Abstract：
:cDNA clones encoding the envelope glycoprotein E1 of rubella virus (RV) were altered by site-directed mutagenesis at consensus sites for addition of N-linked glycans. The resulting plasmids were introduced into COS cells and the mutant E1 proteins were analyzed by indirect immunofluorescence, radioimmunoprecipitation, and immunoblotting. We found that RV E1 contains three N-linked oligosaccharides, each approximately 2 kDa in size. Although lack of glycosylation did not appear to affect targeting of E1 to the Golgi region, mutants lacking N-linked glycans at Asn 177 and Asn 209 failed to bind anti-E1 antibodies under nonreducing conditions. Our results suggest that glycosylation may be important for expression of important immunologic epitopes on RV E1.
journal_name
Virologyjournal_title
Virologyauthors
Hobman TC,Qiu ZY,Chaye H,Gillam Sdoi
10.1016/0042-6822(91)90915-xsubject
Has Abstractpub_date
1991-04-01 00:00:00pages
768-72issue
2eissn
0042-6822issn
1096-0341journal_volume
181pub_type
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