The role of complement receptor 3 (CR3) in<i>Neisseria gonorrhoeae</i>infection of human cervical epithelia

Edwards, Jennifer; Brown, Eric J.; Ault, Kevin A.; Apicella, Michael A.

doi:10.1046/j.1462-5822.2001.00140.x

Cited by 83 publications

(120 citation statements)

References 37 publications

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“…Several of these phenotypes mimic human cell surface structures such as gangliosides (23,55,56). Furthermore, GC LOS interacts with complement receptor 3 (CR3) from female human cervical epithelia (57,58), and the asialoglycoprotein receptor on human sperm (59). In vivo, gonococcal LOS can switch from one phenotype to another in a human challenge model (23), suggesting that different LOS phenotypes could interact with various receptors to adapt to specific host environments.…”

Section: Discussionmentioning

confidence: 99%

Role of N-Acetylglucosamine within Core Lipopolysaccharide of Several Species of Gram-Negative Bacteria in Targeting the DC-SIGN (CD209)

Zhang

Snyder

Feng

et al. 2006

The Journal of Immunology

163

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Our recent studies have shown that the dendritic cell-specific ICAM nonintegrin CD209 (DC-SIGN) specifically binds to the core LPS of Escherichia coli K12 (E. coli), promoting bacterial adherence and phagocytosis. In this current study, we attempted to map the sites within the core LPS that are directly involved in LPS-DC-SIGN interaction. We took advantage of four sets of well-defined core LPS mutants, which are derived from E. coli, Salmonella enterica serovar Typhimurium, Neisseria gonorrhoeae, and Haemophilus ducreyi and determined interaction of each of these four sets with DC-SIGN. Our results demonstrated that N-acetylglucosamine (GlcNAc) sugar residues within the core LPS in these bacteria play an essential role in targeting the DC-SIGN receptor. Our results also imply that DC-SIGN is an innate immune receptor and the interaction of bacterial core LPS and DC-SIGN may represent a primeval interaction between Gram-negative bacteria and host phagocytic cells.

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Section: Discussionmentioning

confidence: 99%

Role of N-Acetylglucosamine within Core Lipopolysaccharide of Several Species of Gram-Negative Bacteria in Targeting the DC-SIGN (CD209)

Zhang

Snyder

Feng

et al. 2006

The Journal of Immunology

163

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“…Exploitation of C3 by cell-invasive bacteria has been described with several organisms. For example, C3-opsonized Mycobacterium tuberculosis (41), Neisseria gonorrhoea (21), and the HIV (20) exhibit facilitated entry into macrophages and epithelial cells. These pathogens use surface-bound C3 to engage the classical opsonic receptors, in particular CR3.…”

Section: Discussionmentioning

confidence: 99%

“…Less is known about the ability of C3-opsonized pathogens to interact with receptors on epithelial cells, and the functional consequence of such C3-receptor-ligand interaction. Colonic and cervical epithelial cells can internalize opsonized HIV (20) and Neisseria gonorrhoea (21), respectively. This occurs through binding to CR3.…”

mentioning

confidence: 99%

CD46 (Membrane Cofactor Protein) Acts as a Human Epithelial Cell Receptor for Internalization of Opsonized Uropathogenic Escherichia coli

Feito

Sacks

et al. 2006

The Journal of Immunology

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Escherichia coli is a common urinary pathogen whose uptake into epithelial cells is mediated by attachment through type 1 fimbriae. In this study, we show by using using human urinary tract epithelial cells that maximal internalization of E. coli is achieved only when bacteria are opsonized with complement. The concentrations of complement proteins in the urine rise sufficiently during infection to allow bacterial opsonization. The complement regulatory protein, CD46 (membrane cofactor protein), acts in cohort with fimbrial adhesion to promote the uptake of pathogenic E. coli. This uptake is inhibited by RNA interference to lower the expression of CD46 and by soluble CD46 that will competitively inhibit opsonized bacteria binding to cell surface CD46. We propose that efficient internalization of uropathogenic E. coli by the human urinary tract depends on cooperation between fimbrial-mediated adhesion and C3 receptor (CD46)–ligand interaction. Complement receptor–ligand interaction could pose a new target for interrupting the cycle of reinfection due to intracellular bacteria.

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“…Edwards et al demonstrated that pili bind to Idomain-containing integrins on primary cell cultures derived from cervical and male urethral epithelia (Edwards and Apicella, 2005;Edwards et al, 2002). In this regard, the complement receptor 3 (CR3; integrin M 2 or CD11b/CD18) serves as the key receptor mediating gonococcal adherence to human cervical epithelia, in vivo, as well as ex vivo (Figure 2) (Edwards et al, 2001). Pilus engagement has also been demonstrated to play a role in host cell cytoskeletal rearrangements Grassme et al, 1996;Griffiss et al, 1999;Merz et al, 1999;Merz and So, 1997).…”

Section: Type IV Pilimentioning

confidence: 99%

“…Engagement of CR3 on primary cervical epithelial cells results in vinculin-and ezrin-enriched focal complex formation before membrane ruffle formation, bacteria reside within macropinosomes, and an accumulation of actin-associated protein occur in response to gonococcal infection . Finally a signal transduction cascade that is dependent upon the activation of phosphatidylinositol 3-kinase or MAP kinases and Rho GTPases is activated (Edwards et al, 2001). …”

Section: Type IV Pilimentioning

confidence: 99%

Mucosal Immunity and Evasion Strategies of Neisseria gonorrhoeae

Imarai¹,

Acuña²,

Escobar³

et al. 2012

Sexually Transmitted Infections

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The role of complement receptor 3 (CR3) inNeisseria gonorrhoeaeinfection of human cervical epithelia

Cited by 83 publications

References 37 publications

Role of N-Acetylglucosamine within Core Lipopolysaccharide of Several Species of Gram-Negative Bacteria in Targeting the DC-SIGN (CD209)

Role of N-Acetylglucosamine within Core Lipopolysaccharide of Several Species of Gram-Negative Bacteria in Targeting the DC-SIGN (CD209)

CD46 (Membrane Cofactor Protein) Acts as a Human Epithelial Cell Receptor for Internalization of Opsonized Uropathogenic Escherichia coli

Mucosal Immunity and Evasion Strategies of Neisseria gonorrhoeae

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