Dissociation of ligand-induced internalization of CXCR-4 from its co-receptor activity for HIV-1 Env-mediated membrane fusion
Copyright policy )Dissociation of ligand-induced internalization of CXCR-4 from its co-receptor activity for HIV-1 Env-mediated membrane fusion
The C-terminal cytoplasmic tail of chemokine receptors is important for their internalization upon ligand binding. We generated several deletion mutants of the C-terminal cytoplasmic tail of CXCR-4, a co-receptor for T cell line tropic strains of human immunodeficiency virus type 1 (HIV-1), to know whether or not co-receptor internalization is associated with HIV-1 entry. Our data showed that the removal of C-terminal 15 amino acid residues of the cytoplasmic tail from CXCR-4 completely abolished its internalization, but did not affect the co-receptor activity at all. Co-receptor activity was fully retained even when all 45 amino acid residues in the C-terminal cytoplasmic tail had been deleted. These data indicated that no cytoplasmic tail nor internalization of CXCR-4 is required for its co-receptor activity for HIV-1 entry.
- Kyoto University Japan
- University of Tokyo Japan
Receptors, CXCR4, Base Sequence, Down-Regulation, Gene Products, env, Ligands, Membrane Fusion, Polymerase Chain Reaction, Chemokine CXCL12, Recombinant Proteins, Cell Line, Mice, HIV-1, Animals, Humans, Chemokines, CXC, DNA Primers, Sequence Deletion
Receptors, CXCR4, Base Sequence, Down-Regulation, Gene Products, env, Ligands, Membrane Fusion, Polymerase Chain Reaction, Chemokine CXCL12, Recombinant Proteins, Cell Line, Mice, HIV-1, Animals, Humans, Chemokines, CXC, DNA Primers, Sequence Deletion
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