Immunogenicity of Neisseria gonorrhoeae Lipooligosaccharide Epitope 2C7, Widely Expressed In Vivo with No Immunochemical Similarity to Human Glycosphingolipids

• Published in: The Journal of infectious diseases 1996-12, Vol.174 (6), p.1223-1237
• Main Authors: Gulati, Sunita, McQuillen, Daniel P., Mandrell, Robert E., Jani, Darshana B., Rice, Peter A.
• Format: Article
• Language: English
• Subjects: Adult; Antibodies; Antibodies, Bacterial - immunology; Antibodies, Monoclonal - immunology; Antigens; Antigens, Bacterial - immunology; Bacteriology; Biological and medical sciences; Blood Group Antigens - immunology; Cross Reactions - immunology; Cytotoxicity, Immunologic; Epitopes; Epitopes - immunology; Erythrocytes; Female; Fluorescence; Fundamental and applied biological sciences. Psychology; Glycosphingolipids - immunology; Gonorrhea - immunology; Heptoses; Humans; Infections; Leukocytes, Mononuclear - immunology; Lipopolysaccharides - immunology; Major Articles; Male; Microbiology; Molecular Structure; Monoclonal antibodies; Morphology, structure, chemical composition; Neisseria gonorrhoeae; Neisseria gonorrhoeae - immunology; Phagocytosis; Polysaccharides, Bacterial - immunology; Vaccination
• ISSN: 0022-1899; 1537-6613
• DOI: 10.1093/infdis/174.6.1223

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 9S% 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.S-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.S-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.