Interaction of Neisseria gonorrhoeae with classical complement components, C1-inhibitor, and a monoclonal antibody directed against the Neisserial H.8 antigen

J. E. Schweinle, P. J. Hitchcock, A. J. Tenner, C. H. Hammer, M. M. Frank, Keith A Joiner

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

Strains of Neisseria gonorrhoeae were used to evaluate bactericidal and opsonic properties of McAb 10 directed against the Neisserial outer membrane antigen, H.8. Gonococci were either serum resistant in the absence but serum sensitive in the presence, of McAb 10, or serum sensitive or serum resistant regardless of the presence of McAb 10. Strain JS3, which fell in the former category, was used in subsequent studies. C1 zymogen formed by reassociation of isolated C1 subunits was not directly activated by JS3 in the presence or absence of C1-inhibitor. JS3 thus was unable to directly activate the classical pathway independently of antibody. When purified classical pathway components were used to deposit C3 on JS3 in the absence of serum regulatory proteins or antibodies, added C1-inhibitor reduced C3 binding to background levels. When McAb 10 was present, C3 binding was unaffected by C1-inhibitor. Covalently bound, large molecular weight C3α-chain-gonococcal complexes were disbanded by methylamine release of ester linkages. Released 125I-C3 migrated as C3b without degradation by gonococcal proteases. Purified classical components alone or McAb 10 alone facilitated JS3 killing by neutrophils; when combined, the two provided maximal killing. Levels of McAb 10 that only slightly increase C3 deposition on JS3 are bacteridical in serum and maximally opsonic in combination with purified classical pathway components.

Original languageEnglish (US)
Pages (from-to)397-403
Number of pages7
JournalJournal of Clinical Investigation
Volume83
Issue number2
StatePublished - 1989
Externally publishedYes

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Complement C1
Neisseria gonorrhoeae
Monoclonal Antibodies
Antigens
Serum
Enzyme Precursors
Antibodies
Blood Proteins
Esters
Neutrophils
Peptide Hydrolases
Molecular Weight
Membranes

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Interaction of Neisseria gonorrhoeae with classical complement components, C1-inhibitor, and a monoclonal antibody directed against the Neisserial H.8 antigen. / Schweinle, J. E.; Hitchcock, P. J.; Tenner, A. J.; Hammer, C. H.; Frank, M. M.; Joiner, Keith A.

In: Journal of Clinical Investigation, Vol. 83, No. 2, 1989, p. 397-403.

Research output: Contribution to journalArticle

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abstract = "Strains of Neisseria gonorrhoeae were used to evaluate bactericidal and opsonic properties of McAb 10 directed against the Neisserial outer membrane antigen, H.8. Gonococci were either serum resistant in the absence but serum sensitive in the presence, of McAb 10, or serum sensitive or serum resistant regardless of the presence of McAb 10. Strain JS3, which fell in the former category, was used in subsequent studies. C1 zymogen formed by reassociation of isolated C1 subunits was not directly activated by JS3 in the presence or absence of C1-inhibitor. JS3 thus was unable to directly activate the classical pathway independently of antibody. When purified classical pathway components were used to deposit C3 on JS3 in the absence of serum regulatory proteins or antibodies, added C1-inhibitor reduced C3 binding to background levels. When McAb 10 was present, C3 binding was unaffected by C1-inhibitor. Covalently bound, large molecular weight C3α-chain-gonococcal complexes were disbanded by methylamine release of ester linkages. Released 125I-C3 migrated as C3b without degradation by gonococcal proteases. Purified classical components alone or McAb 10 alone facilitated JS3 killing by neutrophils; when combined, the two provided maximal killing. Levels of McAb 10 that only slightly increase C3 deposition on JS3 are bacteridical in serum and maximally opsonic in combination with purified classical pathway components.",
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