Cell surface expression of several species of human immunodeficiency virus type 1 major core protein.

1989 ◽  
Vol 63 (9) ◽  
pp. 4074-4078 ◽  
Author(s):  
A G Laurent ◽  
B Krust ◽  
M A Rey ◽  
L Montagnier ◽  
A G Hovanessian
2009 ◽  
Vol 83 (24) ◽  
pp. 13032-13036 ◽  
Author(s):  
Mariana G. Bego ◽  
Mathieu Dubé ◽  
Johanne Mercier ◽  
Éric A. Cohen

ABSTRACT The human immunodeficiency virus type 1 (HIV-1) accessory protein Vpu enhances virus particle release by counteracting a host factor that retains virions at the surfaces of infected cells. It was recently demonstrated that cellular protein BST-2/CD317/Tetherin restricts HIV-1 release in a Vpu-dependent manner. Calcium-modulating cyclophilin ligand (CAML) was also proposed to be involved in this process. We investigated whether CAML is involved in cell surface expression of Tetherin. Here, we show that CAML overexpression in permissive Cos-7 cells or CAML depletion in restrictive HeLa cells has no effect on HIV-1 release or on Tetherin surface expression, indicating that CAML is not required for Tetherin-mediated restriction of HIV-1 release.


1998 ◽  
Vol 72 (11) ◽  
pp. 9054-9060 ◽  
Author(s):  
Scott G. Kitchen ◽  
Yael D. Korin ◽  
Michael D. Roth ◽  
Alan Landay ◽  
Jerome A. Zack

ABSTRACT Human immunodeficiency virus type 1 (HIV-1) infection requires cell surface expression of CD4. Costimulation of CD8+/CD4− T lymphocytes by anti-CD3 and anti-CD28 antibodies or by allogeneic dendritic cells induced expression of CD4 and rendered these CD8 cells susceptible to HIV-1 infection. Naive CD45RA+ cells responded with greater expression of CD4 than did CD45RO+ cells. CD8+lymphocytes derived from fetal or newborn sources exhibited a greater tendency to express CD4, consistent with their naive states. This mechanism of infection suggests HIV-induced perturbation of the CD8 arm of the immune response and could explain the generally rapid disease progression seen in HIV-infected children.


2001 ◽  
Vol 75 (11) ◽  
pp. 5263-5276 ◽  
Author(s):  
Andreas Bültmann ◽  
Walter Muranyi ◽  
Brian Seed ◽  
Jürgen Haas

ABSTRACT During synthesis and export of protein, the majority of the human immunodeficiency virus type 1 (HIV-1) Env glycoprotein gp160 is retained in the endoplasmic reticulum (ER) and subsequently ubiquitinated and degraded by proteasomes. Only a small fraction of gp160 appears to be correctly folded and processed and is transported to the cell surface, which makes it difficult to identify negative sequence elements regulating steady-state surface expression of Env at the post-ER level. Moreover, poorly localized mRNA retention sequences inhibiting the nucleocytoplasmic transport of viral transcripts interfere with the identification of these sequence elements. Using two heterologous systems with CD4 or immunoglobulin extracellular/transmembrane domains in combination with the gp160 cytoplasmic domain, we were able to identify two membrane-distal, neighboring motifs, is1 (amino acids 750 to 763) andis2 (amino acids 764 to 785), which inhibited surface expression and induced Golgi localization of the chimeric proteins. To prove that these two elements act similarly in the homologous context of the Env glycoprotein, we generated a synthetic gp160 gene with synonymous codons, the transcripts of which are not retained within the nucleus. In accordance with the results in heterologous systems, an internal deletion of both elements considerably increased surface expression of gp160.


2003 ◽  
Vol 71 (11) ◽  
pp. 6668-6671 ◽  
Author(s):  
W. Evan Secor ◽  
Amil Shah ◽  
Pauline M. N. Mwinzi ◽  
Bryson A. Ndenga ◽  
Caroline O. Watta ◽  
...  

ABSTRACT Distribution of chemokine receptors CCR5 and CXCR4, which are also coreceptors for human immunodeficiency virus type 1 invasion of cells, was measured on the surfaces of CD4+ T cells and monocytes in peripheral blood samples from a group of Kenyan car washers. Patients with active schistosomiasis displayed higher cell surface densities of these receptors than did cured schistosomiasis patients.


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