Role of Escherichia coli K capsular antigens during complement activation, C3 fixation, and opsonization

Dijk, W. C. van; Verbrugh, Henri A.; Tol, M. E. Van Der; Peters, R.C.; Verhoef, J.

doi:10.1128/iai.25.2.603-609.1979

Cited by 65 publications

(27 citation statements)

References 28 publications

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“…A previous report about the phagocytosis and oxidative burst in isolated human granulocytes stimulated with zymosan particles also supports the critical role of C3 opsonization and CD11b [36]. It is interesting that E. coli strains with K capsular polysaccharides, which activated complement at a slow rate, were opsonized ineffectively by C3 and were resistant to phagocytosis of human granulocytes, further supporting the important role of C3 opsonization [9].…”

Section: Discussionsupporting

confidence: 53%

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The role of complement C3 opsonization, C5a receptor, and CD14 inE. coli-induced up-regulation of granulocyte and monocyte CD11b/CD18 (CR3), phagocytosis, and oxidative burst in human whole blood

Brekke

Christiansen

Fure

et al. 2007

Journal of Leukocyte Biology

105

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The relative role of complement and CD14 in Escherichia coli-induced leukocyte CD11b up-regulation, phagocytosis, and oxidative burst in human whole blood was examined. The highly specific thrombin inhibitor lepirudin was used as anticoagulant, as it does not affect complement activation. Complement inhibition at the level of C3 (anti-C2 and anti-factor D) and C5 (C5a receptor antagonist and anti-C5/C5a) efficiently inhibited CD11b up-regulation, phagocytosis, and oxidative burst in granulocytes. Monocyte activation was generally less complement-dependent, but when C3 activation was blocked, a pronounced inhibition of phagocytosis and oxidative burst was obtained. Only the combination of anti-C2 and antifactor D blocked E. coli C3 opsonization completely. Whole E. coli, disrupted E. coli, and the C3-convertase activator cobra venom factor upregulated CD11b rapidly on both cell types, proportional to their complement activation potential in the fluid phase. In comparison, purified LPS at concentrations comparable with that present in the E. coli preparations did not activate complement. Oxidative burst was induced only by whole bacteria. Finally, the combination of complement inhibition and anti-CD14 completely blocked E. coliinduced granulocyte and monocyte CD11b up-regulation and quantitatively, virtually abolished phagocytosis. The results indicate that complement and CD14, despite differential effects on granulocytes and monocytes, are the two crucial, quantitative factors responsible for E. coli-induced CD11b, phagocytosis, and oxidative burst in both cell types.

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Section: Discussionsupporting

confidence: 53%

“…E. coli entering the bloodstream are opsonized rapidly by complement including C1q, mannose-binding lectin (MBL), C4b, and C3b/iC3b [8], in addition to Igs [9]. The terminal C5b-9 complex (TCC) induces lysis of certain complementsensitive bacterial strains.…”

Section: Introductionmentioning

confidence: 99%

The role of complement C3 opsonization, C5a receptor, and CD14 inE. coli-induced up-regulation of granulocyte and monocyte CD11b/CD18 (CR3), phagocytosis, and oxidative burst in human whole blood

Brekke

Christiansen

Fure

et al. 2007

Journal of Leukocyte Biology

105

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“…By interrupting the C3 amplification loop, sialic acid prevents the efficient activation of the alternative pathway and limits C3 deposition on the particle surface. Evidence for regulation of alternative-pathway activation by capsular sialic acid has been presented for Escherichia coli Kl, GBS type III, and group B Neisseria meningitidis (5,12,21).…”

Section: -mentioning

confidence: 99%

Prevention of C3 deposition by capsular polysaccharide is a virulence mechanism of type III group B streptococci

et al. 1992

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Strains of type III group B streptococci isolated from patients with neonatal sepsis are generally resistant to complement-mediated phagocytic killing in the absence of specific antibody. It has been suggested that the resistance of type HI group B streptococci to phagocytosis results from inhibition of alternative-complementpathway activation by sialic acid residues of the type III polysaccharide. To better define the relationship between structural features of the type III capsule and resistance of type III group B streptococci to complement-mediated phagocytic killing, we measured deposition of human C3 on group B streptococcal strains with altered capsule phenotypes. C3 binding was quantified by incubating bacteria with purified human 12511C3 in 10% senrm. Wild-type group B Streptococcus sp. strain COH1 bound eightfold fewer C3 molecules than did either of two isogenic mutant strains, one expressing a sialic acid-deficient capsule and the other lacking capsule completely. Similar results were obtained when the incubation with 12-I-C3 was performed in serum chelated with Mg-ethylene glycol-bis(3-aminoethyl ether)-N,NN',N'-tetraacetic acid (MgEGTA), suggesting that the majority of C3 deposition occurred via the alternative pathway. In contrast to the wild-type strain, which was relatively resistant, both mutant strains were killed by human leukocytes in 10%/1 serum with or without MgEGTA. We also measured C3 binding to 14 wild-type strains of type IH group B streptococci expressing various amounts of capsule. Comparison of degree of encapsulation with C3 binding revealed a significant inverse correlation (r = -0.72; P < 0.01). C3 fagments released by methylamine treatment of wild-type strain COH1 were predominantly in the form of C3bi, while those released from the acapsular mutant were predominantly C3b and those from the asialo mutant represented approximately equal amounts of C3b and C3bi. We conclude from these studies that the sialylated type III capsular polysaccharide inhibits alternative-pathway activation, prevents C3 deposition on group B streptococci, and protects the organisms from phagocytic killing.

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“…The importance of the somplement cascade for opsonization of the yeast cell led us to examine strain variation in activation and deposition of C3 fragments onto the yeast cells. Our studies were guided by three models for inhibition of vation and binding of C3 fragments onto the yeast cell (13,14,27). Second, phagocytosis-resistant strains might bind C3 fragments at sites beneath the capsular surface, where the opsonic ligands would be spatially unavailable for interaction with phagocyte complement receptors (28,30,31).…”

mentioning

confidence: 99%

Strain variation in phagocytosis of Cryptococcus neoformans: dissociation of susceptibility to phagocytosis from activation and binding of opsonic fragments of C3

et al. 1988

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Phagocytosis of Cryptococcus neoformans is markedly influenced by the presence of a polysaccharide capsule.We examined activation and binding of C3 fragments to eight isolates of C. neqformans. All isolates were shown to have capsules by light and electron microscopy. These strains differed in susceptibility to phagocytosis by neutrophils. Yeast cells were opsonized by incubation in normal human serum. Five strains were resistant to ingestion, two strains showed intermediate levels of resistance to ingestion, and one strain was quite sensitive to phagocytosis. Yeast cells opsonized with heat-inactivated serum (56°C for 30 min) neither attached nor were ingested by neutrophils. A quantitative estimate of the amount of C3 bound to the yeast cells was determined by use of normal human serum containing 1251-labeled C3. The results showed approximately 5 x 106 to 10 x 106 C3 molecules per yeast cell regardless of whether the yeast cells were sensitive or resistant to phagocytosis. Bound C3 was eluted from the yeast cells by treatment with 0.1 M NH2OH (pH 10), and the eluted fragments were examined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis under reducing conditions. Results of this analysis showed that little of the C3 was in the form of C3b, and there was substantial decay to iC3b, the inactive decay product of C3b. This pattern of decay was similar with all strains. Immunoelectron microscopy was used to assess the ultrastructural location of the C3 fragments bound to the yeast cells. C3 fragments were bound to the perimeter of the capsule regardless of whether the isolate was sensitive or resistant to phagocytosis. Thus, phagocytosis-sensitive and phagocytosis-resistant isolates were similar with regard to the amount, molecular form, and ultrastructural location of C3 fragments bound to the cryptococcal capsule. These results further indicate that activation of the complement cascade is necessary but not sufficient for phagocytosis of the yeast cell. 2794 on August 1, 2020 by guest http://iai.asm.org/ Downloaded from on August 1, 2020 by guest http://iai.asm.org/ Downloaded from

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Role of Escherichia coli K capsular antigens during complement activation, C3 fixation, and opsonization

Cited by 65 publications

References 28 publications

The role of complement C3 opsonization, C5a receptor, and CD14 inE. coli-induced up-regulation of granulocyte and monocyte CD11b/CD18 (CR3), phagocytosis, and oxidative burst in human whole blood

The role of complement C3 opsonization, C5a receptor, and CD14 inE. coli-induced up-regulation of granulocyte and monocyte CD11b/CD18 (CR3), phagocytosis, and oxidative burst in human whole blood

Prevention of C3 deposition by capsular polysaccharide is a virulence mechanism of type III group B streptococci

Strain variation in phagocytosis of Cryptococcus neoformans: dissociation of susceptibility to phagocytosis from activation and binding of opsonic fragments of C3

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