Mapping and characterization of B cell linear epitopes in the conservative regions of hepatitis C virus envelope glycoproteins
Identifieur interne : 003390 ( Main/Exploration ); précédent : 003389; suivant : 003391Mapping and characterization of B cell linear epitopes in the conservative regions of hepatitis C virus envelope glycoproteins
Auteurs : L. V. Olenina ; L. I. Nikolaeva ; B. N. Sobolev ; N. P. Blokhina [Russie] ; A. I. Archakov ; E. F. KolesanovaSource :
- Journal of Viral Hepatitis [ 1352-0504 ] ; 2002-05.
English descriptors
- Teeft :
- Acute phase, Amino, Amino acid positions, Amino acid residues, Antibody, Antibody binding, Antigenic, Antigenic determinants, Aspartate aminotransferase, Binding region, Biomedical chemistry, Blackwell science, Chronic hepatitis, Chronic patients, Clin microbiol, Competition binding assay, Competitor peptide, Complete inhibition, Conservative regions, Determinant, Different hepatitis, Elisa, Envelope glycoproteins, Envelope proteins, Epitope, Epitope mapping, General virol, Glycoprotein, Glycoprotein sequences, Hcvinfected patients, Healthy donors, Hepatitis, High frequency, Human sera, Hyperimmune serum, Hypervariable region, Immune, Immune response, Immune responses, Immunodominant, Long peptide, Long peptides, Medical science, Mitokor mimotopes, Moscow infection diseases hospital, Multipin technology, Olenina, Other authors, Other peptides, Patient sera, Peptide, Peptide scanning approach, Peptide synthesis, Present study, Proc natl acad, Prr1, Putative, Reactive, Room temperature, Russian academy, Serum samples, Single serum, Specialized hepatologic center, Synthetic peptides, Variable regions, Viral, Viral hepatitis, Viral replication, Viral survival, Virol, Virus clearance, Virus core, Virus infection.
Abstract
Forty‐eight overlapping octapeptides covering highly conservative regions of E1 and E2 hepatitis C virus (HCV) envelope proteins were synthesized and tested by ELISA against different groups of sera obtained from HCV‐infected patients. All sera from patients with acute infection, except a single case of serum reactivity with the region HINRTALN, were nonreactive with any peptide. Sera obtained from chronic patients reacted with 12 peptides from five selected regions. Two immunodominant B epitopes were found, one being the precisely mapped antigenic site RMAWDM positioned inside the earlier shown immunodominant epitope from E1, and the second site, PALSTGLIH from E2, detected for the first time. New minor antigenic site was determined as PTDCFRKH from E2. We found only minor seroreactivity for one of the putative sites involved in CD81 binding, PYCWHYAP.
Url:
DOI: 10.1046/j.1365-2893.2002.00358.x
Affiliations:
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Kolesanova</name><affiliation><wicri:noCountry code="subField"></wicri:noCountry></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Journal of Viral Hepatitis</title><title level="j" type="alt">JOURNAL OF VIRAL HEPATITIS</title><idno type="ISSN">1352-0504</idno><idno type="eISSN">1365-2893</idno><imprint><biblScope unit="vol">9</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="174">174</biblScope><biblScope unit="page" to="182">182</biblScope><biblScope unit="page-count">9</biblScope><publisher>Blackwell Science Ltd</publisher><pubPlace>Oxford UK</pubPlace><date type="published" when="2002-05">2002-05</date></imprint><idno type="ISSN">1352-0504</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1352-0504</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acute phase</term><term>Amino</term><term>Amino acid positions</term><term>Amino acid residues</term><term>Antibody</term><term>Antibody binding</term><term>Antigenic</term><term>Antigenic determinants</term><term>Aspartate aminotransferase</term><term>Binding region</term><term>Biomedical chemistry</term><term>Blackwell science</term><term>Chronic hepatitis</term><term>Chronic patients</term><term>Clin microbiol</term><term>Competition binding assay</term><term>Competitor peptide</term><term>Complete inhibition</term><term>Conservative regions</term><term>Determinant</term><term>Different hepatitis</term><term>Elisa</term><term>Envelope glycoproteins</term><term>Envelope proteins</term><term>Epitope</term><term>Epitope mapping</term><term>General virol</term><term>Glycoprotein</term><term>Glycoprotein sequences</term><term>Hcvinfected patients</term><term>Healthy donors</term><term>Hepatitis</term><term>High frequency</term><term>Human sera</term><term>Hyperimmune serum</term><term>Hypervariable region</term><term>Immune</term><term>Immune response</term><term>Immune responses</term><term>Immunodominant</term><term>Long peptide</term><term>Long peptides</term><term>Medical science</term><term>Mitokor mimotopes</term><term>Moscow infection diseases hospital</term><term>Multipin technology</term><term>Olenina</term><term>Other authors</term><term>Other peptides</term><term>Patient sera</term><term>Peptide</term><term>Peptide scanning approach</term><term>Peptide synthesis</term><term>Present study</term><term>Proc natl acad</term><term>Prr1</term><term>Putative</term><term>Reactive</term><term>Room temperature</term><term>Russian academy</term><term>Serum samples</term><term>Single serum</term><term>Specialized hepatologic center</term><term>Synthetic peptides</term><term>Variable regions</term><term>Viral</term><term>Viral hepatitis</term><term>Viral replication</term><term>Viral survival</term><term>Virol</term><term>Virus clearance</term><term>Virus core</term><term>Virus infection</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Forty‐eight overlapping octapeptides covering highly conservative regions of E1 and E2 hepatitis C virus (HCV) envelope proteins were synthesized and tested by ELISA against different groups of sera obtained from HCV‐infected patients. All sera from patients with acute infection, except a single case of serum reactivity with the region HINRTALN, were nonreactive with any peptide. Sera obtained from chronic patients reacted with 12 peptides from five selected regions. Two immunodominant B epitopes were found, one being the precisely mapped antigenic site RMAWDM positioned inside the earlier shown immunodominant epitope from E1, and the second site, PALSTGLIH from E2, detected for the first time. New minor antigenic site was determined as PTDCFRKH from E2. We found only minor seroreactivity for one of the putative sites involved in CD81 binding, PYCWHYAP.</div></front></TEI><affiliations><list><country><li>Russie</li></country><region><li>District fédéral central</li></region><settlement><li>Moscou</li></settlement></list><tree><noCountry><name sortKey="Archakov, A I" sort="Archakov, A I" uniqKey="Archakov A" first="A. I." last="Archakov">A. I. 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