title: Deletion of the second immunoglobulin-like domain of nectin-1 alters its intracellular processing and localization and ability to mediate entry of herpes simplex virus.
abstract: Nectin-1 is an immunoglobulin (Ig)-like entry receptor for herpes simplex virus (HSV). Like other nectins, nectin-1 forms dimers and mediates cell adhesion through interactions with other nectins. We constructed a second-domain deletion mutant of nectin-1 (nectin-1-Delta2) to examine the role of the second Ig-like domain in HSV entry. Nectin-1-Delta2 exhibited a severely reduced ability to mediate HSV entry and accumulated in the endoplasmic reticulum but retained the ability to interact with its HSV ligand, gD. The failure of nectin-1-Delta2 to mediate HSV entry probably resulted from its failure to be transported to a membrane targeted by HSV for viral entry.
authors.affiliation: Northwestern University, The Feinberg School of Medicine, Department of Microbiology and Immunology, Searle 6-447, 320 E. Superior St., Chicago, IL 60611, USA.
authors.forename: Frank
authors.initials: F
authors.lastname: Struyf
authors.forename: Aileen E
authors.initials: AE
authors.lastname: Plate
authors.forename: Patricia G
authors.initials: PG
authors.lastname: Spear
mesh_terms: D000818:Animals; D016466:CHO Cells; D015815:Cell Adhesion Molecules / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006224:Cricetinae; D004721:Endoplasmic Reticulum / Q000737:chemistry; D000075983:Nectins; D011485:Protein Binding; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary; D011991:Receptors, Virus / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D017384:Sequence Deletion; D018139:Simplexvirus / Q000502:physiology*; D014759:Viral Envelope Proteins / Q000378:metabolism
chemical_list: D015815:Cell Adhesion Molecules; C000619010:NECTIN1 protein, human; D000075983:Nectins; D011991:Receptors, Virus; D014759:Viral Envelope Proteins; C039447:glycoprotein D, Human herpesvirus 1
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