Mapping the Domains of Cd134 As a Functional Receptor for Feline Immunodeficiency Virus.
From: Retrovirus Research Laboratory, Institute of Comparative Medicine, Faculty of Veterinary Medicine, University of Glasgow, Bearsden Road, Glasgow G61 1QH, United Kingdom. b.willett@vet.gla.ac.uk
Journal of virology
- Publish Date: Aug 2006
- ISSN: 0022-538X
- Volume: 80
- Issue: 15
- Pages: 7744-7
- Medium: Print
- Language: English
- Citation (JAMA): Willett Brian J, McMonagle Elizabeth L, Bonci Francesca, et al. Mapping the Domains of Cd134 As a Functional Receptor for Feline Immunodeficiency Virus.. J. Virol. Aug 2006;80:7744-7
Abstract
The feline homologue of CD134 is the primary binding receptor for feline immunodeficiency virus (FIV), targeting the virus preferentially to activated CD4+ helper T cells. However, strains of FIV differ in utilization of CD134; the prototypic strain PPR requires a minimal determinant in the first cysteine-rich domain (CRD1) of feline CD134 to confer near-optimal receptor function, while strains such as GL8 require additional determinants in the CD134 CRD2. We map this determinant to a loop in CRD2 governing the interaction between the receptor and its ligand; the amino acid substitutions S78N-S79Y-K80E restored full viral receptor activity to the CDR2 of human CD134 in the context of feline CD134, with tyrosine-79 appearing to be the critical residue for restoration of receptor function.
Mesh Headings (Keywords): Amino Acid Substitution, Animals, CD4-Positive T-Lymphocytes, Cats, Hela Cells, Humans, Immunodeficiency Virus, Feline, Ligands, Protein Structure, Tertiary, Receptors, OX40, Receptors, Tumor Necrosis Factor, Receptors, Virus, Tyrosine
Check for Full Text / PubMed Unique Identifier (PMID): 16840353
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