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Immunogenicity of Neisseria gonorrhoeae Lipooligosaccharide Epitope 2C7, Widely Expressed In Vivo with No Immunochemical Similarity to Human Glycosphingolipids
Author(s) -
Sunita Gulati,
D. P. McQuillen,
Robert E. Mandrell,
Darshana Jani,
Peter A. Rice
Publication year - 1996
Publication title -
the journal of infectious diseases
Language(s) - English
Resource type - Journals
eISSN - 1537-6613
pISSN - 0022-1899
DOI - 10.1093/infdis/174.6.1223
Subject(s) - epitope , neisseria gonorrhoeae , immunogenicity , microbiology and biotechnology , monoclonal antibody , virology , biology , antibody , antigen , bacterial outer membrane , immunology , escherichia coli , biochemistry , gene
Natural infection with Neisseria gonorrhoeae may elicit a substantial antibody response directed against gonococcal lipooligosaccharide. Monoclonal antibody (MAb) 2C7 recognized a gonococcal lipooligosaccharide epitope, identified the epitope directly in 94% of 68 consecutive culture-positive genital secretions, and recognized 95% of 101 randomly chosen fresh (second-passage) gonococcal isolates. The epitope was stably maintained after multiple in vitro passages and did not compete with any of the known cross-reactive human glycosphingolipid structures. MAb 2C7 mediated in vitro killing and phagocytosis by human polymorphonuclear leukocytes of 1 serum-sensitive (sialylated or not) and 1 stably serum-resistant gonococcal isolate that expressed the epitope. Gonococcal endometritis and disseminated infection elicited increases (6.5-fold IgM, 4.4-fold IgG; 18-fold IgM, 17-fold IgG, respectively) in anti-2C7 epitope antibody. Immunization with a gonococcal outer membrane vaccine elicited a mean 44.5-fold increase in IgG anti-2C7 epitope antibody in 20 of 28 subjects. The epitope identified by MAb 2C7 may represent an excellent target for a potentially protective gonococcal vaccine candidate.

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