Mannose-6-phosphate: A regulator of LLO destruction

Ningguo Gao, Mark A. Lehrman

Research output: Chapter in Book/Report/Conference proceedingChapter

6 Scopus citations


Oligosaccharyltransferase (OT) catalyzes the signature reaction of the asparagine-linked glycosylation pathway, namely, the transfer of preformed glycans from the lipid-linked oligosaccharide Glc3Man9GlcNAc2-P-P-Dolichol (G3M9Gn2-LLO) to appropriate asparaginyl residues on acceptor polypeptides. We have identified a reaction, possibly catalyzed by OT, that results in the hydrolysis or "transfer to water" of host LLOs in response to viral infection with release of a free G 3M9Gn2 glycan. The loss of LLO ostensibly hinders N-glycosylation of viral polypeptides. This response is achieved by a novel stress-activated signaling pathway in which free mannose-6-phosphate (M6P) acts as a second-messenger. Here, we describe methods with permeabilized mammalian cells for activation of the M6P-regulated LLO hydrolysis, or transfer of glycan to water, in vitro.

Original languageEnglish (US)
Title of host publicationGlycosyltransferases
Subtitle of host publicationMethods and Protocols
PublisherHumana Press Inc.
Number of pages6
ISBN (Print)9781627034647
StatePublished - 2013

Publication series

NameMethods in Molecular Biology
ISSN (Print)1064-3745


  • Dolichol
  • Free glycan
  • Lipid-linked oligosaccharide
  • Mannose-6-phosphate
  • Streptolysin-O

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics


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