منابع مشابه
b-Chemokine MDC and HIV-1 Infection
The human immunodeficiency virus type–1 (HIV-1) uses the chemokine receptors CCR5 or CXCR4 (in conjunction with CD4) to enter healthy cells, and the chemokine ligands to these receptors generally block virus infection (1–3). R. Pal et al. studied a truncated form of the b-chemokine macrophage-derived chemokine (MDC), which lacked the first two NH2-terminal amino acids [(22)MDC] that they purifi...
متن کاملInhibition of HIV-1 infection by a CCR5-binding cyclophilin from Toxoplasma gondii.
The activation of murine dendritic cells by Toxoplasma gondii has recently been shown to depend on a parasite protein that signals through the chemokine receptor CCR5. Here we demonstrate that this molecule, cyclophilin-18 (C-18), is an inhibitor of HIV-1 cell fusion and infection with cell-free virus. T gondii C-18 efficiently blocked syncytium formation between human T cells and effector cell...
متن کاملCD147 facilitates HIV-1 infection by interacting with virus-associated cyclophilin A.
Cyclophilin A (CyPA) is specifically incorporated into the virions of HIV-1 and has been shown to enhance significantly an early step of cellular HIV-1 infection. Our preliminary studies implicated CD147 as a receptor for extracellular CyPA. Here, we demonstrate a role for CyPA-CD147 interaction during the early steps of HIV-1 infection. Expression of human CD147 increased infection by HIV-1 un...
متن کاملComputer-assisted anti-AIDS drug development: cyclophilin B against the HIV-1 subtype A V3 loop
Aim: The objects of this study originated from the experimental observations, whereby the HIV -1 gp120 V3 loop is a high-affinity ligand for immunophilins, and consisted in generating the structural complex of cyclophilin (Cyc) B belonging to immunophilins family with the virus subtype A V3 loop (SA-V3 loop) as well as in specifying the Cyc B segment forming the binding site for V3 synthetic co...
متن کاملA Cyclophilin Homology Domain-Independent Role for Nup358 in HIV-1 Infection
The large nucleoporin Nup358/RanBP2 forms eight filaments that project from the nuclear pore into the cytoplasm where they function as docking platforms for nucleocytoplasmic transport receptors. RNAi screens have implicated Nup358 in the HIV-1 life cycle. The 164 C-terminal amino acids of this 3,224 amino acid protein are a cyclophilin homology domain (Nup358Cyp), which has potential to bind t...
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ژورنال
عنوان ژورنال: Virology
سال: 2016
ISSN: 0042-6822
DOI: 10.1016/j.virol.2015.12.015