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N-Linked glycosylation usually occurs at the sequon,
Asn-X-Ser/Thr. In this sequon, the side chain of the hydroxy
amino acid (Ser or Thr) may play a direct catalytic role in the
enzymatic transfer of core oligosaccharides to the Asn residue. Using
recombinant variants of rabies virus glycoprotein (RGP), we examined
the influence of the hydroxy amino acid on core glycosylation
efficiency. A variant of RGP containing a single Asn-X-Ser
sequon at Asn
Volume 270,
Number 24,
Issue of June 16, pp. 14756-14761, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
was modified by site-directed mutagenesis to
change the sequon to either Asn-X-Cys or Asn-X-Thr.
The impact of these changes on core glycosylation efficiency was
assessed by expressing the variants in a cell-free
transcription/translation/glycosylation system and in transfected
tissue culture cells. Substitution of Cys at position 39 blocks
glycosylation, whereas substitution of Thr dramatically increases core
glycosylation efficiency of Asn
in both membrane-anchored
and secreted forms of RGP. The substitution of Thr for Ser also
dramatically enhances the level of expression and cell surface delivery
of RGP when the sequon at Asn
is the only sequon in the
protein. Novel forms of membrane-anchored and secreted RGP which are
fully glycosylated at all three sequons were also generated by
substitution of Thr at position 39.
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