Expression of human interferon alpha H, an interferon with two potential asparagine-linked glycosylation sites.
Of the large number of human alpha interferon genes identified, only one, Hu-IFN-alpha H, contains potential asparagine-linked glycosylation sites. With the use of a new vector that permits convenient expression, site-specific mutation, and DNA sequencing, Hu-IFN-alpha H was expressed in Escherichia coli. The bacterial product which is not glycosylated is fully active demonstrating that the carbohydrate on this species is not required for antiviral activity.
Zhao
X X
XX
Institute of Virology, China National Centre for Preventive Medicine, Beijing.
Daugherty
B L
BL
Schwartz
B
B
Maeda
S
S
Pestka
S
S
D001216:Asparagine; D001483:Base Sequence; D002872:Chromosome Deletion; D004269:DNA, Bacterial / Q000302:isolation & purification; D004926:Escherichia coli / Q000235:genetics; D005786:Gene Expression Regulation; D005822:Genetic Vectors; D006031:Glycosylation; D006801:Humans; D007370:Interferon Type I / Q000235:genetics*; D009841:Oligonucleotides / Q000138:chemical synthesis / Q000378:metabolism; D010766:Phosphorylation; D010957:Plasmids; D011994:Recombinant Proteins
D004269:DNA, Bacterial; D007370:Interferon Type I; D009841:Oligonucleotides; D011994:Recombinant Proteins; D001216:Asparagine