Complement mediates human immunodeficiency virus type 1 infection of a human T cell line in a CD4- and antibody-independent fashion.

Boyer, Véronique; Des̀granges, Claude; Trabaud, Mary‐Anne; Fischer, Elizabeth; Kazatchkine, Michel D.

doi:10.1084/jem.173.5.1151

Cited by 114 publications

(59 citation statements)

References 42 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In seminal fluid from healthy individuals, concentrations of C3 are low (< 1 mg/dl), but elevated levels orC3 are found in seminal fluid from individuals with prostatic infection which is common in promiscuous homosexual and heterosexual men [28]. Isolated HIV particles can activate complement by the classical pathway [29] and to a lesser extent by the alternative pathway [30]. Complement activation in seminal fluid may therefore lead to deposition of C3b on the surface of virus particles which are free or bound by antibody.…”

Section: Discussionmentioning

confidence: 99%

Investigation of the complement receptor 3 (CD11b/CD18) in human rectal epithelium

Hussain

Kelly

Rodin

et al. 1995

Clinical and Experimental Immunology

View full text Add to dashboard Cite

SUMMARY Rectal and cervicovaginal mucosa are common routes of transmission of HIV, although the mechanism of transmission is unknown. We have investigated human rectal and cervicovaginal epithelia for the expression of complement receptors (CR) and cell adhesion molecules which may be involved in HIV and other infections. In rectal mucosa, CR3 was detected in the surface and crypt epithelial cells by immunohistology, using MoAbs to CD18 and CD11b in 10 out of 15 specimens. RNA transcripts encoding both CD11b and CD18 were also demonstrated in surface and crypt epithelial cells by in situ hybridization. Although CD11b was detected in the epithelial cells in three out of the 14 cervicovaginal specimens, we were unable to detect CD 18. We suggest that expression of the CD11b/CD18 heterodimer might facilitate transmission of HIV by enhancing binding of HIV–antibody complexes in seminal fluid to epithelial cells. Alternatively, since intercellular adhesion molecule‐1 (ICAM‐1) is a receptor for CD11b/CD18, this may promote adhesion between epithelial cells and HIV‐infected mononuclear cells in seminal fluid.

show abstract

Section: Discussionmentioning

confidence: 99%

Investigation of the complement receptor 3 (CD11b/CD18) in human rectal epithelium

Hussain

Kelly

Rodin

et al. 1995

Clinical and Experimental Immunology

View full text Add to dashboard Cite

show abstract

“…uman immunodeficiency virus infection results in the activation of the complement system even in the absence of HIV-specific Abs (1), which results in deposition of C3 fragments on the viral surface both in vitro (2,3) and in vivo (4). HIV bound extracellularly to the follicular dendritic cells (FDC) 3 in germinal centers of lymph nodes represent by far the largest viral reservoir in HIV-infected individuals (5,6).…”

mentioning

confidence: 99%

Factor I-Mediated Processing of Complement Fragments on HIV Immune Complexes Targets HIV to CR2-Expressing B Cells and Facilitates B Cell-Mediated Transmission of Opsonized HIV to T Cells

Bánki

Wilflingseder

Ammann

et al. 2006

The Journal of Immunology

View full text Add to dashboard Cite

Our study demonstrates that binding of complement-opsonized HIV to complement receptor type 1 on human erythrocytes (E) via C3b fragments is followed by a rapid normal human serum-mediated detachment of HIV from E. The release was dependent on the presence of factor I indicating a conversion of C3b fragments to iC3b and C3d on the viral surface. This in turn resulted in an efficient binding of opsonized HIV to CR2-expressing B cells, thus facilitating B cell-mediated transmission of HIV to T cells. These data provide a new dynamic view of complement opsonization of HIV, suggesting that association of virus with E might be a transient phenomenon and the factor I-mediated processing of C3b to iC3b and C3d on HIV targets the virus to complement receptor type 2-expressing cells. Thus, factor I in concert with CR1 on E and factor H in serum due to their cofactor activity are likely to be important contributors for the generation of C3d-opsonized infectious HIV reservoirs on follicular dendritic cells and/or B cells in HIV-infected individuals.

show abstract

“…One particularly relevant outcome of this activity is the retention on FDC of highly infectious HIV-1 present as C3-bound immune complexes (31,32) that can be released from germinal centers in vitro by inhibition of C3-CR2 binding (33). CR2-expressing thymocytes and peripheral T cells can also be infected with HIV-1 immune complexes containing C3 ligands through this receptor (34,35). In addition, freshly isolated peripheral blood and lymph node B cells from HIV-infected patients who are chronically viremic have also been shown to efficiently transfer CR2-bound immune complexes containing HIV-1 from their surface and infect naive T cells using a CD4-dependent mechanism (36).…”

mentioning

confidence: 99%

Epitope Mapping Using the X-Ray Crystallographic Structure of Complement Receptor Type 2 (CR2)/CD21: Identification of a Highly Inhibitory Monoclonal Antibody That Directly Recognizes the CR2-C3d Interface

Guthridge

Young

Gipson

et al. 2001

The Journal of Immunology

View full text Add to dashboard Cite

Complement receptor type 2 (CR2)/CD21 is a B lymphocyte cell membrane C3d/iC3b receptor that plays a central role in the immune response. Human CR2 is also the receptor for the EBV viral membrane glycoprotein gp350/220. Both C3d and gp350/220 bind CR2 within the first two of 15–16 repetitive domains that have been designated short consensus/complement repeats. Many mAbs react with human CR2; however, only one currently available mAb is known to block both C3d/iC3b and gp350/220 binding. We have used a recombinant form of human CR2 containing the short consensus/complement repeat 1-2 ligand-binding fragment to immunize Cr2−/− mice. Following fusion, we identified and further characterized four new anti-CR2 mAbs that recognize this fragment. Three of these inhibited binding of CR2 to C3d and gp350/220 in different forms. We have determined the relative inhibitory ability of the four mAbs to block ligand binding, and we have used overlapping peptide-based approaches to identify linear epitopes recognized by the inhibitory mAbs. Placement of these epitopes on the recently solved crystal structure of the CR2-C3d complex reveals that each inhibitory mAb recognizes a site either within or adjacent to the CR2-C3d contact site. One new mAb, designated 171, blocks CR2 receptor-ligand interactions with the greatest efficiency and recognizes a portion of the C3d contact site on CR2. Thus, we have created an anti-human CR2 mAb that blocks the C3d ligand by direct contact with its interaction site, and we have provided confirmatory evidence that the C3d binding site seen in its crystal structure exists in solution.

show abstract

Complement mediates human immunodeficiency virus type 1 infection of a human T cell line in a CD4- and antibody-independent fashion.

Cited by 114 publications

References 42 publications

Investigation of the complement receptor 3 (CD11b/CD18) in human rectal epithelium

Investigation of the complement receptor 3 (CD11b/CD18) in human rectal epithelium

Factor I-Mediated Processing of Complement Fragments on HIV Immune Complexes Targets HIV to CR2-Expressing B Cells and Facilitates B Cell-Mediated Transmission of Opsonized HIV to T Cells

Epitope Mapping Using the X-Ray Crystallographic Structure of Complement Receptor Type 2 (CR2)/CD21: Identification of a Highly Inhibitory Monoclonal Antibody That Directly Recognizes the CR2-C3d Interface

Contact Info

Product

Resources

About