TY - JOUR
T1 - Molecular piracy of mammalian interleukin-8 receptor type B by herpesvirus saimiri
AU - Ahuja, S. K.
AU - Murphy, P. M.
N1 - Copyright:
Copyright 2004 Elsevier B.V., All rights reserved.
PY - 1993
Y1 - 1993
N2 - Viruses are known to acquire and modify the genes of their hosts to attain a survival advantage in the host environment. Herpesvirus saimiri (HVS) is a T-lymphotropic virus that causes fatal lymphoproliferative diseases in several non-human primates. The gene ECRF3 of HVS was most likely acquired from a primate host. ECRF3 encodes a putative seven-transmembrane-domain receptor that is remotely related (~30% amino acid identity) to the known mammalian α and β chemokine receptors, namely interleukin-8 receptor (IL8R) types A and B and the MIP-1α/RANTES receptor, respectively. Chemokines regulate the trafficking, activation, and, in some cases, proliferation of myeloid and lymphoid cell types. We now show that ECRF3 encodes a functional receptor for the α chemokines IL-8, GRO/melanoma growth stimulatory activity (MGSA), and NAP-2 but not for β chemokines, a specificity identical to that of IL8RB. Paradoxically, IL8RA shares 77% amino acid identity with IL8RB but is not a receptor for GRO/MGSA or NAP-2. This is the first functional characterization of a viral seven-transmembrane-domain receptor. It suggests a novel role for α chemokines in the pathogenesis of HVS infection by transmembrane signaling via the product of ECRF3.
AB - Viruses are known to acquire and modify the genes of their hosts to attain a survival advantage in the host environment. Herpesvirus saimiri (HVS) is a T-lymphotropic virus that causes fatal lymphoproliferative diseases in several non-human primates. The gene ECRF3 of HVS was most likely acquired from a primate host. ECRF3 encodes a putative seven-transmembrane-domain receptor that is remotely related (~30% amino acid identity) to the known mammalian α and β chemokine receptors, namely interleukin-8 receptor (IL8R) types A and B and the MIP-1α/RANTES receptor, respectively. Chemokines regulate the trafficking, activation, and, in some cases, proliferation of myeloid and lymphoid cell types. We now show that ECRF3 encodes a functional receptor for the α chemokines IL-8, GRO/melanoma growth stimulatory activity (MGSA), and NAP-2 but not for β chemokines, a specificity identical to that of IL8RB. Paradoxically, IL8RA shares 77% amino acid identity with IL8RB but is not a receptor for GRO/MGSA or NAP-2. This is the first functional characterization of a viral seven-transmembrane-domain receptor. It suggests a novel role for α chemokines in the pathogenesis of HVS infection by transmembrane signaling via the product of ECRF3.
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M3 - Article
C2 - 8407886
AN - SCOPUS:0027372763
VL - 268
SP - 20691
EP - 20694
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 28
ER -