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The envelope glycoprotein of HIV‐1 gp120 and human complement protein C1q bind to the same peptides derived from three different regions of gp41, the transmembrane glycoprotein of HIV‐1, and share antigenic homology

European Journal of Immunology, 1994
AbstractGp41, the transmembrane glycoprotein of HIV‐1, has been shown to be non‐covalently associated with gp120. We have shown that it also binds human C1q. To analyze the interaction site(s) of gp41 with these two molecules, we established an enzyme‐linked immunosorbent assay (ELISA) system using recombinant soluble gp41 [amino acids (aa) 539–684 ...
H, Stoiber   +4 more
openaire   +2 more sources

T21/DP107, A Synthetic Leucine Zipper-Like Domain of the HIV-1 Envelope gp41, Attracts and Activates Human Phagocytes by Using G-Protein-Coupled Formyl Peptide Receptors

The Journal of Immunology, 1999
Abstract A leucine zipper-like domain, T21/DP107, located in the amino terminus of the ectodomain of gp41, is crucial to the formation of fusogenic configuration of the HIV-1 envelope protein gp41. We report that the synthetic T21/DP107 segment is a potent stimulant of migration and calcium mobilization in human monocytes and ...
S B, Su   +6 more
openaire   +2 more sources

P-C3 Analysis of the immunosuppressive properties of a trimeric recombinant transmembrane envelope protein gp41 of HIV-1

JAIDS Journal of Acquired Immune Deficiency Syndromes, 2017
Michael MüHle   +6 more
openaire   +1 more source

Inhibition of HIV Entry by Targeting the Envelope Transmembrane Subunit gp41

Current HIV Research, 2016
Amy Jacobs, Robert C Rizzo
exaly  

Trilobatin as an HIV-1 Entry Inhibitor Targeting the HIV-1 Gp41 Envelope

FEBS Letters, 2018
Shuwen Liu, Lin Li, Wanying Lin
exaly  

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