Sialylation of Neisseria meningitidis lipooligosaccharide inhibits serum bactericidal activity by masking lacto-N-neotetraose.

Eitemau Tebyg

• Affinity-Purified Human Immunoglobulin G That Binds a Lacto-N-Neotetraose-Dependent Lipooligosaccharide Structure Is Bactericidal for Serogroup B Neisseria meningitidis
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  Cyhoeddwyd: (2007)
• Endogenous sialylation of the lipooligosaccharides of Neisseria meningitidis.
  gan: Mandrell, R E, et al.
  Cyhoeddwyd: (1991)
• Human Lipooligosaccharide IGG That Prevents Endemic Meningococcal Disease Recognizes an Internal Lacto-N-neotetraose Structure
  gan: Cheng, Hui, et al.
  Cyhoeddwyd: (2011)
• Enhanced Factor H Binding to Sialylated Gonococci Is Restricted to the Sialylated Lacto-N-Neotetraose Lipooligosaccharide Species: Implications for Serum Resistance and Evidence for a Bifunctional Lipooligosaccharide Sialyltransferase in Gonococci
  gan: Gulati, Sunita, et al.
  Cyhoeddwyd: (2005)
• Enhanced Factor H Binding to Sialylated Gonococci Is Restricted to the Sialylated Lacto-N-Neotetraose Lipooligosaccharide Species: Implications for Serum Resistance and Evidence for a Bifunctional Lipooligosaccharide Sialyltransferase in Gonococci
  gan: Gulati, Sunita, et al.
  Cyhoeddwyd: (2006)