one velogenic strain of the virus, calling into question the potential of this antibody as a diagnostic reagent for avirulent NDV strains.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=16081986&dopt=Abstract ">Link to article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1128/JCM.43.8.4229-4233.2005
dc.subjectAntibodies, Monoclonal; Binding Sites, Antibody; Epitopes; HN Protein; Hemagglutination Inhibition Tests; Neutralization Tests; Newcastle disease virus; Protein Conformation; Structure-Activity Relationship; Virulence
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleMonoclonal antibody routinely used to identify avirulent strains of Newcastle disease virus binds to an epitope at the carboxy terminus of the hemagglutinin-neuraminidase protein and recognizes individual mesogenic and velogenic strains
dc.typeJournal Article
dc.source.journaltitleJournal of clinical microbiology
dc.source.volume43
dc.source.issue8
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/40
dc.identifier.contextkey537403
html.description.abstract<p>Newcastle disease virus (NDV) strains are classified as having high (velogenic), intermediate (mesogenic), or low (lentogenic) pathogenesis and virulence in chickens. Recent studies have established that the hemagglutinin-neuraminidase (HN) protein plays an important role in viral tropism and virulence. A monoclonal antibody (AVS-I) has previously been shown to be specific for lentogenic strains of NDV (Srinivasappa et al., Avian Dis. 30:562-567, 1986) and is routinely used to identify these strains. We have used competition antibody binding assays with a previously characterized panel of monoclonal antibodies, binding to chimeric HN proteins, and the characterization of an escape mutant to localize the binding site of AVS-I to the extreme carboxy terminus of the protein. In addition, we have shown that AVS-I does recognize at least one mesogenic strain and one velogenic strain of the virus, calling into question the potential of this antibody as a diagnostic reagent for avirulent NDV strains.</p>
dc.identifier.submissionpathgsbs_sp/40
dc.contributor.departmentDepartment of Molecular Genetics and Microbiology
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages4229-33


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