Hepatitis C virus asialoglycoproteins

Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Recombinant dna technique included in method of making a...

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435 5, 435 699, 4241851, 4242281, 530395, 530820, C12P 2102, C12Q 170, A61K 3929, C07K 100

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06074846&

ABSTRACT:
Two Hepatitis C Virus envelope proteins (E1 and E2) are expressed without sialylation. Recombinant expression of these proteins in lower eukaryotes, or in mammalian cells in which terminal glycosylation is blocked, results in recombinant proteins which are more similar to native HCV glycoproteins. When isolated by GNA lectin affinity, the E1 and E2 proteins aggregate into virus-like particles.

REFERENCES:
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patent: 5350671 (1994-09-01), Houghton et al.
Lanford et al., "Analysis of Hepatitis C Virus Capsid, E1, and E2/NS1 Proteins Expressed in Insect Cells," Virology 197:225-235 (1993).
Spaete et al., "Characterization of the Hepatitis C Virus E2/NSl Gene Product Expressed in Mammalian Cells," Virology 188:819-830 (1992).
Saunders Dictionary & Encyclopedia of Laboratory Medicine and Technology p. 138 (1987).
Hedo, "Lectins as Tools . . . ," Receptor Purification Procedures (Alan R Liss,)NY) pp. 45-60 (1984).
Goochee et al., "The Oligosccharides of glycoproteins . . . , " Biotechnology 9:1347-1355 (1991).

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