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Conformational HIV-1 envelope on particulate structures: a tool for chemokine coreceptor binding studies Tagliamonte M; Tornesello ML; Buonaguro FM; Buonaguro LJ Transl Med 2011[Jan]; 9 Suppl 1 (Suppl 1): S1The human immunodeficiency virus type 1 (HIV-1) external envelope glycoprotein gp120 presents conserved binding sites for binding to the primary virus receptor CD4 as well as the major HIV chemokine coreceptors, CCR5 and CXCR4. Concerted efforts are underway to understand the specific interactions between gp120 and coreceptors as well as their contribution to the subsequent membrane fusion process. The present review summarizes the current knowledge on this biological aspect, which represents one of the key and essential points of the HIV-host cell interplay and HIV life cycle. The relevance of conformational HIV-1 Envelope proteins presented on Virus-like Particles for appropriate assessment of this molecular interaction, is also discussed.|Animals[MESH]|CD4-Positive T-Lymphocytes/virology[MESH]|Chemokines/*metabolism[MESH]|Gene Products, env/*chemistry[MESH]|HIV Envelope Protein gp120/chemistry[MESH]|HIV-1/*metabolism[MESH]|Humans[MESH]|Macaca mulatta[MESH]|Protein Binding[MESH]|Protein Conformation[MESH]|Receptors, CCR5/metabolism[MESH]|Receptors, CXCR4/metabolism[MESH]|Vaccines, Virus-Like Particle/chemistry[MESH] |
