HIV-gp120 can block CD4-class II MHC-mediated adhesion.
A possible component of the immune dysfunction associated with infection by HIV is the inhibition of CD4 function resulting from the avid binding of soluble HIV envelope glycoprotein (gp120) to cell surface CD4. We assessed CD4 function by measuring the ability of CD4+ T cells to form conjugates with cell size lipid vesicles, artificial target cells (ATC), bearing the natural ligand for CD4, MHC class II proteins. Conjugate formation was a transient process with the greatest number of specific cell to ATC conjugates found after approximately 30 min of incubation at 37 degrees C. Addition of gp120 specifically blocked conjugates between CD4+ cells and class II ATC in a concentration-dependent manner. These data indicate that T lymphocyte adhesion mediated by CD4 is a dynamic event and that binding of gp120 to CD4 is able to disrupt the normal progression of the interaction between CD4+ T lymphocytes and class II+ APC.
Rosenstein
Y
Y
Division of Pediatric Oncology, Dana-Farber Cancer Institute, Boston, MA.
Burakoff
S J
SJ
Herrmann
S H
SH
D015704:CD4 Antigens / Q000378:metabolism*; D015496:CD4-Positive T-Lymphocytes / Q000166:cytology*; D002448:Cell Adhesion / Q000187:drug effects; D015699:HIV Envelope Protein gp120 / Q000378:metabolism / Q000494:pharmacology*; D006681:HLA-D Antigens / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D008285:Major Histocompatibility Complex; D008954:Models, Biological; D011485:Protein Binding
D015704:CD4 Antigens; D015699:HIV Envelope Protein gp120; D006681:HLA-D Antigens