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Processing of the Hepatitis C virus precursor protein expressed in the methylotrophic yeast Pichia pastoris.

Abstract：

:The expression and processing of the Hepatitis C virus core protein (HCcAg) were analyzed in the methylotrophic yeast Pichia pastoris. Two proteins with 21 (p21) and 23 kDa (p23) were detected in immunoblot with a serum from a chronic carrier patient, as the major products for HCcAg. Both proteins, p21 and p23, produced by proteolytic processing in P. partoris, share the same N-terminal region and reacted with a monoclonal antibody towards the first 35 amino acids of HCcAg. The proteolytic processing of the recombinant polypeptide, having the HCcAg and the first 148 aa of E1 protein, was also confirmed by immunoblot analysis using mAbs with HCcAg and E1 specificities, respectively. The 32 kDa glycosilated E1 protein was then immuno-identified, as well as the processed HCcAg. These data demonstrated the usefulness of P. pastoris, as expression system, to study the processing of HCV structural proteins.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Acosta-Rivero N,Musacchio A,Lorenzo L,Alvarez C,Morales J

doi

10.1016/s0006-291x(02)00635-6

subject

Has Abstract

pub_date

2002-07-05 00:00:00

pages

81-4

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(02)00635-6

journal_volume

295

pub_type

杂志文章

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