| Literature DB >> 11748209 |
Chao-Ming Tsai1, George Kao, Peixuan Zhu.
Abstract
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.Entities:
Mesh:
Substances:
Year: 2002 PMID: 11748209 PMCID: PMC127647 DOI: 10.1128/IAI.70.1.407-411.2002
Source DB: PubMed Journal: Infect Immun ISSN: 0019-9567 Impact factor: 3.441