Journal article
Expression of sialyltransferase is not required for interaction of Neisseria gonorrhoeae with human epithelial cells and human neutrophils
Infection and immunity, v 64(10), pp 4129-4136
Oct 1996
PMID: 8926079
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Sialyltransferase (Stase) in Neisseria gonorrhoeae organisms (gonococci [GC]) transfers sialic acid (N-acetylneuraminic acid [NANA]) from cytidine 5'-monophospho-N-acetylneuraminic acid (CMP-NANA) mainly to the terminal galactose (Gal) residue in the Gal beta-1,4 N-acetylglucosamine (Gal-GlcNAc)-R lipooligosaccharide (LOS) structure. Sialylated GC resist killing by normal human serum, sometimes show reduced invasion of epithelial cells, and have reduced adhesion to and stimulation of human neutrophils. We questioned whether Stase itself modulates the interactions of GC with human epithelial cells and neutrophils in the absence of exogenous CMP-NANA. To that end, we treated strain F62 with ethyl methanesulfonate and grew approximately 175,000 colonies on CMP-NANA plates, and screened them with monoclonal antibody 1B2-1B7 (MAb 1B2). MAb 1B2 is specific for Gal-GlcNAc and reacts only with asialylated GC. We isolated 13 MAb 1B2-reactive mutants, including five null mutants, that had Stase activities ranging from barely detectable to fivefold less than that of wild-type (WT) F62. The LOS phenotype of Stase null mutants was identical to that of WT F62, yet the mutants could not sialylate their LOS when grown with CMP-NANA. The Stase null phenotype was rescuable to Stase+ by transformation with chromosomal DNA from WT F62. Stase null mutants remained serum sensitive even when grown with CMP-NANA. One Stase null mutant, ST94A, adhered to and invaded the human cervical epithelial cell line ME-180 at levels indistinguishable from that of WT F62 in the absence of CMP-NANA. In human neutrophil studies, ST94A stimulated the oxidative burst in and adhered to human neutrophils at levels similar to those of WT F62. ST94A and WT F62 were also phagocytically killed by neutrophils at similar levels. These results indicate that expression of Stase activity is not required for interaction of GC with human cells.
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Details
- Title
- Expression of sialyltransferase is not required for interaction of Neisseria gonorrhoeae with human epithelial cells and human neutrophils
- Creators
- D J McGee - Department of Microbiology and Immunology, MCP-Hahnemann School of Medicine, Allegheny University of the Health Sciences, Philadelphia, Pennsylvania 19102, USAG C Chen - Department of Microbiology and Immunology, MCP-Hahnemann School of Medicine, Allegheny University of the Health Sciences, Philadelphia, Pennsylvania 19102, USAR F Rest - Department of Microbiology and Immunology, MCP-Hahnemann School of Medicine, Allegheny University of the Health Sciences, Philadelphia, Pennsylvania 19102, USA
- Publication Details
- Infection and immunity, v 64(10), pp 4129-4136
- Publisher
- American Society for Microbiology (ASM)
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- [Retired Faculty]
- Web of Science ID
- WOS:A1996VJ79400026
- Scopus ID
- 2-s2.0-0029839236
- Other Identifier
- 991014878476204721
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- Web of Science research areas
- Immunology
- Infectious Diseases