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. 1997 Apr 28;231(1):105-11.
doi: 10.1006/viro.1997.8506.

Role of the amino-terminal extracellular domain of CXCR-4 in human immunodeficiency virus type 1 entry

L Picard  1 , D A Wilkinson, A McKnight, P W Gray, J A Hoxie, P R Clapham, R A Weiss
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Free article

Role of the amino-terminal extracellular domain of CXCR-4 in human immunodeficiency virus type 1 entry

L Picard et al. Virology. .
Free article

Abstract

We have studied the role of the N-terminal extracellular domain of the human immunodeficiency virus type 1 (HIV-1) coreceptor, CXCR-4, in the entry and fusion of syncytium-inducing strains of HIV-1. Progressive deletions were introduced in the N-terminal extracellular domain of CXCR-4 and the effect on infection by different isolates was tested. Infection of cells expressing the different CXCR-4 deletion mutants by HIV-1 LAI and 89.6 was reduced only about twofold. In contrast, the HIV-1 GUN-1 and RF isolates were substantially more impaired in their ability to mediate cell-free infection and cell-cell fusion. Since LAI and RF are T-cell line-tropic viruses while 89.6 and GUN-1 are dual tropic, no clear correlation between tropism and requirements for CXCR-4 N-terminal sequences emerged. We also introduced point mutations at the two N-linked glycosylation sites. The isolates tested (LAI, RF, GUN-1, and 89.6) were not affected by the removal of predicted N-linked glycosylation sites in CXCR-4. We conclude that distinct virus strains interact differently with the CXCR-4 coreceptor and that the N-terminal extracellular domain is not the sole functional domain important for HIV-1 entry.

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