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Query: UMLS:C0019158 (hepatitis)
 30,205 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A hepatitis C virus (HCV) genome was isolated and sequenced from a single Japanese patient with chronic non-A, non-B hepatitis. The genome (HCV-JT), which was constructed with 23 cDNA clones, consisted of 9436 nucleotides with a long open reading frame which could encode a sequence of 3010 amino acid residues. To study the sequence variation of the HCV genome in an individual, we analyzed another sequence of the HCV genome (HCV-JT') constructed with different cDNA clones derived from the same patient. The nucleotide variation between HCV-JT and -JT' was less than 1%, and was distributed throughout the genome except in the 5' non-coding region, where no variation was observed. The diversity was higher (1.6%) in the putative envelope protein region than in other regions. The nucleotide and deduced amino acid sequences of HCV-JT showed homologies of about 91 and 95%, respectively, with those of other Japanese HCV isolates. The nucleotide diversity was high in the gp 70 region (corresponding to the NS 1 region of flaviviruses) and low in the 5' non-coding and p22 (putative core protein) regions. A similar pattern of distribution of nucleotide changes was observed on comparison of HCV-JT with an American isolate HCV-US, where the homologies in nucleotide and amino acid sequences were about 79 and 85%, respectively. Base transversions contributed about 50% of the total base exchanges between the Japanese and American HCV sequences, but only 20% or less of those among Japanese HCV or among American HCV sequences. Thus, the Japanese and American HCVs are genetically distinguishable, supporting our earlier prediction that these two HCVs could be classified as different subtypes.
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PMID:Molecular cloning of hepatitis C virus genome from a single Japanese carrier: sequence variation within the same individual and among infected individuals. 131 27

We examined sequential serum samples from 12 patients with well-characterized posttransfusion non-A, non-B hepatitis who had an acute, resolving self-limited type of clinical course for the presence of antibody to the hepatitis C virus nucleocapsid (core) protein (p22) expressed by a recombinant baculovirus. These sera were simultaneously examined for antibody to the hepatitis C virus nonstructural protein (C100-3) that is presently used for blood screening worldwide. In three patients, both anti-p22 and anti-C100-3 antibodies were detected, but anti-p22 was detected much earlier. In four patients, only anti-p22 was detected. Two other patients were considered to be hepatitis C virus carriers who had been already infected with hepatitis C virus. In one patient, only anti-C100-3 was detected, and it was transient. In two patients, neither antibody was detected. Anti-p22 was detected in at least one of eight samples of transfused blood. Of the nine samples of donated blood that were positive for anti-p22, only four were positive for anti-C100-3. This new assay detecting the antibody to the p22 protein is thus useful for the serodiagnosis of non-A, non-B hepatitis in the acute phase and for blood screening.
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PMID:Improved serodiagnosis of non-A, non-B hepatitis by an assay detecting antibody to hepatitis C virus core antigen. 137 81

An enzyme-linked immunosorbent assay (ELISA) was developed for serological diagnosis of hepatitis C virus (HCV) infection, using HCV core protein (p22) synthesized by a recombinant baculovirus. Among 58 clinically well-defined chronic non-A, non-B hepatitis (NANBH) patients, 49 (84.5%) were positive for p22 antibody (anti-p22), whereas 42 (72.4%) were positive for C100-3 antibody (anti-C100-3), as measured by the present assay using the HCV nonstructural protein as antigen. Thirty-nine patients (67.2%) had both antibodies. No significant level of anti-p22 was detected in sera of chronic hepatitis B patients or normal blood donors. In typical post-transfusion NANBH patients, anti-p22 could be detected at, or even before, the first alanine aminotransferase peak. Anti-p22 was also detected in blood donors who were previously shown to be involved in transmitting HCV but in whose serum anti-C100-3 was not detectable. The ELISA detecting antibody to the HCV core protein expressed and properly processed in animal cells will be useful for mass screening of donor blood as well as for early diagnosis of hepatitis C.
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PMID:Serodiagnosis of hepatitis C virus (HCV) infection with an HCV core protein molecularly expressed by a recombinant baculovirus. 190 12

Mouse L fibroblasts infected with mouse hepatitis virus, MHV3, and radiolabelled with 35S-methionine, contained, in addition to the three major structural polypeptides, p24, p56 and p180, two additional ones, p22 and p50. Of these total five polypeptides, only three, p22, p56 and p180, were labelled in infected cells during a 2 min 35S-methionine pulse and are, therefore, presumed to be immediate translation products. Pulse-chases and chymotryptic peptide mapping experiments showed apparent precursor-product relationships between p56 and p50 and between p22 and p24. Protein synthesis in infected cells was synchronized at the initiation stage by pre-exposure to hypertonic medium. Using a 0.5 min pulse-10 min chase sequence, to limit incorporation of 35S-methionine to stretches of approx. 100 amino acids adjacent to translational initiation sites, it was found that all three polypeptides, p22, and p56 and p180 contained radiolabel. It is thus apparent that translation of the three major structural proteins (or precursors) is initiated independently rather than at a single site as in the cases of other positive-strand RNA viruses such as polio or Semliki Forest virus.
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PMID:Cellular synthesis and modification of murine hepatitis virus polypeptides. 627 Feb 50

We identified eight protein species in virions of mouse hepatitis virus strain A59. Based on their sizes, prosthetic groups, and locations in virions, these proteins were designated gp180/E2, gp90/E2, pp54/N, gp26.5/E1, gp25.5/E1, p24/E1, p22/X, and p14.5/Y. The positions of the last two proteins in virions are not known. Host protein synthesis in Sac(-) cells infected with mouse hepatitis virus strain A59 was inhibited, and the following novel proteins appeared: gp150, gp90, p54, gp26.5, gp25.5, p24, p22, and p14.5. Except for gp150, these polypeptides all co-electrophoresed with mouse hepatitis virus strain A59 structural proteins. In addition, all of these proteins could be immunoprecipitated with a convalescent mouse serum or a rabbit antiserum raised against purified disrupted virus. After a 15-min pulse of infected cells with radioactive amino acids at 7h postinfection, gp90 was not detected, whereas gp26.5 and gp25.5 were only labeled to a small extent. During a subsequent chase period gp150 was processed to gp90, whereas the radioactivity in gp26.5 and gp25.5 increased concomitantly with a reduction of label in p24. Tunicamycin, an antibiotic which inhibits the synthesis of glycopeptides bearing N glycosidically linked oligosaccharides, prevented the appearance of gp150 in mouse hepatitis virus strain A59-infected cells. Instead, a 110,000-dalton protein accumulated. In contrast, the syntheses of the smaller viral glycoproteins gp26.5 and gp25.5 were resistant to this drug, indicating that these glycosylations were of the O glycosidical type. Although the production of infectious virus in tunicamycin-treated cells was inhibited by more than 99%, release of noninfectious viral particles continued. An analysis of these particles revealed that they lacked the peplomeric glycoproteins gp90/E2 and gp180/E2. Obviously, although the surface projections were not essential for budding of virus particles from the cells, they were required for infectivity.
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PMID:Viral protein synthesis in mouse hepatitis virus strain A59-infected cells: effect of tunicamycin. 627 93

The relationships of various polypeptides associated with hepatitis B surface antigen (HBsAg), ground squirrel hepatitis surface antigen (GSHsAg), woodchuck hepatitis surface antigen (WHsAg), and duck hepatitis B surface antigen (DHBsAg) were studied by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and tryptic peptide mapping. Analysis of independent antigen isolates by SDS-PAGE resulted in bands consistently observed at 24,000, 28,000, 32,000, 43,000, and 50,000 Da with HBsAg; at 22,000, 25,000, 35,000, 37,000, 39,000, and 42,000 Da with GSHsAg and WHsAg; and at 18,500, 30,000, and 38,500, Da with DHBsAg. Comparison of the major polypeptide pair from the mammalian viruses by tryptic peptide mapping suggests more than a single point of glycosylation or other post-translational modification(s) in some paired comparisons and/or heterogeneity in glycosylation in others. Comparison of the major component of each mammalian virus (HBsAg p24, GSHsAg p22, or WHsAg p22), or the major polypeptide of DHBsAg (p18.5), with their respective larger polypeptides by peptide mapping indicated that one or more of the larger components in each virus shares extensive homology with the appropriate major component. Further, these larger components possess additional spots, interpreted as additional primary sequences, which were not found in the map of the appropriate major component. Collectively, the results suggest that a number of surface antigen-associated polypeptides may be partially encoded for by the pre-S gene region known to exist in hepatitis B virus (HBV) and woodchuck hepatitis virus (WHV), and likely to exist in ground squirrel hepatitis virus (GSHV) and duck hepatitis B virus (DHBV) DNA.
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PMID:The nature of polypeptides larger in size than the major surface antigen components of hepatitis b and like viruses in ground squirrels, woodchucks, and ducks. 663 42

The relationships among the core antigen polypeptides of hepatitis B virus (HBV) and ground squirrel hepatitis virus (GSHV) were studied using sodium dodecyl sulfate-polyacrylamide gel electrophoresis and tryptic peptide mapping. The major core antigen polypeptides of liver-derived HBV (p22) and GSHV (p20.5) shared 56% of the spots in their peptide maps. Comparison of hepatitis B core antigen (HBcAg) p19 or ground squirrel hepatitis core antigen (GSHcAg) p16.5 with their respective major polypeptides indicated that these components probably resulted from cleavage of the major polypeptide of each virus. Other polypeptides smaller than the major component of each virus were often faint on polyacrylamide gels and probably resulted from the cleavage or degradation of components larger than p22 of HBcAg or p20.5 of GSHcAg, since their peptide maps contained spots unique to these high-molecular-weight components. p26 of GSHcAg and p27.5 of HBcAg shared approximately two-thirds of the spots on their peptide maps with those of their respective major core polypeptides. Furthermore, p37.5 of GSHcAg and p40 of HBcAg shared about 60% homology with their respective major polypeptides, and also shared many of the spots that were unique to p26 of GSHcAg or p27.5 of HBcAg but were not found in the peptide map of their respective core antigen polypeptides. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis bands larger than 40,000 daltons were variably present, and peptide mapping indicated that these were aggregates of various smaller core antigen-associated polypeptides. The results suggest that p40 of HBcAg and p37.5 of GSHcAg are the largest unique polypeptides in these core particles, and that they are encoded for by the genome of each virus. That a subset of the spots unique to p40 or p37.5 was also found in p27.5 of HBcAg or p26 of GSHcAg, respectively, as compared to the major core polypeptides, also suggests that p27.5 and p26 are unique proteins encoded by the genome of each virus. It is proposed that the core antigen gene of each virus is larger than that which would encode the major polypeptide of each virus, and that the genetic organizations of the core genes of HBV and GSHV are very similar.
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PMID:Core particles of hepatitis B virus and ground squirrel hepatitis virus. I. Relationship between hepatitis B core antigen- and ground squirrel hepatitis core antigen-associated polypeptides by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and tryptic peptide mapping. 710 37

Hepatitis C virus (HCV) is a main causative agent for transfusion-associated and sporadic cases of non-A, non-B hepatitis throughout the world. HCV has a positive-strand RNA of about 9,400 nucleotides as its genome, whose organization is similar to those of animal pestiviruses or human flaviviruses. In spite of the lack of an effective replication system in tissue culture cells, genes coding for viral proteins of HCV have been identified. The putative nucleocapsid (p22) and envelope (gp35 and gp60) proteins have been expressed in cells by different vectors under various foreign promoters. Furthermore, a truncated core protein and association of envelope proteins with nonstructural proteins have also been observed. These synthesized viral proteins have been shown to be useful for diagnostic assays.
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PMID:Characterization of HCV structural proteins expressed in various animal cells. 752 19

We retrospectively examined the antibodies to p22, a hepatitis C virus (HCV) nucleocapsid protein, and to c100-3, a HCV nonstructural protein, in donors whose blood was transfused to patients who later developed post-transfusion non-A, non-B hepatitis. Of 13 such blood donors, three seroconverted and three seroreverted with the anti-c100-3 test. In contrast, 12 of the 13 blood donors showed the same results at transfusion and follow-up, and one donor showed seroconversion with the anti-p22 assay. The follow-up study shows that the anti-p22 antibody test provides consistent results and is far more suitable for screening blood than the anti-c100-3 test.
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PMID:Follow-up study of anti-hepatitis C virus antibodies in blood donors implicated in post-transfusion non-A, non-B hepatitis. 769 Jun 40

We evaluated the clinical significance of the antibody to hepatitis C core protein (anti-p22) analysing 147 sera from 99 patients; 45 of them had post-transfusion non A non B (NANB) hepatitis, 28 cryptogenic non A non B hepatitis, 12 chronic hepatitis B, 7 chronic hepatitis D, 6 other forms of liver disease (4 primary biliary cirrhosis, 2 autoimmune hepatitis) and 1 rheumatoid arthritis. All sera were tested by commercial 1st and 2nd-generation ELISAs and anti-p22 single antibody ELISA. We found a highly significant correspondence between anti-p22 and commercial assays (p = 0.0001). HCV-RNA was detected by reverse transcriptase polymerase chain reaction (RT-PCR) in sera showing positive or negative concordant results and in all sera (24) that showed discordant results by anti-p22 and commercial ELISAs. HCV-RNA was found in 14 of 17 (82%) anti-p22 positive sera that were negative by commercial ELISAs, in 1 of 7 (14.3%) anti-p22 negative sera that were positive by commercial ELISAs (p = 0.001) and in all control sera from patients with positive concordant results. It was undetectable in 7 sera from patients with autoimmune diseases (negative by all ELISAs). We studied follow-up sera from 16 patients treated with interferon: 8 long-term responders (with persistently normal ALT levels for at least 24 months after discontinuation of therapy and histological remission) and 8 non-responders. Sera were also tested by a 4-antigen recombinant immunoblotting assay (RIBA II).(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Clinical significance of the antibody to the putative core protein of hepatitis C virus in patients with chronic liver disease. 769 Aug 74


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