Abstract:
:The C-C chemokine receptor 5 (CCR5) plays a crucial role in facilitating the entry of macrophage-tropic strains of the HIV-1 into cells, but the mechanism of this phenomenon is completely unknown. To explore the role of CCR5-derived signal transduction in viral entry, we introduced mutations into two cytoplasmic domains of CCR5 involved in receptor-mediated function. Truncation of the terminal carboxyl-tail to eight amino acids or mutation of the highly conserved aspartate-arginine-tyrosine, or DRY, sequence in the second cytoplasmic loop of CCR5 effectively blocked chemokine-dependent activation of classic second messengers, intracellular calcium fluxes, and the cellular response of chemotaxis. In contrast, none of the mutations altered the ability of CCR5 to act as an HIV-1 coreceptor. We conclude that the initiation of signal transduction, the prototypic function of G protein coupled receptors, is not required for CCR5 to act as a coreceptor for HIV-1 entry into cells.
journal_name
Proc Natl Acad Sci U S Aauthors
Gosling J,Monteclaro FS,Atchison RE,Arai H,Tsou CL,Goldsmith MA,Charo IFdoi
10.1073/pnas.94.10.5061subject
Has Abstractpub_date
1997-05-13 00:00:00pages
5061-6issue
10eissn
0027-8424issn
1091-6490journal_volume
94pub_type
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