Abstract
Based on the findings that two cellular proteins of 45 kDa (P45) and 62 kDa (P62) serve as the putative receptor molecules for binding of HIV-1 transmembrane protein gp41 to human T, B lymphocytes and monocytes, we examined whether HIV-2 gp36 and HIV-1 gp41 share the putative receptor proteins P45 and P62. In SPR-assay (SPR: surface plasmon resonance), the recombinant soluble gp36 (rsgp36: Env aa518-678 from clone ROD) like the recombinant soluble gp41 (rsgp41: Env aa539-684 from clone BHlO) was binding to P45 and P62. By affinity capillary electrophoresis (ACE)-analysis, formation of stable rsgp36-P45 and rsgp36-P62 complexes were confirmed, and the interactions of rsgp36 with P45 and P62 is quite strong with a fast association rate and a slow dissociation rate. These results indicate that HIV-2 gp36 andHIV-1 gp41 have the common putative cellular receptor proteins P45 and P62, and the binding of gp36 to human lymphocytes and monocytes could be based on the interaction between gp36 and P45 and P62.
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