The human homologue of the bovine leukemia virus receptor BLVRcp1 is the δ-subunit of adaptor-related AP-3 protein that does not bind the BVLgp51

The human homologue of the bovine leukemia virus receptor BLVRcp1 is the δ-subunit of... The relationship between the putative bovine leukemia virus receptor gene (BVLRcp) and the susceptibility of human cells to BLV infection was studied. Three cDNA clones encoding different portions of the human equivalent of bovine BLVRcp1 were isolated by DNA-DNA hybridization by comparison of the human cDNA clones to bovine BLVRcp1. Amino acid sequence indicated that the human sequence encodes the $\trdelta$ subunit of the AP-3 adaptor-related protein. When the recombinant human homologue BLVRcp2 was expressed in E. coli , it failed to bind the BLVgp51. However, the BVLVgp51 binding ability was restored when the chimerical BLVRcp molecule was prepared by exchanging 5′ ends between bovine and human BLVRcp cDNAs. This finding implies that this BLVgp51 binding site is present only on the bovine BLVRcp and therefore its human homologue cannot be recognized by BLVgp51. This might also explain the resistance of human cells to BLV infection. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Virology Springer Journals

The human homologue of the bovine leukemia virus receptor BLVRcp1 is the δ-subunit of adaptor-related AP-3 protein that does not bind the BVLgp51

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Publisher
Springer-Verlag
Copyright
Copyright © Wien by 1999 Springer-Verlag/
Subject
Legacy
ISSN
0304-8608
eISSN
1432-8798
D.O.I.
10.1007/s007050050722
Publisher site
See Article on Publisher Site

Abstract

The relationship between the putative bovine leukemia virus receptor gene (BVLRcp) and the susceptibility of human cells to BLV infection was studied. Three cDNA clones encoding different portions of the human equivalent of bovine BLVRcp1 were isolated by DNA-DNA hybridization by comparison of the human cDNA clones to bovine BLVRcp1. Amino acid sequence indicated that the human sequence encodes the $\trdelta$ subunit of the AP-3 adaptor-related protein. When the recombinant human homologue BLVRcp2 was expressed in E. coli , it failed to bind the BLVgp51. However, the BVLVgp51 binding ability was restored when the chimerical BLVRcp molecule was prepared by exchanging 5′ ends between bovine and human BLVRcp cDNAs. This finding implies that this BLVgp51 binding site is present only on the bovine BLVRcp and therefore its human homologue cannot be recognized by BLVgp51. This might also explain the resistance of human cells to BLV infection.

Journal

Archives of VirologySpringer Journals

Published: Oct 1, 1999

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