Antigenic domains of the open reading frame 2-encoded protein of hepatitis E virus
Identifieur interne : 003977 ( Main/Exploration ); précédent : 003976; suivant : 003978Antigenic domains of the open reading frame 2-encoded protein of hepatitis E virus
Auteurs : Y. E. Khudyakov [États-Unis, Inde] ; E. N. Lopareva [États-Unis, Inde] ; D. L. Jue [Inde, États-Unis] ; T. K. Crews [Inde, États-Unis] ; S. P. Thyagarajan [Inde] ; H. A. Fields [États-Unis, Inde]Source :
- Journal of clinical microbiology [ 0095-1137 ] ; 1999.
Descripteurs français
- KwdFr :
- MESH :
- génétique : Antigènes d'hépatite virale.
- immunologie : Anticorps de l'hépatite, Antigènes d'hépatite virale, Immunoglobuline G, Immunoglobuline M, Virus de l'hépatite E.
- Pascal (Inist)
English descriptors
- KwdEn :
- Antigenic determinant, Antigenicity, Epitopes, Hepatitis Antibodies (immunology), Hepatitis Antigens (genetics), Hepatitis Antigens (immunology), Hepatitis E virus, Hepatitis E virus (immunology), Humans, Identification, Immunoglobulin G (immunology), Immunoglobulin M (immunology), Molecular domain, Open Reading Frames, Peptides, Property structure relationship.
- MESH :
- chemical , genetics : Hepatitis Antigens.
- chemical , immunology : Hepatitis Antibodies, Hepatitis Antigens, Immunoglobulin G, Immunoglobulin M.
- chemical : Epitopes.
- immunology : Hepatitis E virus.
- Humans, Open Reading Frames.
Abstract
The antigenic composition of the hepatitis E virus (HEV) protein encoded by open reading frame 2 (ORF2) was determined by using synthetic peptides. Three sets of overlapping 18-, 25-, and 30-mer peptides, with each set spanning the entire ORF2 protein of the HEV Burma strain, were synthesized. All synthetic peptides were tested by enzyme immunoassay against a panel of 32 anti-HEV-positive serum specimens obtained from acutely HEV-infected persons. Six antigenic domains within the ORF2 protein were identified. Domains 1 and 6 located at the N and C termini of the ORF2 protein, respectively, contain strong immunoglobulin G (IgG) and IgM antigenic epitopes that can be efficiently modeled with peptides of different sizes. In contrast, antigenic epitopes identified within the two central domains (3 and 4) were modeled more efficiently with 30-mer peptides than with either 18- or 25-mers. Domain 2 located at amino acids (aa) 143 to 222 was modeled best with 25-mer peptides. A few 30-mer synthetic peptides derived from domain 5 identified at aa 490 to 579 demonstrated strong IgM antigenic reactivity. Several 30-mer synthetic peptides derived from domains 1, 4, and 6 immunoreacted with IgG or IgM with more than 70% of anti-HEV-positive serum specimens. Thus, the results of this study demonstrate the existence of six diagnostically relevant antigenic domains within the HEV ORF2 protein.
Affiliations:
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E." last="Khudyakov">Y. E. Khudyakov</name><affiliation wicri:level="2"><inist:fA14 i1="01"><s1>Hepatitis Branch, Division of Viral and Rickettsial Diseases, National Center for Infectious Diseases, Centers for Disease Control and Prevention, U. S. Department of Health and Human Services</s1><s2>Atlanta, Georgia</s2><s3>USA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>6 aut.</sZ></inist:fA14><country>États-Unis</country><placeName><region type="state">Géorgie (États-Unis)</region></placeName></affiliation><affiliation wicri:level="1"><inist:fA14 i1="02"><s1>Department of Microbiology, University of Madras</s1><s2>Madras</s2><s3>IND</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ></inist:fA14><country>Inde</country><wicri:noRegion>Madras</wicri:noRegion></affiliation></author><author><name sortKey="Lopareva, E N" sort="Lopareva, E N" uniqKey="Lopareva E" first="E. N." last="Lopareva">E. N. 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Jue</name><affiliation wicri:level="1"><inist:fA14 i1="02"><s1>Department of Microbiology, University of Madras</s1><s2>Madras</s2><s3>IND</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ></inist:fA14><country>Inde</country><wicri:noRegion>Madras</wicri:noRegion></affiliation><affiliation wicri:level="2"><inist:fA14 i1="03"><s1>Biotechnology Core Facility Branch, Scientific Resources, National Center for Infectious Diseases, Centers for Disease Control and Prevention, U. S. Department of Health and Human Services</s1><s2> Atlanta, Georgia</s2><s3>USA</s3><sZ>3 aut.</sZ><sZ>4 aut.</sZ></inist:fA14><country>États-Unis</country><placeName><region type="state">Géorgie (États-Unis)</region></placeName></affiliation></author><author><name sortKey="Crews, T K" sort="Crews, T K" uniqKey="Crews T" first="T. K." last="Crews">T. K. 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Thyagarajan</name><affiliation wicri:level="1"><inist:fA14 i1="02"><s1>Department of Microbiology, University of Madras</s1><s2>Madras</s2><s3>IND</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ></inist:fA14><country>Inde</country><wicri:noRegion>Madras</wicri:noRegion></affiliation></author><author><name sortKey="Fields, H A" sort="Fields, H A" uniqKey="Fields H" first="H. A." last="Fields">H. A. Fields</name><affiliation wicri:level="2"><inist:fA14 i1="01"><s1>Hepatitis Branch, Division of Viral and Rickettsial Diseases, National Center for Infectious Diseases, Centers for Disease Control and Prevention, U. S. Department of Health and Human Services</s1><s2>Atlanta, Georgia</s2><s3>USA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>6 aut.</sZ></inist:fA14><country>États-Unis</country><placeName><region type="state">Géorgie (États-Unis)</region></placeName></affiliation><affiliation wicri:level="1"><inist:fA14 i1="02"><s1>Department of Microbiology, University of Madras</s1><s2>Madras</s2><s3>IND</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ></inist:fA14><country>Inde</country><wicri:noRegion>Madras</wicri:noRegion></affiliation></author></analytic><series><title level="j" type="main">Journal of clinical microbiology</title><title level="j" type="abbreviated">J. clin. microbiol.</title><idno type="ISSN">0095-1137</idno><imprint><date when="1999">1999</date></imprint></series></biblStruct></sourceDesc><seriesStmt><title level="j" type="main">Journal of clinical microbiology</title><title level="j" type="abbreviated">J. clin. microbiol.</title><idno type="ISSN">0095-1137</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antigenic determinant</term><term>Antigenicity</term><term>Epitopes</term><term>Hepatitis Antibodies (immunology)</term><term>Hepatitis Antigens (genetics)</term><term>Hepatitis Antigens (immunology)</term><term>Hepatitis E virus</term><term>Hepatitis E virus (immunology)</term><term>Humans</term><term>Identification</term><term>Immunoglobulin G (immunology)</term><term>Immunoglobulin M (immunology)</term><term>Molecular domain</term><term>Open Reading Frames</term><term>Peptides</term><term>Property structure relationship</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Anticorps de l'hépatite (immunologie)</term><term>Antigènes d'hépatite virale (génétique)</term><term>Antigènes d'hépatite virale (immunologie)</term><term>Cadres ouverts de lecture</term><term>Humains</term><term>Immunoglobuline G (immunologie)</term><term>Immunoglobuline M (immunologie)</term><term>Virus de l'hépatite E (immunologie)</term><term>Épitopes</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Hepatitis Antigens</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Hepatitis Antibodies</term><term>Hepatitis Antigens</term><term>Immunoglobulin G</term><term>Immunoglobulin M</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Epitopes</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Antigènes d'hépatite virale</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Anticorps de l'hépatite</term><term>Antigènes d'hépatite virale</term><term>Immunoglobuline G</term><term>Immunoglobuline M</term><term>Virus de l'hépatite E</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Hepatitis E virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term><term>Open Reading Frames</term></keywords><keywords scheme="Pascal" xml:lang="fr"><term>Cadres ouverts de lecture</term><term>Humains</term><term>Virus hépatite E</term><term>Déterminant antigénique</term><term>Peptide</term><term>Identification</term><term>Relation structure propriété</term><term>Domaine moléculaire</term><term>Antigénicité</term><term>Protéine ORF2</term><term>Épitopes</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The antigenic composition of the hepatitis E virus (HEV) protein encoded by open reading frame 2 (ORF2) was determined by using synthetic peptides. Three sets of overlapping 18-, 25-, and 30-mer peptides, with each set spanning the entire ORF2 protein of the HEV Burma strain, were synthesized. All synthetic peptides were tested by enzyme immunoassay against a panel of 32 anti-HEV-positive serum specimens obtained from acutely HEV-infected persons. Six antigenic domains within the ORF2 protein were identified. Domains 1 and 6 located at the N and C termini of the ORF2 protein, respectively, contain strong immunoglobulin G (IgG) and IgM antigenic epitopes that can be efficiently modeled with peptides of different sizes. In contrast, antigenic epitopes identified within the two central domains (3 and 4) were modeled more efficiently with 30-mer peptides than with either 18- or 25-mers. Domain 2 located at amino acids (aa) 143 to 222 was modeled best with 25-mer peptides. A few 30-mer synthetic peptides derived from domain 5 identified at aa 490 to 579 demonstrated strong IgM antigenic reactivity. Several 30-mer synthetic peptides derived from domains 1, 4, and 6 immunoreacted with IgG or IgM with more than 70% of anti-HEV-positive serum specimens. Thus, the results of this study demonstrate the existence of six diagnostically relevant antigenic domains within the HEV ORF2 protein.</div></front></TEI><affiliations><list><country><li>Inde</li><li>États-Unis</li></country><region><li>Géorgie (États-Unis)</li></region></list><tree><country name="États-Unis"><region name="Géorgie (États-Unis)"><name sortKey="Khudyakov, Y E" sort="Khudyakov, Y E" uniqKey="Khudyakov Y" first="Y. E." last="Khudyakov">Y. E. Khudyakov</name></region><name sortKey="Crews, T K" sort="Crews, T K" uniqKey="Crews T" first="T. K." last="Crews">T. K. Crews</name><name sortKey="Fields, H A" sort="Fields, H A" uniqKey="Fields H" first="H. A." last="Fields">H. A. Fields</name><name sortKey="Jue, D L" sort="Jue, D L" uniqKey="Jue D" first="D. L." last="Jue">D. L. Jue</name><name sortKey="Lopareva, E N" sort="Lopareva, E N" uniqKey="Lopareva E" first="E. N." last="Lopareva">E. N. Lopareva</name></country><country name="Inde"><noRegion><name sortKey="Khudyakov, Y E" sort="Khudyakov, Y E" uniqKey="Khudyakov Y" first="Y. E." last="Khudyakov">Y. E. Khudyakov</name></noRegion><name sortKey="Crews, T K" sort="Crews, T K" uniqKey="Crews T" first="T. K." last="Crews">T. K. Crews</name><name sortKey="Fields, H A" sort="Fields, H A" uniqKey="Fields H" first="H. A." last="Fields">H. A. Fields</name><name sortKey="Jue, D L" sort="Jue, D L" uniqKey="Jue D" first="D. L." last="Jue">D. L. Jue</name><name sortKey="Lopareva, E N" sort="Lopareva, E N" uniqKey="Lopareva E" first="E. N." last="Lopareva">E. N. Lopareva</name><name sortKey="Thyagarajan, S P" sort="Thyagarajan, S P" uniqKey="Thyagarajan S" first="S. P." last="Thyagarajan">S. P. Thyagarajan</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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