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. © Springer Science+Business Media New York 2013.
CITATION STYLE
Gao, N., & Lehrman, M. A. (2013). Mannose-6-phosphate: A regulator of LLO destruction. Methods in Molecular Biology, 1022, 277–282. https://doi.org/10.1007/978-1-62703-465-4_20
Mendeley helps you to discover research relevant for your work.