Synergism between HIV gp120 and gp120-specific antibody in blocking human T cell activation Journal Article
| Authors: | Mittler, R. S.; Hoffmann, M. K. |
| Article Title: | Synergism between HIV gp120 and gp120-specific antibody in blocking human T cell activation |
| Abstract: | The human immunodeficiency virus (HIV) binds to CD4-positive cells through interaction of its envelope glycoprotein (gp120) with the CD4 molecule. CD4 is a prominent immunoregulatory molecule, and chronic exposure to antibody against CD4 (anti-CD4) has been shown to cause immunodeficiency in mice. T cell-dependent in vitro immune responses can also be inhibited by anti-CD4. Experimental findings reported here indicate that CD4-bound gp120 attracts gp120-specific antibodies derived from the blood of HIV-seropositive individuals to form a trimolecular complex with itself and CD4. Thus targeted to CD4, the gp120-specific antibody functions as an antibody to CD4; it cross-links and modulates the CD4 molecules and suppresses the activation of T cells as measured by mobilization of intracellular calcium (Ca2+). The synergism between gp120 and anti-gp120 in blocking T cell activation occurs at low concentrations of both components. Neither gp120 nor anti-gp120 inhibits T cell activation by itself in the concentrations tested. |
| Keywords: | human cell; human immunodeficiency virus infection; calcium; lymphocyte activation; receptors, antigen, t-cell; cd4-positive t-lymphocytes; acquired immunodeficiency syndrome; cd4 antigen; t lymphocyte activation; hiv; antigen-antibody reactions; antigens, differentiation, t-lymphocyte; hiv antibodies; hiv envelope protein gp120; viral envelope proteins; dose-response relationship, immunologic; glycoprotein gp 120; human; priority journal; human immunodeficiency virus antibody; hiv antigens; retroviridae proteins; immunologic capping |
| Journal Title: | Science |
| Volume: | 245 |
| Issue: | 4924 |
| ISSN: | 0036-8075 |
| Publisher: | American Association for the Advancement of Science |
| Date Published: | 1989-09-22 |
| Start Page: | 1380 |
| End Page: | 1382 |
| Language: | English |
| DOI: | 10.1126/science.2571187 |
| PUBMED: | 2571187 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Article -- Export Date: 14 April 2020 -- Source: Scopus |
