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T20/DP178, an ectodomain peptide of human immunodeficiency virus type 1 gp41, is an activator of human phagocyte N-formyl peptide receptor.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Gong, Wang Hua Gao, Ji-Liang Shen, W. P. Grimm, M. C. Deng, Xingming Murphy, Philip M. Oppenheim, Joost J. Wang, Ji ming |
| Copyright Year | 1999 |
| Abstract | Human immunodeficiency virus type 1 (HIV-1) envelope protein gp41 mediates viral fusion with human host cells. The peptide segment T20/DP178, located in the C-terminus of the ectodomain of gp41, interacts with the N-terminal leucine zipper-like domain on gp41 to establish the fusogenic conformation of the virus. Synthetic T20/DP178 peptide is highly efficacious in inhibiting HIV-1 infection in vitro by disrupting the transformation of fusogenic status of viral gp41; thus, it has been proposed for clinical trial. We report that synthetic T20/DP178 is a chemoattractant and activator of human peripheral blood phagocytes but not of T lymphocytes. We further demonstrate that T20/DP178 specifically activates a seven-transmembrane, G-protein-coupled phagocyte receptor for N-formylated chemotactic peptides, formyl peptide receptor (FPR). Moreover, synthetic T20/DP178 analogs lacking N-terminal amino acids acted as FPR antagonists. Our results suggest that gp41 peptides regulate phagocyte function via FPR and identify a novel mechanism by which HIV-1 may modulate innate immunity. |
| File Format | PDF HTM / HTML |
| DOI | 10.1182/blood.V93.11.3885.411k19_3885_3892 |
| PubMed reference number | 10339497 |
| Journal | Medline |
| Volume Number | 93 |
| Issue Number | 11 |
| Alternate Webpage(s) | http://www.bloodjournal.org/content/bloodjournal/93/11/3885.full.pdf?sso-checked=true |
| Alternate Webpage(s) | https://doi.org/10.1182/blood.V93.11.3885.411k19_3885_3892 |
| Journal | Blood |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |