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Detection of the putative E2 protein of hepatitis C virus in human liver
Author(s) -
Nakamoto Yasunari,
Kaneko Shuichi,
Honda Masao,
Unoura Masashi,
Cheong Jaehun,
Harada Akihisa,
Matsushima Kouji,
Kobayashi Kenichi,
Murakami Seishi
Publication year - 1994
Publication title -
journal of medical virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 121
eISSN - 1096-9071
pISSN - 0146-6615
DOI - 10.1002/jmv.1890420409
Subject(s) - polyclonal antibodies , recombinant dna , hepatitis c virus , virology , biology , antibody , microbiology and biotechnology , virus , viral envelope , antiserum , flaviviridae , gene , immunology , biochemistry
The question was asked whether a predicted envelope protein, considered to be processed from the polyprotein precursor encoded by the putative E2/NS1 region of the hepatitis C virus (HCV) genome, may be observed in HCV‐infected humans. Two polyclonal antibodies against recombinant E2/NS1 proteins were prepared and their reactivity tested against liver extracts from HCV‐infected patients by immunoblotting analysis. A band corresponding to a size of 44 kDa was detected in liver extracts from patients who were positive for the HCV‐specific antibody anti‐C100‐3 but not in liver extracts from patients who did not have anti‐C100‐3 antibody. Additionally, no band was detected using preimmune sera or antisera which had been preabsorbed with recombinant E2/NS1 proteins. Deglycosylation studies demonstrated that the 44 kDa protein was a glycosylated form of a 38 kDa protein which corresponds to the predicted molecular weight of the putative E2/NS1 protein. These results suggest that the 44 kDa protein is a product of the E2/NS1 region. Frequent observation of the 44 kDa band in cases of chronic active hepatitis C suggests a correlation between the expression of this protein and the progression of hepatitis. © 1994 Wiley‐Liss, Inc.