Interaction of CD4 T lymphocytes with the V3 segment of glycoprotein 120 present in the Human Immunodeficiency Virus type 1
DOI:
https://doi.org/10.54495/Rev.Cientifica.EdicionEspecial2009.179%20Keywords:
HIV-1, T lymphocytesAbstract
The entry of the human immunodeficiency virus type 1 (HIV-1) into a CD4+ Th lymphocyte is initiated by the interaction of the viral trimer gp160, which contains the glycoprotein gp120 at its end. This interacts directly with the CD4 lymphocyte receptor and subsequently the CD4-gp120 complex reacts with a co-receptor present on ThCD4+ lymphocytes. This research proposes a reaction mechanism between the glycoprotein gp120 in its V3 segment when it interacts with the second extracellular segment in the CCR5 co-receptor, for which protein-ligand binding computational programs have been used to obtain details of the existing biochemical reactions between these regions. , with these analyzes it has been possible to explain the CCR5-gp120 orientation that forms this complex. In addition, a computational molecular model has been designed that explains and is consistent with the results obtained between this investigation and previous investigations. The results found show that there are regions in the V3 segment of gp120 that interact with the second extracellular segment in CCR5, in addition to confirming the regions that interact in gp120 with the first 15 amino acids of the CCR5 co-receptor. This proposal better explains what happens in the X5, X5/R4 and R4 strains of HIV that select between different co-receptors (CXCR4 and CCR5 respectively) and suggests that there are amino acids in V3 of gp120 whose function is the specific orientation to a bond stabilized by all reaction regions between HIV-1 gp120 and the CCR5 co-receptor.
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