Residues involved in the antigenic sites of transmissible gastroenteritis coronavirus S glycoprotein

The S glycoprotein of transmissible gastroenteritis virus (TGEV) has been shown to contain four major antigenic sites (A, B, C, and D). Site A is the main inducer of neutralizing antibodies and has been previously subdivided into the three subsites Aa, Ab, and Ac. The residues that contribute to the...

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Published inVirology (New York, N.Y.) Vol. 183; no. 1; pp. 225 - 238
Main Authors Gebauer, Fátima, Posthumus, Willem P.A., Correa, Isabel, Sae, Carlos, Smerdou, Cristian, Sanchez, Carlos M., Lenstra, Johannes A., Meloen, Rob H., Enjuanes, Luis
Format Journal Article
LanguageEnglish
Published San Diego, CA Elsevier Inc 01.07.1991
Elsevier
Published by Elsevier Inc
Subjects
ACIDE AMINE
Amino Acid Sequence
AMINOACIDOS
Animals
Antibodies, Monoclonal - immunology
ANTICORPS MONOCLONAL
ANTICUERPOS MONOCLONALES
ANTIGENE
ANTIGENOS
Antigens, Viral - analysis
Base Sequence
Biological and medical sciences
Cells, Cultured
DNA, Viral - chemistry
Epitopes - analysis
Fundamental and applied biological sciences. Psychology
GLICOPROTEINAS
GLYCOPROTEINE
Glycosylation
Microbiology
Molecular Sequence Data
Morphology, structure, chemical composition, physicochemical properties
MUTANT
MUTANTES
Mutation
NUCLEOTIDE
NUCLEOTIDOS
REACCION ANTIGENO-ANTICUERPO
REACTION ANTIGENE ANTICORPS
RNA, Viral - chemistry
Software
Swine
Transmissible gastroenteritis virus - immunology
Viral Proteins - genetics
Viral Proteins - immunology
Virology
VIRUS GASTROENTERITE DU PORC
VIRUS GASTROENTERITIS TRANSMISIBLE
Virus
Resistance
Coronavirus
Antigenic determinant
Peptides
Monoclonal antibody
Mutation
Coronaviridae
Porcine transmissible gastroenteritis virus
Online AccessGet full text

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Abstract The S glycoprotein of transmissible gastroenteritis virus (TGEV) has been shown to contain four major antigenic sites (A, B, C, and D). Site A is the main inducer of neutralizing antibodies and has been previously subdivided into the three subsites Aa, Ab, and Ac. The residues that contribute to these sites were localized by sequence analysis of 21 mutants that escaped neutralization or binding by TGEV-specific monoclonal antibodies (MAbs), and by epitope scanning (PEPSCAN). Site A contains the residues 538, 591, and 543, which are essential in the formation of subsites Aa, Ab, and Ac, respectively. In addition, mar mutant 1B.H6 with residue 586 changed had partially altered both subsite Aa and Ab, indicating that these subsites overlap in residue 586; i.e. this residue also is part of site A. The peptide 537-MKSGYGQPIA-547 represents, at least partially, subsite Ac which is highly conserved among coronaviruses. This site is relevant for diagnosis and could be of interest for protection. Other residues contribute to site B (residues 97 and 144), site C (residues 50 and 51), and site D (residue 385). The location of site D is in agreement with PEPSCAN results. Site C can be represented by the peptide 48-P-P/S-N-S-D/E-52 but is not exposed on the surface of native virus. Its accessibility can be modulated by treatment at pH >11 (at 4°) and temperatures >45°. Sites A and B are fully dependent on glycosylation for proper folding, while sites C and D are fully or partially independent of glycosylation, respectively. Once the S glycoprotein has been assembled into the virion, the carbohydrate moiety is not essential for the antigenic sites.
AbstractList The S glycoprotein of transmissible gastroenteritis virus (TGEV) has been shown to contain four major antigenic sites (A, B, C, and D). Site A is the main inducer of neutralizing antibodies and has been previously subdivided into the three subsites Aa, Ab, and Ac. The residues that contribute to these sites were localized by sequence analysis of 21 mutants that escaped neutralization or binding by TGEV-specific monoclonal antibodies (MAbs), and by epitope scanning (PEPSCAN). Site A contains the residues 538, 591, and 543, which are essential in the formation of subsites Aa, Ab, and Ac, respectively. In addition, mar mutant 1 B.H6 with residue 586 changed had partially altered both subsite Aa and Ab, indicating that these subsites overlap in residue 586; i.e. this residue also is part of site A. The peptide 537-MKSGYGQPIA-547 represents, at least partially, subsite Ac which is highly conserved among coronaviruses. This site is relevant for diagnosis and could be of interest for protection. Other residues contribute to site B (residues 97 and 144), site C (residues 50 and 51), and site D (residue 385). The location of site D is in agreement with PEPSCAN results. Site C can be represented by the peptide 48-P-P/S-N-S-D/E-52 but is not exposed on the surface of native virus. Its accessibility can be modulated by treatment at pH 11 (at 4 degrees) and temperatures 45 degrees. Sites A and B are fully dependent on glycosylation for proper folding, while sites C and D are fully or partially independent of glycosylation, respectively. Once the S glycoprotein has been assembled into the virion, the carbohydrate moiety is not essential for the antigenic sites
The S glycoprotein of transmissible gastroenteritis virus (TGEV) has been shown to contain four major antigenic sites (A, B, C, and D). Site A is the main inducer of neutralizing antibodies and has been previously subdivided into the three subsites Aa, Ab, and Ac. The residues that contribute to these sites were localized by sequence analysis of 21 mutants that escaped neutralization or binding by TGEV-specific monoclonal antibodies (MAbs), and by epitope scanning (PEPSCAN). Site A contains the residues 538, 591, and 543, which are essential in the formation of subsites Aa, Ab, and Ac, respectively. In addition, mar mutant 1B.H6 with residue 586 changed had partially altered both subsite Aa and Ab, indicating that these subsites overlap in residue 586; i.e. this residue also is part of site A. The peptide 537-MKSGYGQPIA-547 represents, at least partially, subsite Ac which is highly conserved among coronaviruses. This site is relevant for diagnosis and could be of interest for protection. Other residues contribute to site B (residues 97 and 144), site C (residues 50 and 51), and site D (residue 385). The location of site D is in agreement with PEPSCAN results. Site C can be represented by the peptide 48-P-P/S-N-S-D/E-52 but is not exposed on the surface of native virus. Its accessibility can be modulated by treatment at pH >11 (at 4°) and temperatures >45°. Sites A and B are fully dependent on glycosylation for proper folding, while sites C and D are fully or partially independent of glycosylation, respectively. Once the S glycoprotein has been assembled into the virion, the carbohydrate moiety is not essential for the antigenic sites.
The S glycoprotein of transmissible gastroenteritis virus (TGEV) has been shown to contain four major antigenic sites (A, B, C, and D). Site A is the main inducer of neutralizing antibodies and has been previously subdivided into the three subsites Aa, Ab, and Ac. The residues that contribute to these sites were localized by sequence analysis of 21 mutants that escaped neutralization or binding by TGEV-specific monoclonal antibodies (MAbs), and by epitope scanning (PEPSCAN). Site A contains the residues 538, 591, and 543, which are essential in the formation of subsites Aa, Ab, and Ac, respectively. In addition, mar mutant 1B.H6 with residue 586 changed had partially altered both subsite Aa and Ab, indicating that these subsites overlap in residue 586; i.e. this residue also is part of site A. The peptide 537-MKSGYGQPIA-547 represents, at least partially, subsite Ac which is highly conserved among coronaviruses. This site is relevant for diagnosis and could be of interest for protection. Other residues contribute to site B (residues 97 and 144), site C (residues 50 and 51), and site D (residue 385). The location of site D is in agreement with PEPSCAN results. Site C can be represented by the peptide 48-P-P/S-N-S-D/E-52 but is not exposed on the surface of native virus. Its accessibility can be modulated by treatment at pH greater than 11 (at 4 degrees) and temperatures greater than 45 degrees. Sites A and B are fully dependent on glycosylation for proper folding, while sites C and D are fully or partially independent of glycosylation, respectively. Once the S glycoprotein has been assembled into the virion, the carbohydrate moiety is not essential for the antigenic sites.
The S glycoprotein of transmissible gastroenteritis virus (TGEV) has been shown to contain four major antigenic sites (A, B, C, and D). Site A is the main inducer of neutralizing antibodies and has been previously subdivided into the three subsites Aa, Ab, and Ac. The residues that contribute to these sites were localized by sequence analysis of 21 mutants that escaped neutralization or binding by TGEV-specific monoclonal antibodies (MAbs), and by epitope scanning (PEPSCAN). Site A contains the residues 538, 591, and 543, which are essential in the formation of subsites Aa, Ab, and Ac, respectively. In addition, mar mutant 1B.H6 with residue 586 changed had partially altered both subsite Aa and Ab, indicating that these subsites overlap in residue 586; i.e. this residue also is part of site A. The peptide 537-MKSGYGQPIA-547 represents, at least partially, subsite Ac which is highly conserved among coronaviruses. This site is relevant for diagnosis and could be of interest for protection. Other residues contribute to site B (residues 97 and 144), site C (residues 50 and 51), and site D (residue 385). The location of site D is in agreement with PEPSCAN results. Site C can be represented by the peptide 48-P-P/S-N-S-D/E-52 but is not exposed on the surface of native virus. Its accessibility can be modulated by treatment at pH >11 (at 4°) and temperatures >45°. Sites A and B are fully dependent on glycosylation for proper folding, while sites C and D are fully or partially independent of glycosylation, respectively. Once the S glycoprotein has been assembled into the virion, the carbohydrate moiety is not essential for the antigenic sites.
Author Sae, Carlos
Posthumus, Willem P.A.
Lenstra, Johannes A.
Enjuanes, Luis
Sanchez, Carlos M.
Smerdou, Cristian
Correa, Isabel
Meloen, Rob H.
Gebauer, Fátima
AuthorAffiliation c lnstitute of Infectious Diseases and Immunology, Veterinary Faculty, State University, P.O. Box 80, 165, 3508 TD Utrecht, The Netherlands
a Centro de Biología Molecular, CSIC-Universidad Autónoma, Canto Blanco, 28049 Madrid, Spain
b Central Veterinary Institute, P.O. Box 65, 8200 AB Lelystad, The Netherlands
AuthorAffiliation_xml – name: b Central Veterinary Institute, P.O. Box 65, 8200 AB Lelystad, The Netherlands
– name: a Centro de Biología Molecular, CSIC-Universidad Autónoma, Canto Blanco, 28049 Madrid, Spain
– name: c lnstitute of Infectious Diseases and Immunology, Veterinary Faculty, State University, P.O. Box 80, 165, 3508 TD Utrecht, The Netherlands
Author_xml – sequence: 1
  givenname: Fátima
  surname: Gebauer
  fullname: Gebauer, Fátima
  organization: Centro de Biología Molecular, CSIC-Universidad Autónoma, Canto Blanco, 28049 Madrid, Spain
– sequence: 2
  givenname: Willem P.A.
  surname: Posthumus
  fullname: Posthumus, Willem P.A.
  organization: Central Veterinary Institute, P.O. Box 65, 8200 AB Lelystad, The Netherlands
– sequence: 3
  givenname: Isabel
  surname: Correa
  fullname: Correa, Isabel
  organization: Centro de Biología Molecular, CSIC-Universidad Autónoma, Canto Blanco, 28049 Madrid, Spain
– sequence: 4
  givenname: Carlos
  surname: Sae
  fullname: Sae, Carlos
  organization: Centro de Biología Molecular, CSIC-Universidad Autónoma, Canto Blanco, 28049 Madrid, Spain
– sequence: 5
  givenname: Cristian
  surname: Smerdou
  fullname: Smerdou, Cristian
  organization: Centro de Biología Molecular, CSIC-Universidad Autónoma, Canto Blanco, 28049 Madrid, Spain
– sequence: 6
  givenname: Carlos M.
  surname: Sanchez
  fullname: Sanchez, Carlos M.
  organization: Centro de Biología Molecular, CSIC-Universidad Autónoma, Canto Blanco, 28049 Madrid, Spain
– sequence: 7
  givenname: Johannes A.
  surname: Lenstra
  fullname: Lenstra, Johannes A.
  organization: lnstitute of Infectious Diseases and Immunology, Veterinary Faculty, State University, P.O. Box 80, 165, 3508 TD Utrecht, The Netherlands
– sequence: 8
  givenname: Rob H.
  surname: Meloen
  fullname: Meloen, Rob H.
  organization: Central Veterinary Institute, P.O. Box 65, 8200 AB Lelystad, The Netherlands
– sequence: 9
  givenname: Luis
  surname: Enjuanes
  fullname: Enjuanes, Luis
  organization: Centro de Biología Molecular, CSIC-Universidad Autónoma, Canto Blanco, 28049 Madrid, Spain
BackLink http://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4980870$$DView record in Pascal Francis
https://www.ncbi.nlm.nih.gov/pubmed/1711257$$D View this record in MEDLINE/PubMed
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Cites_doi 10.1007/978-1-4757-0456-3_11
10.1016/0042-6822(89)90061-5
10.1016/0042-6822(86)90328-4
10.1099/0022-1317-71-6-1313
10.1016/0168-1702(90)90051-C
10.1099/0022-1317-70-12-3281
10.1016/0168-1702(88)90059-7
10.1099/0022-1317-69-12-2939
10.1016/0168-1702(87)90008-6
10.1126/science.3008333
10.1099/0022-1317-67-7-1405
10.1016/0042-6822(89)90619-3
10.1016/0378-1135(79)90034-8
10.1016/0042-6822(82)90095-2
10.1016/S0021-9258(18)38002-5
10.1099/0022-1317-71-2-271
10.1128/jvi.64.3.1283-1289.1990
10.1128/jvi.56.3.904-911.1985
10.1099/0022-1317-70-6-1493
10.1099/0022-1317-68-7-1883
10.1128/jvi.62.6.1870-1874.1988
10.1007/978-1-4684-5823-7_41
10.1016/0168-1702(90)90090-X
10.1016/0042-6822(90)90521-R
10.1128/iai.6.3.289-301.1972
10.1128/jvi.60.1.131-139.1986
10.1128/jvi.53.1.128-136.1985
10.1016/0042-6822(90)90094-8
10.1128/jvi.64.7.3304-3309.1990
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Issue 1
Keywords Virus
Resistance
Coronavirus
Antigenic determinant
Peptides
Monoclonal antibody
Mutation
Coronaviridae
Porcine transmissible gastroenteritis virus
Language English
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References Posthumus, Lenstra, Schaaper, van Niewstadt, Enjuanes, Meloen (BIB24) 1990; 64
Spaan, Cavanagh, Horzineck (BIB29) 1990
Suñé, Jiménez, Correa, Bullido, Gebauer, Smerdou, Enjuanes (BIB31) 1990; 177
Parry, Barnett, Ouldridge, Rowlands, Brown (BIB23) 1989; 70
Holmes, Williams, Stephensen (BIB16) 1989
McClurkin, Norman (BIB21) 1966; 30
Britton, Page (BIB2) 1990; 18
Collins, Knobler, Powell, Buchmeier (BIB3) 1982; 119
Laviada, Videgain, Moreno, Alonso, Enjuanes, Escribano (BIB19) 1990; 16
Taniguchi, Hoshino, Nishikawa, Green, Maloy, Morita, Urasawa, Kapikian, Chanock, Gorziglia (BIB33) 1988; 62
Sánchez, Jiménez, Laviada, Correa, Suñé, Bullido, Gebauer, Smerdou, Callebaut, Escribano, Enjuanes (BIB26) 1990; 174
Spaan, Cavanagh, Horzinek (BIB28) 1988; 69
Enjuanes, Van Der Zeijst (BIB12) 1991
Rasschaert, Laude (BIB25) 1987; 68
Davies, Sheriff, Padlan (BIB6) 1988; 263
Sanger, Nicklen, Coulson (BIB27) 1977; 74
Wiegers, Wetz, Dernick (BIB36) 1990; 64
Bohl, Gupta, Olquín, Saif (BIB1) 1972; 6
DiMarchi, Brook, Gale, Crancknell, Doel, Mowat (BIB11) 1986; 232
Sturman, Ricard, Holmes (BIB30) 1985; 56
Wesley (BIB35) 1990; 276
Garwes, Lucas, Higgins, Pike, Cartwright (BIB13) 1978; 3
Jiménez, Correa, Melgosa, Bullido, Enjuanes (BIB18) 1986; 60
Lenstra, Erkens, Zwaagstra, Posthumus, Meloen, Gebauer, Enjuanes, Stanley (BIB20) 1991
Delmas, Gelfi, Laude (BIB8) 1986; 67
Correa, Gebauer, Bullido, Suñé, Baay, Zwaagstra, Posthumus, Lenstra, Enjuanes (BIB4) 1990; 71
Taguchi, Fleming (BIB32) 1989; 169
Delmas, Rasschaert, Godet, Gelfi, Laude (BIB9) 1990; 71
Correa, Jiménez, Suñé, Bullido, Enjuanes (BIB5) 1988; 10
De Groot, Van Leen, Dalderup, Vennema, Horzineck, Spaan (BIB7) 1989; 171
Díez, Mated, Domingo (BIB10) 1989; 70
Geysen, Meloen, Barteling (BIB14) 1984; 81
Holmes, Roller, Behnke (BIB15) 1981; 142
Jacobs, de Groot, Van Der Zeijst, Horzineck, Spaan (BIB17) 1987; 8
Zimmern, Kaesberg (BIB37) 1978; 75
Marlin, Holland, Levine, Glorioso (BIB22) 1985; 53
Vandepol, Lefrancois, Holland (BIB34) 1986; 148
Bohl (10.1016/0042-6822(91)90135-X_BIB1) 1972; 6
Suñé (10.1016/0042-6822(91)90135-X_BIB31) 1990; 177
Enjuanes (10.1016/0042-6822(91)90135-X_BIB12) 1991
Marlin (10.1016/0042-6822(91)90135-X_BIB22) 1985; 53
Vandepol (10.1016/0042-6822(91)90135-X_BIB34) 1986; 148
McClurkin (10.1016/0042-6822(91)90135-X_BIB21) 1966; 30
Britton (10.1016/0042-6822(91)90135-X_BIB2) 1990; 18
Wesley (10.1016/0042-6822(91)90135-X_BIB35) 1990; 276
Posthumus (10.1016/0042-6822(91)90135-X_BIB24) 1990; 64
Garwes (10.1016/0042-6822(91)90135-X_BIB13) 1978; 3
Delmas (10.1016/0042-6822(91)90135-X_BIB8) 1986; 67
Correa (10.1016/0042-6822(91)90135-X_BIB4) 1990; 71
Collins (10.1016/0042-6822(91)90135-X_BIB3) 1982; 119
Delmas (10.1016/0042-6822(91)90135-X_BIB9) 1990; 71
Jiménez (10.1016/0042-6822(91)90135-X_BIB18) 1986; 60
Spaan (10.1016/0042-6822(91)90135-X_BIB29) 1990
Taguchi (10.1016/0042-6822(91)90135-X_BIB32) 1989; 169
Holmes (10.1016/0042-6822(91)90135-X_BIB15) 1981; 142
Spaan (10.1016/0042-6822(91)90135-X_BIB28) 1988; 69
Wiegers (10.1016/0042-6822(91)90135-X_BIB36) 1990; 64
Correa (10.1016/0042-6822(91)90135-X_BIB5) 1988; 10
Taniguchi (10.1016/0042-6822(91)90135-X_BIB33) 1988; 62
Díez (10.1016/0042-6822(91)90135-X_BIB10) 1989; 70
Jacobs (10.1016/0042-6822(91)90135-X_BIB17) 1987; 8
Sanger (10.1016/0042-6822(91)90135-X_BIB27) 1977; 74
Geysen (10.1016/0042-6822(91)90135-X_BIB14) 1984; 81
Sturman (10.1016/0042-6822(91)90135-X_BIB30) 1985; 56
Lenstra (10.1016/0042-6822(91)90135-X_BIB20) 1991
DiMarchi (10.1016/0042-6822(91)90135-X_BIB11) 1986; 232
Rasschaert (10.1016/0042-6822(91)90135-X_BIB25) 1987; 68
Holmes (10.1016/0042-6822(91)90135-X_BIB16) 1989
Zimmern (10.1016/0042-6822(91)90135-X_BIB37) 1978; 75
Sánchez (10.1016/0042-6822(91)90135-X_BIB26) 1990; 174
Laviada (10.1016/0042-6822(91)90135-X_BIB19) 1990; 16
De Groot (10.1016/0042-6822(91)90135-X_BIB7) 1989; 171
Parry (10.1016/0042-6822(91)90135-X_BIB23) 1989; 70
Davies (10.1016/0042-6822(91)90135-X_BIB6) 1988; 263
References_xml – volume: 10
  start-page: 77
  year: 1988
  end-page: 94
  ident: BIB5
  article-title: Antigenic structure of the E2 glycoprotein from transmissible gastroenteritis coronavirus
  publication-title: Virus Res.
  contributor:
    fullname: Enjuanes
– volume: 232
  start-page: 639
  year: 1986
  end-page: 641
  ident: BIB11
  article-title: A mutation in the R body-coding sequence destroys expression of the killer trait in P. Tetraurelia
  publication-title: Science
  contributor:
    fullname: Mowat
– volume: 30
  start-page: 190
  year: 1966
  end-page: 198
  ident: BIB21
  article-title: Studies on transmissible gastroenteritis of swine. II. Selected characteristics of a cytopathogenic virus common to five isolates from transmissible gastroenteritis
  publication-title: Can. J. Comp. Vet. Sci.
  contributor:
    fullname: Norman
– volume: 75
  start-page: 4257
  year: 1978
  end-page: 4261
  ident: BIB37
  article-title: 3′-Terminal nucleotide sequence of encephalomyocarditis virus RNA determined by reverse transcriptase and chain-terminating inhibitors
  publication-title: Proc. Natl. Acad. Sci. USA
  contributor:
    fullname: Kaesberg
– volume: 81
  start-page: 3998
  year: 1984
  end-page: 4002
  ident: BIB14
  article-title: Use of peptide synthesis to probe viral antigens for epitopes to a resolution of a single amino acid
  publication-title: Proc. Natl. Acad. Sci. USA
  contributor:
    fullname: Barteling
– volume: 64
  start-page: 3304
  year: 1990
  end-page: 3309
  ident: BIB24
  article-title: Analysis and simulation of a neutralizing epitope of transmissible gastroenteritis virus
  publication-title: J. Virol.
  contributor:
    fullname: Meloen
– volume: 62
  start-page: 1870
  year: 1988
  end-page: 1874
  ident: BIB33
  article-title: Cross-reactive and serotype-specific neutralization epitopes on VP7 of human rotavirus: Nucleotide sequence analysis of antigenic mutants selected with monoclonal antibodies
  publication-title: J. Virol.
  contributor:
    fullname: Gorziglia
– volume: 71
  start-page: 1313
  year: 1990
  end-page: 1323
  ident: BIB9
  article-title: Four major antigenic sites of the coronavirus transmissible gastroenteritis virus are located on the amino-terminal half of spike glycoprotein S
  publication-title: J. Gen. Virol.
  contributor:
    fullname: Laude
– volume: 56
  start-page: 904
  year: 1985
  end-page: 911
  ident: BIB30
  article-title: Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: Activation of cell-fusing activity of virions by trypsin and separation of two different 90K cleavage fragments
  publication-title: J. Virol.
  contributor:
    fullname: Holmes
– start-page: 106
  year: 1989
  end-page: 113
  ident: BIB16
  article-title: Coronavirus Receptors
  publication-title: Concepts in Viral Pathogenesis III
  contributor:
    fullname: Stephensen
– volume: 16
  start-page: 247
  year: 1990
  end-page: 254
  ident: BIB19
  article-title: Expression of swine transmissible gastroenteritis virus envelope antigens on the surface of infected cells: Epitopes externally exposed
  publication-title: Virus Res.
  contributor:
    fullname: Escribano
– volume: 3
  start-page: 179
  year: 1978
  end-page: 190
  ident: BIB13
  article-title: Antigenicity of structural components from porcine transmissible gastroenteritis virus
  publication-title: Vet. Microbiol.
  contributor:
    fullname: Cartwright
– volume: 174
  start-page: 410
  year: 1990
  end-page: 417
  ident: BIB26
  article-title: Antigenic homology among coronaviruses related to transmissible gastroenteritis virus
  publication-title: Virology
  contributor:
    fullname: Enjuanes
– volume: 142
  start-page: 133
  year: 1981
  end-page: 142
  ident: BIB15
  article-title: Analysis of the functions of coronavirus glycoproteins by differential inhibition of synthesis with tunicamycin
  publication-title: Adv. Exp. Med. Biol.
  contributor:
    fullname: Behnke
– year: 1991
  ident: BIB20
  article-title: Selection of mimotopes from a random sequence expression library using monoclonal antibodies against transmissible gastroenteritis coronavirus
  publication-title: J. Immunol.
  contributor:
    fullname: Stanley
– start-page: 359
  year: 1990
  end-page: 379
  ident: BIB29
  article-title: Coronaviruses
  publication-title: Immunochemistry of Viruses. II. The Basis for Serodiagnosis and Vaccines
  contributor:
    fullname: Horzineck
– volume: 263
  start-page: 10,541
  year: 1988
  end-page: 10,544
  ident: BIB6
  article-title: Antibody-antigen complexes
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Padlan
– volume: 60
  start-page: 131
  year: 1986
  end-page: 139
  ident: BIB18
  article-title: Critical epitopes in transmissible gastroenteritis virus neutralization
  publication-title: J. Virol.
  contributor:
    fullname: Enjuanes
– volume: 68
  start-page: 1883
  year: 1987
  end-page: 1890
  ident: BIB25
  article-title: The predicted primary structure of the peplomer protein E2 of the porcine coronavirus transmissible gastroenteritis virus
  publication-title: J. Gen. Virol.
  contributor:
    fullname: Laude
– volume: 70
  start-page: 3281
  year: 1989
  end-page: 3289
  ident: BIB10
  article-title: Selection of antigenic variants of foot-and-mouth disease virus in the absence of antibodies, as revealed by an
  publication-title: J. Gen. Virol.
  contributor:
    fullname: Domingo
– volume: 53
  start-page: 128
  year: 1985
  end-page: 136
  ident: BIB22
  article-title: Epitopes of herpes simplex virus type 1 glycoprotein gC are clustered in two distinct antigenic sites
  publication-title: J. Virol.
  contributor:
    fullname: Glorioso
– volume: 74
  start-page: 5463
  year: 1977
  end-page: 5467
  ident: BIB27
  article-title: DNA sequencing with chain-terminating inhibitors
  publication-title: Proc. Natl. Acad. Sci. USA
  contributor:
    fullname: Coulson
– volume: 148
  start-page: 312
  year: 1986
  end-page: 325
  ident: BIB34
  article-title: Sequences of the major antibody binding epitopes of the Indiana serotype of vesicular stomatitis virus
  publication-title: Virology
  contributor:
    fullname: Holland
– volume: 8
  start-page: 363
  year: 1987
  end-page: 371
  ident: BIB17
  article-title: The nucleotide sequence of the peplomer gene of porcine transmissible gastroenteritis virus (TGEV): Comparison with the sequence of the peplomer protein of feline infectious peritonitis virus (FIPV)
  publication-title: Virus Res.
  contributor:
    fullname: Spaan
– volume: 70
  start-page: 1493
  year: 1989
  end-page: 1503
  ident: BIB23
  article-title: Neutralizing epitopes of type 0 foot-and-mouth virus. II. Mapping three conformational sites with synthetic peptide reagents
  publication-title: J. Gen. Virol.
  contributor:
    fullname: Brown
– volume: 6
  start-page: 289
  year: 1972
  end-page: 301
  ident: BIB1
  article-title: Antibody responses in serum, colostrum and milk of swine after infection or vaccination with transmissible gastroenteritis virus
  publication-title: Infect. Immun.
  contributor:
    fullname: Saif
– volume: 71
  start-page: 271
  year: 1990
  end-page: 279
  ident: BIB4
  article-title: Localization of antigenic sites of the E2 glycoprotein of transmissible gastroenteritis coronavirus
  publication-title: J. Gen. Virol.
  contributor:
    fullname: Enjuanes
– year: 1991
  ident: BIB12
  article-title: Molecular basis of transmissible gastroenteritis coronavirus (TGEV) epidemiology
  publication-title: The Coronaviruses
  contributor:
    fullname: Van Der Zeijst
– volume: 276
  start-page: 301
  year: 1990
  end-page: 306
  ident: BIB35
  article-title: Nucleotide sequence of the E2-peplomer protein gene and partial nucleotide sequence of the upstream polymerase gene of transmissible gastroenteritis virus (Miller strain)
  publication-title: Adv. Exp. Med. Biol.
  contributor:
    fullname: Wesley
– volume: 119
  start-page: 358
  year: 1982
  end-page: 371
  ident: BIB3
  article-title: Monoclonal antibodies to murine hepatitis virus-4 (strain JHM) define the viral glycoprotein responsible for attachment and cell-cell fusion
  publication-title: Virology
  contributor:
    fullname: Buchmeier
– volume: 169
  start-page: 223
  year: 1989
  end-page: 235
  ident: BIB32
  article-title: Comparison of six different murine coronavirus JHM variants by monoclonal antibodies against the E2 glycoprotein
  publication-title: Virology
  contributor:
    fullname: Fleming
– volume: 171
  start-page: 493
  year: 1989
  end-page: 502
  ident: BIB7
  article-title: Stably expressed FIPV peplomer protein induces cell fusion and elicits neutralizing antibodies in mice
  publication-title: Virology
  contributor:
    fullname: Spaan
– volume: 67
  start-page: 1405
  year: 1986
  end-page: 1418
  ident: BIB8
  article-title: Antigenic structure of transmissible gastroenteritis virus. II. Domains in the peplomer glycoprotein
  publication-title: J. Gen. Virol.
  contributor:
    fullname: Laude
– volume: 69
  start-page: 2939
  year: 1988
  end-page: 2952
  ident: BIB28
  article-title: Coronaviruses: Structure and genome expression
  publication-title: J. Gen. Virol.
  contributor:
    fullname: Horzinek
– volume: 177
  start-page: 559
  year: 1990
  end-page: 569
  ident: BIB31
  article-title: Mechanisms of transmissible gastroenteritis coronavirus neutralization
  publication-title: Virology
  contributor:
    fullname: Enjuanes
– volume: 18
  start-page: 71
  year: 1990
  end-page: 80
  ident: BIB2
  article-title: Sequence of the S-gene from a virulent British field isolate of transmissible gastroenteritis virus
  publication-title: Virus Res.
  contributor:
    fullname: Page
– volume: 64
  start-page: 1283
  year: 1990
  end-page: 1289
  ident: BIB36
  article-title: Molecular basis for linkage of a continuous and discontinuous neutralization epitope on the structural polypeptlde VP2 of poliovirus type 1
  publication-title: J. Virol.
  contributor:
    fullname: Dernick
– volume: 142
  start-page: 133
  year: 1981
  ident: 10.1016/0042-6822(91)90135-X_BIB15
  article-title: Analysis of the functions of coronavirus glycoproteins by differential inhibition of synthesis with tunicamycin
  publication-title: Adv. Exp. Med. Biol.
  doi: 10.1007/978-1-4757-0456-3_11
  contributor:
    fullname: Holmes
– start-page: 106
  year: 1989
  ident: 10.1016/0042-6822(91)90135-X_BIB16
  article-title: Coronavirus Receptors
  contributor:
    fullname: Holmes
– volume: 169
  start-page: 223
  year: 1989
  ident: 10.1016/0042-6822(91)90135-X_BIB32
  article-title: Comparison of six different murine coronavirus JHM variants by monoclonal antibodies against the E2 glycoprotein
  publication-title: Virology
  doi: 10.1016/0042-6822(89)90061-5
  contributor:
    fullname: Taguchi
– volume: 148
  start-page: 312
  year: 1986
  ident: 10.1016/0042-6822(91)90135-X_BIB34
  article-title: Sequences of the major antibody binding epitopes of the Indiana serotype of vesicular stomatitis virus
  publication-title: Virology
  doi: 10.1016/0042-6822(86)90328-4
  contributor:
    fullname: Vandepol
– volume: 71
  start-page: 1313
  year: 1990
  ident: 10.1016/0042-6822(91)90135-X_BIB9
  article-title: Four major antigenic sites of the coronavirus transmissible gastroenteritis virus are located on the amino-terminal half of spike glycoprotein S
  publication-title: J. Gen. Virol.
  doi: 10.1099/0022-1317-71-6-1313
  contributor:
    fullname: Delmas
– volume: 16
  start-page: 247
  year: 1990
  ident: 10.1016/0042-6822(91)90135-X_BIB19
  article-title: Expression of swine transmissible gastroenteritis virus envelope antigens on the surface of infected cells: Epitopes externally exposed
  publication-title: Virus Res.
  doi: 10.1016/0168-1702(90)90051-C
  contributor:
    fullname: Laviada
– volume: 70
  start-page: 3281
  year: 1989
  ident: 10.1016/0042-6822(91)90135-X_BIB10
  article-title: Selection of antigenic variants of foot-and-mouth disease virus in the absence of antibodies, as revealed by an in situ assay
  publication-title: J. Gen. Virol.
  doi: 10.1099/0022-1317-70-12-3281
  contributor:
    fullname: Díez
– volume: 10
  start-page: 77
  year: 1988
  ident: 10.1016/0042-6822(91)90135-X_BIB5
  article-title: Antigenic structure of the E2 glycoprotein from transmissible gastroenteritis coronavirus
  publication-title: Virus Res.
  doi: 10.1016/0168-1702(88)90059-7
  contributor:
    fullname: Correa
– volume: 69
  start-page: 2939
  year: 1988
  ident: 10.1016/0042-6822(91)90135-X_BIB28
  article-title: Coronaviruses: Structure and genome expression
  publication-title: J. Gen. Virol.
  doi: 10.1099/0022-1317-69-12-2939
  contributor:
    fullname: Spaan
– volume: 8
  start-page: 363
  year: 1987
  ident: 10.1016/0042-6822(91)90135-X_BIB17
  article-title: The nucleotide sequence of the peplomer gene of porcine transmissible gastroenteritis virus (TGEV): Comparison with the sequence of the peplomer protein of feline infectious peritonitis virus (FIPV)
  publication-title: Virus Res.
  doi: 10.1016/0168-1702(87)90008-6
  contributor:
    fullname: Jacobs
– volume: 75
  start-page: 4257
  year: 1978
  ident: 10.1016/0042-6822(91)90135-X_BIB37
  article-title: 3′-Terminal nucleotide sequence of encephalomyocarditis virus RNA determined by reverse transcriptase and chain-terminating inhibitors
  contributor:
    fullname: Zimmern
– volume: 232
  start-page: 639
  year: 1986
  ident: 10.1016/0042-6822(91)90135-X_BIB11
  article-title: A mutation in the R body-coding sequence destroys expression of the killer trait in P. Tetraurelia
  publication-title: Science
  doi: 10.1126/science.3008333
  contributor:
    fullname: DiMarchi
– volume: 67
  start-page: 1405
  year: 1986
  ident: 10.1016/0042-6822(91)90135-X_BIB8
  article-title: Antigenic structure of transmissible gastroenteritis virus. II. Domains in the peplomer glycoprotein
  publication-title: J. Gen. Virol.
  doi: 10.1099/0022-1317-67-7-1405
  contributor:
    fullname: Delmas
– volume: 171
  start-page: 493
  year: 1989
  ident: 10.1016/0042-6822(91)90135-X_BIB7
  article-title: Stably expressed FIPV peplomer protein induces cell fusion and elicits neutralizing antibodies in mice
  publication-title: Virology
  doi: 10.1016/0042-6822(89)90619-3
  contributor:
    fullname: De Groot
– volume: 3
  start-page: 179
  year: 1978
  ident: 10.1016/0042-6822(91)90135-X_BIB13
  article-title: Antigenicity of structural components from porcine transmissible gastroenteritis virus
  publication-title: Vet. Microbiol.
  doi: 10.1016/0378-1135(79)90034-8
  contributor:
    fullname: Garwes
– start-page: 359
  year: 1990
  ident: 10.1016/0042-6822(91)90135-X_BIB29
  article-title: Coronaviruses
  contributor:
    fullname: Spaan
– volume: 119
  start-page: 358
  year: 1982
  ident: 10.1016/0042-6822(91)90135-X_BIB3
  article-title: Monoclonal antibodies to murine hepatitis virus-4 (strain JHM) define the viral glycoprotein responsible for attachment and cell-cell fusion
  publication-title: Virology
  doi: 10.1016/0042-6822(82)90095-2
  contributor:
    fullname: Collins
– volume: 263
  start-page: 10,541
  year: 1988
  ident: 10.1016/0042-6822(91)90135-X_BIB6
  article-title: Antibody-antigen complexes
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(18)38002-5
  contributor:
    fullname: Davies
– volume: 71
  start-page: 271
  year: 1990
  ident: 10.1016/0042-6822(91)90135-X_BIB4
  article-title: Localization of antigenic sites of the E2 glycoprotein of transmissible gastroenteritis coronavirus
  publication-title: J. Gen. Virol.
  doi: 10.1099/0022-1317-71-2-271
  contributor:
    fullname: Correa
– volume: 64
  start-page: 1283
  year: 1990
  ident: 10.1016/0042-6822(91)90135-X_BIB36
  article-title: Molecular basis for linkage of a continuous and discontinuous neutralization epitope on the structural polypeptlde VP2 of poliovirus type 1
  publication-title: J. Virol.
  doi: 10.1128/jvi.64.3.1283-1289.1990
  contributor:
    fullname: Wiegers
– volume: 56
  start-page: 904
  year: 1985
  ident: 10.1016/0042-6822(91)90135-X_BIB30
  article-title: Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: Activation of cell-fusing activity of virions by trypsin and separation of two different 90K cleavage fragments
  publication-title: J. Virol.
  doi: 10.1128/jvi.56.3.904-911.1985
  contributor:
    fullname: Sturman
– volume: 70
  start-page: 1493
  year: 1989
  ident: 10.1016/0042-6822(91)90135-X_BIB23
  article-title: Neutralizing epitopes of type 0 foot-and-mouth virus. II. Mapping three conformational sites with synthetic peptide reagents
  publication-title: J. Gen. Virol.
  doi: 10.1099/0022-1317-70-6-1493
  contributor:
    fullname: Parry
– volume: 68
  start-page: 1883
  year: 1987
  ident: 10.1016/0042-6822(91)90135-X_BIB25
  article-title: The predicted primary structure of the peplomer protein E2 of the porcine coronavirus transmissible gastroenteritis virus
  publication-title: J. Gen. Virol.
  doi: 10.1099/0022-1317-68-7-1883
  contributor:
    fullname: Rasschaert
– volume: 62
  start-page: 1870
  year: 1988
  ident: 10.1016/0042-6822(91)90135-X_BIB33
  article-title: Cross-reactive and serotype-specific neutralization epitopes on VP7 of human rotavirus: Nucleotide sequence analysis of antigenic mutants selected with monoclonal antibodies
  publication-title: J. Virol.
  doi: 10.1128/jvi.62.6.1870-1874.1988
  contributor:
    fullname: Taniguchi
– volume: 74
  start-page: 5463
  year: 1977
  ident: 10.1016/0042-6822(91)90135-X_BIB27
  article-title: DNA sequencing with chain-terminating inhibitors
  contributor:
    fullname: Sanger
– year: 1991
  ident: 10.1016/0042-6822(91)90135-X_BIB20
  article-title: Selection of mimotopes from a random sequence expression library using monoclonal antibodies against transmissible gastroenteritis coronavirus
  publication-title: J. Immunol.
  contributor:
    fullname: Lenstra
– volume: 276
  start-page: 301
  year: 1990
  ident: 10.1016/0042-6822(91)90135-X_BIB35
  article-title: Nucleotide sequence of the E2-peplomer protein gene and partial nucleotide sequence of the upstream polymerase gene of transmissible gastroenteritis virus (Miller strain)
  publication-title: Adv. Exp. Med. Biol.
  doi: 10.1007/978-1-4684-5823-7_41
  contributor:
    fullname: Wesley
– volume: 30
  start-page: 190
  year: 1966
  ident: 10.1016/0042-6822(91)90135-X_BIB21
  article-title: Studies on transmissible gastroenteritis of swine. II. Selected characteristics of a cytopathogenic virus common to five isolates from transmissible gastroenteritis
  publication-title: Can. J. Comp. Vet. Sci.
  contributor:
    fullname: McClurkin
– year: 1991
  ident: 10.1016/0042-6822(91)90135-X_BIB12
  article-title: Molecular basis of transmissible gastroenteritis coronavirus (TGEV) epidemiology
  contributor:
    fullname: Enjuanes
– volume: 81
  start-page: 3998
  year: 1984
  ident: 10.1016/0042-6822(91)90135-X_BIB14
  article-title: Use of peptide synthesis to probe viral antigens for epitopes to a resolution of a single amino acid
  contributor:
    fullname: Geysen
– volume: 18
  start-page: 71
  year: 1990
  ident: 10.1016/0042-6822(91)90135-X_BIB2
  article-title: Sequence of the S-gene from a virulent British field isolate of transmissible gastroenteritis virus
  publication-title: Virus Res.
  doi: 10.1016/0168-1702(90)90090-X
  contributor:
    fullname: Britton
– volume: 177
  start-page: 559
  year: 1990
  ident: 10.1016/0042-6822(91)90135-X_BIB31
  article-title: Mechanisms of transmissible gastroenteritis coronavirus neutralization
  publication-title: Virology
  doi: 10.1016/0042-6822(90)90521-R
  contributor:
    fullname: Suñé
– volume: 6
  start-page: 289
  year: 1972
  ident: 10.1016/0042-6822(91)90135-X_BIB1
  article-title: Antibody responses in serum, colostrum and milk of swine after infection or vaccination with transmissible gastroenteritis virus
  publication-title: Infect. Immun.
  doi: 10.1128/iai.6.3.289-301.1972
  contributor:
    fullname: Bohl
– volume: 60
  start-page: 131
  year: 1986
  ident: 10.1016/0042-6822(91)90135-X_BIB18
  article-title: Critical epitopes in transmissible gastroenteritis virus neutralization
  publication-title: J. Virol.
  doi: 10.1128/jvi.60.1.131-139.1986
  contributor:
    fullname: Jiménez
– volume: 53
  start-page: 128
  year: 1985
  ident: 10.1016/0042-6822(91)90135-X_BIB22
  article-title: Epitopes of herpes simplex virus type 1 glycoprotein gC are clustered in two distinct antigenic sites
  publication-title: J. Virol.
  doi: 10.1128/jvi.53.1.128-136.1985
  contributor:
    fullname: Marlin
– volume: 174
  start-page: 410
  year: 1990
  ident: 10.1016/0042-6822(91)90135-X_BIB26
  article-title: Antigenic homology among coronaviruses related to transmissible gastroenteritis virus
  publication-title: Virology
  doi: 10.1016/0042-6822(90)90094-8
  contributor:
    fullname: Sánchez
– volume: 64
  start-page: 3304
  year: 1990
  ident: 10.1016/0042-6822(91)90135-X_BIB24
  article-title: Analysis and simulation of a neutralizing epitope of transmissible gastroenteritis virus
  publication-title: J. Virol.
  doi: 10.1128/jvi.64.7.3304-3309.1990
  contributor:
    fullname: Posthumus
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Snippet The S glycoprotein of transmissible gastroenteritis virus (TGEV) has been shown to contain four major antigenic sites (A, B, C, and D). Site A is the main...
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SubjectTerms ACIDE AMINE
Amino Acid Sequence
AMINOACIDOS
Animals
Antibodies, Monoclonal - immunology
ANTICORPS MONOCLONAL
ANTICUERPOS MONOCLONALES
ANTIGENE
ANTIGENOS
Antigens, Viral - analysis
Base Sequence
Biological and medical sciences
Cells, Cultured
DNA, Viral - chemistry
Epitopes - analysis
Fundamental and applied biological sciences. Psychology
GLICOPROTEINAS
GLYCOPROTEINE
Glycosylation
Microbiology
Molecular Sequence Data
Morphology, structure, chemical composition, physicochemical properties
MUTANT
MUTANTES
Mutation
NUCLEOTIDE
NUCLEOTIDOS
REACCION ANTIGENO-ANTICUERPO
REACTION ANTIGENE ANTICORPS
RNA, Viral - chemistry
Software
Swine
Transmissible gastroenteritis virus - immunology
Viral Proteins - genetics
Viral Proteins - immunology
Virology
VIRUS GASTROENTERITE DU PORC
VIRUS GASTROENTERITIS TRANSMISIBLE
Title Residues involved in the antigenic sites of transmissible gastroenteritis coronavirus S glycoprotein
URI https://dx.doi.org/10.1016/0042-6822(91)90135-X
https://www.ncbi.nlm.nih.gov/pubmed/1711257
https://search.proquest.com/docview/80628711
https://pubmed.ncbi.nlm.nih.gov/PMC7130809
Volume 183
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