Dissociation of ligand-induced internalization of CXCR-4 from its co-receptor activity for HIV-1 Env-mediated membrane fusion
| Autor: | Chikaya Moriya, Kouji Matsushima, Y. Sakai, Toshi Shioda, Yoshiyuki Nagai, Huiling Hu, Atsushi Kato, T. Hori, Takashi Uchiyama |
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| Rok vydání: | 1998 |
| Předmět: |
Receptors
CXCR4 Chemokine Co-receptor T cell media_common.quotation_subject education Down-Regulation Ligands Membrane Fusion Polymerase Chain Reaction Cell Line Mice Chemokine receptor Virology medicine Animals Humans Internalization DNA Primers Sequence Deletion media_common Base Sequence biology Gene Products env Lipid bilayer fusion General Medicine Ligand (biochemistry) Chemokine CXCL12 Recombinant Proteins medicine.anatomical_structure Cytoplasm HIV-1 biology.protein Chemokines CXC |
| Zdroj: | Archives of Virology. 143:851-861 |
| ISSN: | 1432-8798 0304-8608 |
| DOI: | 10.1007/s007050050337 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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