JVI Figure table search 04
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Willett, B. J.
Right arrow Articles by Hosie, M. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Willett, B. J.
Right arrow Articles by Hosie, M. J.

 Previous Article  |  Next Article 

Journal of Virology, August 2006, p. 7744-7747, Vol. 80, No. 15
0022-538X/06/$08.00+0     doi:10.1128/JVI.00722-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Mapping the Domains of CD134 as a Functional Receptor for Feline Immunodeficiency Virus

Brian J. Willett,1* Elizabeth L. McMonagle,1 Francesca Bonci,2 Mauro Pistello,2 and Margaret J. Hosie1

Retrovirus Research Laboratory, Institute of Comparative Medicine, Faculty of Veterinary Medicine, University of Glasgow, Bearsden Road, Glasgow G61 1QH, United Kingdom,1 Department of Experimental Pathology, Retrovirus Center and Virology Section, University of Pisa, Via San Zeno 35, I-56127 Pisa, Italy2

Received 10 April 2006/ Accepted 4 May 2006

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.

* Corresponding author. Mailing address: Retrovirus Research Laboratory, Institute of Comparative Medicine, Faculty of Veterinary Medicine, University of Glasgow, Bearsden Road, Glasgow G61 1QH, United Kingdom. Phone: 44 141 330 3274. Fax: 44 141 330 2271. E-mail: b.willett{at}vet.gla.ac.uk.

Journal of Virology, August 2006, p. 7744-7747, Vol. 80, No. 15
0022-538X/06/$08.00+0     doi:10.1128/JVI.00722-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. Mol. Cell. Biol. Microbiol. Mol. Biol. Rev.
Clin. Vaccine Immunol. ALL ASM JOURNALS

Copyright © 2006 by the American Society for Microbiology. All rights reserved.