| http://purl.uniprot.org/citations/12438620 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12438620 | http://www.w3.org/2000/01/rdf-schema#comment | "Nectin-1 and nectin-2 are related molecules that can function with different specificities as entry receptors for mammalian alphaherpesviruses through interaction with viral glycoprotein D (gD). The normal function of members of the nectin family is to mediate cell-cell adhesion through homotypic and heterotypic nectin-nectin interactions in cadherin-based adherens junctions. We examined mutations in three equivalent regions of the N-terminal V-like domains of nectin-1 and nectin-2 to test the effects on entry of various alphaherpesviruses, nectin-nectin interactions, and interactions of the mutant nectins with gD. Mutations in region I previously shown to severely impair herpes simplex virus (HSV) entry activity, but not pseudorabies virus (PRV) or bovine herpesvirus 1 (BHV-1) entry, did not reduce homotypic trans interactions for either nectin-1 or nectin-2 or binding of nectin-3 to nectin-1. Mutations in region II, patterned after a reported single-nucleotide polymorphism in nectin-2, enhanced intracellular accumulation of both nectin-1 and nectin-2 and had a deleterious effect on all of the activities under study. Mutations in region III previously shown to reduce homotypic trans interactions of nectin-2 impaired the entry of PRV and BHV-1 when introduced into either nectin-1 or nectin-2, but only the nectin-2 mutation reduced HSV entry activity. Binding of nectin-1 to nectin-3 was not affected. Effects of the nectin-1 and nectin-2 mutations on interactions with gD did not necessarily correlate with entry activity of the mutant receptors. We can conclude that structural requirements for HSV entry, PRV and BHV-1 entry, and homotypic and heterotypic trans interactions are all different despite the previously reported ability of HSV and HSV gD to inhibit trans interactions."xsd:string |
| http://purl.uniprot.org/citations/12438620 | http://purl.org/dc/terms/identifier | "doi:10.1128/jvi.76.24.12940-12950.2002"xsd:string |
| http://purl.uniprot.org/citations/12438620 | http://purl.uniprot.org/core/author | "Spear P.G."xsd:string |
| http://purl.uniprot.org/citations/12438620 | http://purl.uniprot.org/core/author | "Martinez W.M."xsd:string |
| http://purl.uniprot.org/citations/12438620 | http://purl.uniprot.org/core/author | "Struyf F."xsd:string |
| http://purl.uniprot.org/citations/12438620 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/12438620 | http://purl.uniprot.org/core/name | "J Virol"xsd:string |
| http://purl.uniprot.org/citations/12438620 | http://purl.uniprot.org/core/pages | "12940-12950"xsd:string |
| http://purl.uniprot.org/citations/12438620 | http://purl.uniprot.org/core/title | "Mutations in the N-terminal domains of nectin-1 and nectin-2 reveal differences in requirements for entry of various alphaherpesviruses and for nectin-nectin interactions."xsd:string |
| http://purl.uniprot.org/citations/12438620 | http://purl.uniprot.org/core/volume | "76"xsd:string |
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