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
Number of pages6
StatePublished - 2013

Publication series

NameMethods in Molecular Biology
ISSN (Print)1064-3745


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

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

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