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Glycobiology Advance Access originally published online on May 9, 2009
Glycobiology 2009 19(8):816-828; 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 Lommel2 and Sabine Strahl1,2

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

1 To whom correspondence should be addressed: Tel: +49 (0)6221 54 6286; Fax: +49 (0)6221 54 5859; e-mail: sstrahl{at}HIP.uni-heidelberg.de

Received on March 18, 2009; revised on May 6, 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: congenital muscular dystrophy / glycosylation / mannosyltransferase / O-mannosylation

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


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