Mannose-6-phosphate: A regulator of LLO destruction

Ningguo Gao, Mark A. Lehrman

Research output: Chapter in Book/Report/Conference proceedingChapter

6 Scopus citations

Abstract

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
Pages277-282
Number of pages6
DOIs
StatePublished - Jul 25 2013

Publication series

NameMethods in Molecular Biology
Volume1022
ISSN (Print)1064-3745

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Keywords

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

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

Cite this

Gao, N., & Lehrman, M. A. (2013). Mannose-6-phosphate: A regulator of LLO destruction. In Glycosyltransferases: Methods and Protocols (pp. 277-282). (Methods in Molecular Biology; Vol. 1022). https://doi.org/10.1007/978-1-62703-465-4-20