Journal article
Regulation of gonococcal sialyltransferase, lipooligosaccharide, and serum resistance by glucose, pyruvate, and lactate
Infection and immunity, v 64(11), pp 4630-4637
Nov 1996
PMID: 8890217
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Strain F62 of Neisseria gonorrhoeae gonococci (GC) is sensitive to normal human serum unless CMP-N-acetylneuraminic acid (CMP-NANA) is present. NANA is transferred primarily to a 4.5-kDa lipooligosaccharide (LOS) structure by a GC sialyltransferase (Stase). We investigated LOS and Stase expression and serum resistance in strain F62 grown in different carbon sources and growth conditions. Pyruvate-grown GC expressed 1.9- to 5.6-fold more Stase activity than did glucose-grown GC, whereas lactate-grown GC generally expressed intermediate Stase activities. Broth-grown GC expressed two- to fourfold more Stase activity than did plate-grown GC in all carbon sources. Pyruvate- or lactate-grown GC expressed significantly more of the sialylateable 4.5-kDa LOS species than did glucose-grown GC. Anaerobically, the 4.5-kDa LOS species was expressed in greater quantity than the 4.9-kDa N-acetyl galactosamine-terminating species in all carbon sources. Pyruvate-grown GC also incorporated up to threefold more radiolabelled CMP-NANA onto the 4.5-kDa LOS species than did glucose-grown GC. In serum resistance studies, pyruvate-grown GC were 6.5- to 16.1-fold more serum resistant than glucose-grown GC at limiting CMP-NANA concentrations (1.56 to 12.50 microg/ml). Taken together, these results indicate that gonococcal expression of Stase activity is up-regulated by growth in pyruvate or lactate, which correlates with enhanced expression of the sialylateable 4.5-kDa LOS and, for growth in pyruvate, correlates with enhanced sialylation of gonococcal LOS and greater serum resistance. In different in vivo niches, gonococcal LOS sialylation, serum resistance, and interaction with host cells can be highly regulated.
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Details
- Title
- Regulation of gonococcal sialyltransferase, lipooligosaccharide, and serum resistance by glucose, pyruvate, and lactate
- Creators
- D J McGee - Department of Microbiology and Immunology, MCP-Hahnemann School of Medicine, Allegheny University of the Health Sciences, Philadelphia, Pennsylvania 19129, USAR F Rest
- Publication Details
- Infection and immunity, v 64(11), pp 4630-4637
- Publisher
- American Society for Microbiology (ASM); United States
- Grant note
- AI33505 / NIAID NIH HHS
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- [Retired Faculty]
- Web of Science ID
- WOS:A1996VP42800032
- Scopus ID
- 2-s2.0-0029958319
- Other Identifier
- 991014878086204721
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Data related to this publication, from InCites Benchmarking & Analytics tool:
- Web of Science research areas
- Immunology
- Infectious Diseases