Stimulation of human leukocytes by protein II+ gonococci is mediated by lectin-like gonococcal components

Rest, Richard F.; Lee, N; Bowden, C

doi:10.1128/iai.50.1.116-122.1985

Cited by 39 publications

(27 citation statements)

References 58 publications

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“…Selection for Opa+ Gc occurs in naturally and experimentally infected individuals and in the female mouse genital tract (James and Swanson, ; Jerse, ; Cole et al ., ; Hobbs et al ., ). However, Opa+ Gc is more readily killed by PMNs (Rest et al ., 1982; 1985; Virji and Heckels, ; Fischer and Rest, ; Rest and Shafer, ; Sarantis and Gray‐Owen, ; Criss et al ., ; Ball and Criss, ). Therefore, Opa protein expression would be both advantageous and disadvantageous during gonorrhoeal infection.…”

Section: Discussionmentioning

confidence: 99%

“…Together, these results would suggest there is a disadvantage to Gc expressing CEACAM‐binding Opa proteins during infection. In support of this notion, Opa+ Gc have decreased survival compared with Opa− Gc in human PMNs (Rest et al ., 1982; 1985; Virji and Heckels, ; Fischer and Rest, ; Rest and Shafer, ; Sarantis and Gray‐Owen, ; Criss et al ., ; Ball and Criss, ). However, the precise mechanism leading to this survival defect is not yet defined.…”

Section: Introductionmentioning

confidence: 99%

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Opa+Neisseria gonorrhoeaeexhibits reduced survival in human neutrophils via Src family kinase-mediated bacterial trafficking into mature phagolysosomes

et al. 2014

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Summary During gonorrheal infection, there is a heterogeneous population of Neisseria gonorrhoeae (Gc) varied in their expression of opacity-associated (Opa) proteins. While Opa proteins are important for bacterial attachment and invasion of epithelial cells, Opa+ Gc has a survival defect after exposure to neutrophils. Here, we use constitutively Opa- and OpaD+ Gc in strain background FA1090 to show that Opa+ Gc is more sensitive to killing inside adherent, chemokine-treated primary human neutrophils due to increased bacterial residence in mature, degradative phagolysosomes that contain primary and secondary granule antimicrobial content. Although Opa+ Gc stimulates a potent oxidative burst, neutrophil killing of Opa+ Gc was instead attributable to non-oxidative components, particularly neutrophil proteases and the bactericidal/permeability-increasing protein. Blocking interaction of Opa+ Gc with carcinoembryonic antigen-related cell adhesion molecules (CEACAMs) or inhibiting Src family kinase signaling, which is downstream of CEACAM activation, enhanced the survival of Opa+ Gc in neutrophils. Src family kinase signaling was required for fusion of Gc phagosomes with primary granules to generate mature phagolysosomes. Conversely, ectopic activation of Src family kinases or coinfection with Opa+ Gc resulted in decreased survival of Opa- Gc in neutrophils. From these results, we conclude that Opa protein expression is an important modulator of Gc survival characteristics in neutrophils by influencing phagosome dynamics and thus bacterial exposure to neutrophils’ full antimicrobial arsenal.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Opa+Neisseria gonorrhoeaeexhibits reduced survival in human neutrophils via Src family kinase-mediated bacterial trafficking into mature phagolysosomes

et al. 2014

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“…If CEACAM1 is participating in the interaction of gonococci with neutrophils, the neutrophils should also phagocytose the Opa À gonococci. But, it is well-known that neutrophils mainly phagocytose Opa þ gonococci but not Opa À gonococci [4,7,22,[29][30][31]. Our explanation is that CEACAM1 is an inhibitory receptor that contains an immunoreceptor tyrosine-based inhibition motif (ITIM) [32].…”

Section: Discussionmentioning

confidence: 99%

Retinoic acid treated HL60 cells express CEACAM1 (CD66a) and phagocytoseNeisseria gonorrhoeae

Pantelic¹,

Chen²,

Parker³

et al. 2004

FEMS Immunology &Amp; Medical Microbiology

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Neisseria gonorrhoeae (gonococci, GC) are phagocytosed by neutrophils through the interaction between opacity proteins (Opa) and the CEA (CD66) family of antigens. In order to study this interaction, we used the human myeloid leukemia HL60 cell line, which differentiates into granulocyte-like cells upon treatment with dimethylsulfoxide (DMSO) or retinoic acid (RA). We found that RA-, but not DMSO- or untreated-HL60 cells, can phagocytose OpaI-expressing gonococci as well as Escherichia coli. The interaction of OpaI E. coli with RA-treated HL60 cells was inhibited by antibodies against CEACAM1. Phagocytosis of OpaI E. coli was found to be a result of the expression of CEACAM1 in RA-treated HL60 cells. Our results indicate that the level of expression of CEACAM1 in HL60 cells can be regulated by treatment with RA in a differentiation-dependent manner, and that this is important for phagocytosis of OpaI-expressing gonococci or E. coli.

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“…Other studies have found that lectins, either on the bacterial cell wall or on the phagocyte, may mediate bacterial attachment and phagocytosis (5,15,17,19,29,30). For example, fimbriae from Escherichia coli (30) and the outer membrane of N. gonorrhoeae (35) appear to contain lectins which bind sugars on the phagocyte membrane and stimulate phagocytic activity.…”

Section: Discussionmentioning

confidence: 99%

Opsonic effect of jacalin and human immunoglobulin A on type II group B streptococci

1990

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This study examined the effect of immunoglobulin A (IgA) and the IgA-binding lectin jacalin on the phagocytosis of type II group B streptococci (GBS). Strains possessing the trypsin-sensitive and trypsinresistant components of the c protein (II/c) and type II GBS lacking the c protein (II) were examined by radiolabeled bacterial uptake, bactericidal assays, and electron microscopy. Type II/c GBS resisted phagocytosis by monocytes (4.9% ± 0.8% uptake, mean + SE, n = 25) compared with type II GBS (8.5% ± 1.4% uptake, n = 14, P = 0.03). Phagocytic killing by polymorphonuclear leukocytes was also less for the type II/c strain 78-471 than for the type II strain 79-176 (68% ± 5% versus 86% ± 4% reduction in CFU at 45 min, P = 0.03). IgA binding did not explain the resistance of type II/c GBS to phagocytosis. The uptake of type II/c GBS was not significantly different after opsonization in cord sera lacking endogenous IgA (5.93% ± 1.4%) than in the same cord sera after addition of exogenous IgA (5.48% ± 1.4%, P = 0.69, n = 9). Attempts to remove serum IgA with the IgA-binding lectin jacalin resulted in the binding of IgA-jacalin complexes to 1I/c GBS. This combination of nonspecific IgA and jacalin increased uptake of II/c GBS from 4.9% ± 0.8% to 11.8% ± 1.9% (P = 0.002). Jacalin also combined with specific, immune, monoclonal IgA bound to the surface of Haemophilus influenzae and promoted the uptake of these bacteria. Jacalin and IgA mediated phagocytosis of II/c GBS via receptors that were not dependent on divalent cations and that were not modulated by plating monocytes on antigen-antibody complexes.

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Stimulation of human leukocytes by protein II+ gonococci is mediated by lectin-like gonococcal components

Cited by 39 publications

References 58 publications

Opa+Neisseria gonorrhoeaeexhibits reduced survival in human neutrophils via Src family kinase-mediated bacterial trafficking into mature phagolysosomes

Opa+Neisseria gonorrhoeaeexhibits reduced survival in human neutrophils via Src family kinase-mediated bacterial trafficking into mature phagolysosomes

Retinoic acid treated HL60 cells express CEACAM1 (CD66a) and phagocytoseNeisseria gonorrhoeae

Opsonic effect of jacalin and human immunoglobulin A on type II group B streptococci

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