Influence of the length of the lipooligosaccharide alpha chain on its sialylation in Neisseria meningitidis.
The sialylation of lipooligosaccharide (LOS) in Neisseria meningitidis plays a role in the resistance of the organism to killing by normal human serum. The length of the alpha chain extending out from the heptose I [Hep (I)] moiety of LOS influenced sialylation of N. meningitidis LOS in vitro and in vivo. The alpha chain required a terminal Gal and a trisaccharide or longer oligosaccharide to serve as an acceptor for sialylation. The disaccharide lactose (Galbeta1-4Glc) in the alpha chain of immunotype L8 LOS could not function as an acceptor for the sialyltransferase, probably due to steric hindrance imposed by the neighboring Hep (II) with phosphorylethanolamine and another group attached.
Tsai
Chao-Ming
CM
Division of Bacterial, Parasitic, and Allergenic Products, Center for Biologics, Food and Drug Administration, Bethesda, Maryland 20892, USA. tsai@cber.fda.gov
Kao
George
G
Zhu
Peixuan
P
D002240:Carbohydrate Sequence; D002462:Cell Membrane / Q000378:metabolism; D003569:Cytidine Monophosphate N-Acetylneuraminic Acid / Q000378:metabolism; D008070:Lipopolysaccharides / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D008969:Molecular Sequence Data; D019158:N-Acetylneuraminic Acid / Q000378:metabolism; D009345:Neisseria meningitidis / Q000254:growth & development / Q000378:metabolism*; D012799:Sialyltransferases / Q000302:isolation & purification / Q000378:metabolism*; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D000094663:beta-Galactoside alpha-2,3-Sialyltransferase
D008070:Lipopolysaccharides; C023023:lipid-linked oligosaccharides; D003569:Cytidine Monophosphate N-Acetylneuraminic Acid; D012799:Sialyltransferases; D019158:N-Acetylneuraminic Acid; D000094663:beta-Galactoside alpha-2,3-Sialyltransferase