Ontology highlight
ABSTRACT:
SUBMITTER: Ketterer MR
PROVIDER: S-EPMC6392504 | biostudies-literature | 2016 Dec
REPOSITORIES: biostudies-literature
Ketterer Margaret R MR Rice Peter A PA Gulati Sunita S Kiel Steven S Byerly Luke L Fortenberry J Dennis JD Soper David E DE Apicella Michael A MA
The Journal of infectious diseases 20160728 11
Previous studies have demonstrated that Neisseria gonorrhoeae sialylates the terminal N-acetyllactosamine present on its lipooligosaccharide (LOS) by acquiring CMP-N-acetyl-5-neuraminic acid upon entering human cells during infection. This renders the organism resistant to killing by complement in normal human serum. N-acetyllactosamine residues on LOS must be free of N-acetyl-5-neuraminc acid (Neu5Ac; also known as "sialic acid") in order for organisms to bind to and enter urethral epithelial c ...[more]