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Glycobiology Advance Access published online on May 9, 2009
Glycobiology, doi:10.1093/glycob/cwp066
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© The Author 2009. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Review

Protein O-Mannosylation: Conserved from Bacteria to Humans

Mark Lommel and Sabine Strahl*

Heidelberg Institute for Plant Sciences, Dept. V Cell Chemistry, University of Heidelberg, Im Neuenheimer Feld 360, 69120 Heidelberg, Germany

* Author for correspondence: email: sstrahl{at}HIP.uni-heidelberg.de

Received on March 18, 2009; accepted on May 6, 2009

Protein O-mannosylation is an essential modification in fungi and animals. Different from most other types of O-glycosylation, protein O-mannosylation is initiated in the endoplasmic reticulum by the transfer of mannose from dolichol monophosphate-activated mannose to serine and threonine residues of secretory proteins. In recent years, it has emerged that even bacteria are capable of O-mannosylation and that the biosynthetic pathway of O-mannosyl glycans is conserved between pro- and eukaryotes. In this review we summarize the observations that have opened up the field, and highlight characteristics of O-mannosylation in the different domains/kingdoms of life.

Key words: O-mannosylation / mannosyltransferase / glycosylation / congential muscular dystrophy / bacteria / yeast

Dedicated to Professor Widmar Tanner on the occasion of his 70th birthday


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