Open AccessThe sialylation of gonococcal lipopolysaccharide by host factors: A major impact on pathogenicity
Author(s) -
Smith Harry,
Cole Jeffery A.,
Parsons Nicholas J.
Publication year - 1992
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1992.tb14054.x
Subject(s) - microbiology and biotechnology , lipopolysaccharide , neuraminic acid , neisseria gonorrhoeae , biology , antibody , cytidine , neisseria meningitidis , bacteria , glycoprotein , chemistry , immunology , biochemistry , enzyme , genetics
The resistance of gonococci in most patients to complement mediated killing by human serum is due to sialylation of their lipopolysaccharide (LPS) which prevents bactericidal antibody from reacting with target sites. Two of the host factors responsible are: cytidine 5′‐monophospho‐ N ‐acetyl neuraminic acid (CMP‐NANA), a well‐known sialylating agent, and another factor which enhances the transfer of sialyl groups from CMP‐NANA to LPS catalysed by a gonococcal sialytransferase. The bacterial determinant of resistance is a conserved LPS component of about 4.5 kDa which is sialylated at a terminal Galβ1‐4GlcNAc site on its side chain. The sialylated LPS forms a surface coat which is stainable by ruthenium red and connected with previously described ‘capsules’. These observations sparked off an explosion of research. Recent publications show that sialylation of LPS by CMP‐NANA affects additional important aspect of gonococcal pathogenicity, notably interactions with antibodies and phagocytes, and rendering the gonococcal surface more ‘host‐like’. Also, the observations have prompted an examination of LPS from some other pathogens for the presence of sialyl groups with positive results for Neisseria meningitidis and Haemophilus influenzae .