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J Biol Chem, Vol. 273, Issue 45, 29905-29914, November 6, 1998
,
From the Institute of Virology, Department of Infectious Diseases
and Immunology, Faculty of Veterinary Medicine, and the Institute of
Biomembranes, Utrecht University, Yalelaan 1, 3584 CL Utrecht, The
Netherlands and the The mouse hepatitis virus (MHV) membrane (M)
protein contains only O-linked oligosaccharides. We have
used this protein as a model to study the structural requirements for
O-glycosylation. We show that MHV M is modified by the
addition of a single oligosaccharide side chain at the cluster of 4 hydroxylamino acids present at its extreme amino terminus and
identified Thr at position 5 as the functional acceptor site. The
hydroxylamino acid cluster, which is quite conserved among
O-glycosylated coronavirus M proteins, is not in itself
sufficient for O-glycosylation. Downstream amino acids are
required to introduce a functional O-glycosylation site into a foreign protein. In a mutagenic analysis
O-glycosylation was found to be sensitive to some
particular changes but no unique sequence motif for
O-glycosylation could be identified. Expression of mutant M
proteins in cells revealed that substitution of any 1 residue was
tolerated, conceivably due to the occurrence of multiple
UDP-N-acetylgalactosamine:polypeptide
N-acetylgalactosaminyltransferases (GalNAc transferases).
Indeed, MHV M served as a substrate for GalNac-T1, -T2, and -T3, as was
demonstrated using an in situ glycosylation assay based on
the co-expression of endoplasmic reticulum-retained forms of the GalNAc
transferases with endoplasmic reticulum-resident MHV M mutants. The
GalNAc transferases were found to have largely overlapping, but
distinct substrate specificities. The requirement for a threonine as
acceptor rather than a serine residue and the requirement for a proline
residue three positions downstream of the acceptor site were found to
be distinctive features.
Cell Biology Programme, EMBL, 69012 Heidelberg, Germany
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