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Opsonization of Four Bacteroides Species: Role of the Classical Complement Pathway and Immunoglobulin

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Journal Infect Immun
Date 1980 Mar 1
PMID 6103873
Citations 26
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Abstract

Previous investigators have suggested that opsonization of two Bacteroides species is mediated exclusively by the alternative complement pathway and requires immunoglobulins. In this study, the nature of the opsonic factors in nonimmune human serum for four species of Bacteroides was investigated by measuring uptake of [(3)H]thymidine-labeled bacteria by human polymorphonuclear leukocytes. Normal human serum, C2-deficient serum, immunoglobulin-deficient serum, and serum chelated with ethylene glycol-bis(beta-aminoethyl ether)-N,N-tetraacetic acid (EGTA), MgEGTA, and ethylenediaminetetraacetic acid (EDTA) were used as opsonic sources. Heat inactivation of each of these sera significantly reduced its opsonic activity for all four Bacteroides species, suggesting that serum complement was essential for effective opsonization. All strains were opsonized in the absence of the classical complement pathway; however, kinetics studies revealed that opsonization proceeded at a significantly faster rate when the classical complement pathway was intact. Although two strains were opsonized in immunoglobulin-deficient sera, opsonization was less efficient and appeared to occur via the alternative complement pathway. Unexpectedly, all strains were well opsonized by the classical complement pathway in 10% serum which had been effectively chelated with EGTA or EDTA. The explanation for this finding is unknown; however, it is possible that cell wall cations of Bacteroides species may participate in the activation of complement in chelated serum, resulting in effective opsonization. It was also found that Bacteroides, when incubated with an Escherichia coli strain in normal serum, could compete for opsonins and thereby reduce phagocytosis of E. coli. It is possible that competition for opsonins among bacterial species contributes to the synergistic role these organisms share in mixed floral infections.

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References
1.
Williams Jr R, Quie P . Opsonic activity of agammaglobulinemic human sera. J Immunol. 1971; 106(1):51-5. View

2.
Sandberg A, OSLER A . Dual pathways of complement interaction with guinea pig immunoglobulins. J Immunol. 1971; 107(5):1268-73. View

3.
Washington 2nd J . Comparison of two commercially available media for detection of bacteremia. Appl Microbiol. 1971; 22(4):604-7. PMC: 376371. DOI: 10.1128/am.22.4.604-607.1971. View

4.
Anderson P, JOHNSTON Jr R, Smith D . Human serum activities against Hemophilus influenzae, type b. J Clin Invest. 1972; 51(1):31-8. PMC: 332925. DOI: 10.1172/JCI106793. View

5.
Johnson F, Agnello V, Williams Jr R . Opsonic activity in human serum deficient in C2. J Immunol. 1972; 109(1):141-5. View