Abstract
alpha-2,3-Sialyltransferase mutants of three genetically and phenotypically diverse Neisseria meningitidis strains were compared with regard to resistance to human serum and systemic spread in the infant rat. Lipopolysaccharide sialylation was found to be of minor importance for the resistance of serogroup B and C meningococcal disease isolates to complement attack.
MeSH terms
-
Animals
-
Bacterial Capsules
-
Blood Bactericidal Activity
-
Disease Models, Animal
-
Humans
-
Immunity, Innate
-
Lipopolysaccharides / metabolism*
-
Meningococcal Infections / immunology*
-
Meningococcal Infections / microbiology
-
Mutagenesis
-
N-Acetylneuraminic Acid / metabolism*
-
Neisseria meningitidis / enzymology
-
Neisseria meningitidis / genetics
-
Neisseria meningitidis / immunology*
-
Neisseria meningitidis / isolation & purification
-
Polysaccharides, Bacterial / physiology
-
Rats
-
Sialyltransferases / genetics
-
Sialyltransferases / metabolism
-
UDPglucose 4-Epimerase / genetics
-
UDPglucose 4-Epimerase / metabolism
-
beta-Galactoside alpha-2,3-Sialyltransferase
Substances
-
Lipopolysaccharides
-
Polysaccharides, Bacterial
-
capsular polysaccharide, meningococcal group B
-
meningococcal group C polysaccharide
-
Sialyltransferases
-
UDPglucose 4-Epimerase
-
galactose epimerase
-
N-Acetylneuraminic Acid
-
beta-Galactoside alpha-2,3-Sialyltransferase