Eintrag weiter verarbeiten
A Single Amino Acid Change within Antigenic Domain II of the Spike Protein of Bovine Coronavirus Confers Resistance to Virus Neutralization
Gespeichert in:
| Zeitschriftentitel: | Clinical Diagnostic Laboratory Immunology |
|---|---|
| Personen und Körperschaften: | , |
| In: | Clinical Diagnostic Laboratory Immunology, 8, 2001, 2, S. 297-302 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Society for Microbiology
|
| Schlagwörter: |
| author_facet |
Yoo, Dongwan Deregt, Dirk Yoo, Dongwan Deregt, Dirk |
|---|---|
| author |
Yoo, Dongwan Deregt, Dirk |
| spellingShingle |
Yoo, Dongwan Deregt, Dirk Clinical Diagnostic Laboratory Immunology A Single Amino Acid Change within Antigenic Domain II of the Spike Protein of Bovine Coronavirus Confers Resistance to Virus Neutralization Microbiology (medical) Clinical Biochemistry Immunology Immunology and Allergy |
| author_sort |
yoo, dongwan |
| spelling |
Yoo, Dongwan Deregt, Dirk 1071-412X 1098-6588 American Society for Microbiology Microbiology (medical) Clinical Biochemistry Immunology Immunology and Allergy http://dx.doi.org/10.1128/cdli.8.2.297-302.2001 <jats:title>ABSTRACT</jats:title><jats:p>The spike glycoprotein is a major neutralizing antigen of bovine coronavirus (BCV). Conformational neutralizing epitopes of group A and group B monoclonal antibodies (MAbs) have previously been mapped to two domains at amino acids 351 to 403 (domain I) and amino acids 517 to 621 (domain II). To further map antigenic sites, neutralization escape mutants of BCV were selected with a group A MAb which has both in vitro and in vivo virus-neutralizing ability. The escape mutants were demonstrated to be neutralization resistant to the selecting group A MAb and remained sensitive to neutralization by a group B MAb. In radioimmunoprecipitation assays, the spike proteins of neutralization escape mutants were shown to have lost their reactivities with the selecting group A MAb. Sequence analysis of the spike protein genes of the escape mutants identified a single nucleotide substitution of C to T at position 1583, resulting in the change of alanine to valine at amino acid position 528 (A528V). The mutation occurs in domain II and in a location which corresponds to the hypervariable region of the spike protein of the coronavirus mouse hepatitis virus. Experimental introduction of the A528V mutation into the wild-type spike protein resulted in the loss of MAb binding of the mutant protein, confirming that the single point mutation was responsible for the escape of BCV from immunological selective pressure.</jats:p> A Single Amino Acid Change within Antigenic Domain II of the Spike Protein of Bovine Coronavirus Confers Resistance to Virus Neutralization Clinical Diagnostic Laboratory Immunology |
| doi_str_mv |
10.1128/cdli.8.2.297-302.2001 |
| facet_avail |
Online Free |
| finc_class_facet |
Biologie Medizin Chemie und Pharmazie |
| format |
ElectronicArticle |
| fullrecord |
blob:ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTEyOC9jZGxpLjguMi4yOTctMzAyLjIwMDE |
| id |
ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTEyOC9jZGxpLjguMi4yOTctMzAyLjIwMDE |
| institution |
DE-15 DE-Pl11 DE-Rs1 DE-105 DE-14 DE-Ch1 DE-L229 DE-D275 DE-Bn3 DE-Brt1 DE-Zwi2 DE-D161 DE-Gla1 DE-Zi4 |
| imprint |
American Society for Microbiology, 2001 |
| imprint_str_mv |
American Society for Microbiology, 2001 |
| issn |
1071-412X 1098-6588 |
| issn_str_mv |
1071-412X 1098-6588 |
| language |
English |
| mega_collection |
American Society for Microbiology (CrossRef) |
| match_str |
yoo2001asingleaminoacidchangewithinantigenicdomainiiofthespikeproteinofbovinecoronavirusconfersresistancetovirusneutralization |
| publishDateSort |
2001 |
| publisher |
American Society for Microbiology |
| recordtype |
ai |
| record_format |
ai |
| series |
Clinical Diagnostic Laboratory Immunology |
| source_id |
49 |
| title |
A Single Amino Acid Change within Antigenic Domain II of the Spike Protein of Bovine Coronavirus Confers Resistance to Virus Neutralization |
| title_unstemmed |
A Single Amino Acid Change within Antigenic Domain II of the Spike Protein of Bovine Coronavirus Confers Resistance to Virus Neutralization |
| title_full |
A Single Amino Acid Change within Antigenic Domain II of the Spike Protein of Bovine Coronavirus Confers Resistance to Virus Neutralization |
| title_fullStr |
A Single Amino Acid Change within Antigenic Domain II of the Spike Protein of Bovine Coronavirus Confers Resistance to Virus Neutralization |
| title_full_unstemmed |
A Single Amino Acid Change within Antigenic Domain II of the Spike Protein of Bovine Coronavirus Confers Resistance to Virus Neutralization |
| title_short |
A Single Amino Acid Change within Antigenic Domain II of the Spike Protein of Bovine Coronavirus Confers Resistance to Virus Neutralization |
| title_sort |
a single amino acid change within antigenic domain ii of the spike protein of bovine coronavirus confers resistance to virus neutralization |
| topic |
Microbiology (medical) Clinical Biochemistry Immunology Immunology and Allergy |
| url |
http://dx.doi.org/10.1128/cdli.8.2.297-302.2001 |
| publishDate |
2001 |
| physical |
297-302 |
| description |
<jats:title>ABSTRACT</jats:title><jats:p>The spike glycoprotein is a major neutralizing antigen of bovine coronavirus (BCV). Conformational neutralizing epitopes of group A and group B monoclonal antibodies (MAbs) have previously been mapped to two domains at amino acids 351 to 403 (domain I) and amino acids 517 to 621 (domain II). To further map antigenic sites, neutralization escape mutants of BCV were selected with a group A MAb which has both in vitro and in vivo virus-neutralizing ability. The escape mutants were demonstrated to be neutralization resistant to the selecting group A MAb and remained sensitive to neutralization by a group B MAb. In radioimmunoprecipitation assays, the spike proteins of neutralization escape mutants were shown to have lost their reactivities with the selecting group A MAb. Sequence analysis of the spike protein genes of the escape mutants identified a single nucleotide substitution of C to T at position 1583, resulting in the change of alanine to valine at amino acid position 528 (A528V). The mutation occurs in domain II and in a location which corresponds to the hypervariable region of the spike protein of the coronavirus mouse hepatitis virus. Experimental introduction of the A528V mutation into the wild-type spike protein resulted in the loss of MAb binding of the mutant protein, confirming that the single point mutation was responsible for the escape of BCV from immunological selective pressure.</jats:p> |
| container_issue |
2 |
| container_start_page |
297 |
| container_title |
Clinical Diagnostic Laboratory Immunology |
| container_volume |
8 |
| format_de105 |
Article, E-Article |
| format_de14 |
Article, E-Article |
| format_de15 |
Article, E-Article |
| format_de520 |
Article, E-Article |
| format_de540 |
Article, E-Article |
| format_dech1 |
Article, E-Article |
| format_ded117 |
Article, E-Article |
| format_degla1 |
E-Article |
| format_del152 |
Buch |
| format_del189 |
Article, E-Article |
| format_dezi4 |
Article |
| format_dezwi2 |
Article, E-Article |
| format_finc |
Article, E-Article |
| format_nrw |
Article, E-Article |
| _version_ |
1792344962830958598 |
| geogr_code |
not assigned |
| last_indexed |
2024-03-01T17:15:39.386Z |
| geogr_code_person |
not assigned |
| openURL |
url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=A+Single+Amino+Acid+Change+within+Antigenic+Domain+II+of+the+Spike+Protein+of+Bovine+Coronavirus+Confers+Resistance+to+Virus+Neutralization&rft.date=2001-03-01&genre=article&issn=1098-6588&volume=8&issue=2&spage=297&epage=302&pages=297-302&jtitle=Clinical+Diagnostic+Laboratory+Immunology&atitle=A+Single+Amino+Acid+Change+within+Antigenic+Domain+II+of+the+Spike+Protein+of+Bovine+Coronavirus+Confers+Resistance+to+Virus+Neutralization&aulast=Deregt&aufirst=Dirk&rft_id=info%3Adoi%2F10.1128%2Fcdli.8.2.297-302.2001&rft.language%5B0%5D=eng |
| SOLR | |
| _version_ | 1792344962830958598 |
| author | Yoo, Dongwan, Deregt, Dirk |
| author_facet | Yoo, Dongwan, Deregt, Dirk, Yoo, Dongwan, Deregt, Dirk |
| author_sort | yoo, dongwan |
| container_issue | 2 |
| container_start_page | 297 |
| container_title | Clinical Diagnostic Laboratory Immunology |
| container_volume | 8 |
| description | <jats:title>ABSTRACT</jats:title><jats:p>The spike glycoprotein is a major neutralizing antigen of bovine coronavirus (BCV). Conformational neutralizing epitopes of group A and group B monoclonal antibodies (MAbs) have previously been mapped to two domains at amino acids 351 to 403 (domain I) and amino acids 517 to 621 (domain II). To further map antigenic sites, neutralization escape mutants of BCV were selected with a group A MAb which has both in vitro and in vivo virus-neutralizing ability. The escape mutants were demonstrated to be neutralization resistant to the selecting group A MAb and remained sensitive to neutralization by a group B MAb. In radioimmunoprecipitation assays, the spike proteins of neutralization escape mutants were shown to have lost their reactivities with the selecting group A MAb. Sequence analysis of the spike protein genes of the escape mutants identified a single nucleotide substitution of C to T at position 1583, resulting in the change of alanine to valine at amino acid position 528 (A528V). The mutation occurs in domain II and in a location which corresponds to the hypervariable region of the spike protein of the coronavirus mouse hepatitis virus. Experimental introduction of the A528V mutation into the wild-type spike protein resulted in the loss of MAb binding of the mutant protein, confirming that the single point mutation was responsible for the escape of BCV from immunological selective pressure.</jats:p> |
| doi_str_mv | 10.1128/cdli.8.2.297-302.2001 |
| facet_avail | Online, Free |
| finc_class_facet | Biologie, Medizin, Chemie und Pharmazie |
| format | ElectronicArticle |
| format_de105 | Article, E-Article |
| format_de14 | Article, E-Article |
| format_de15 | Article, E-Article |
| format_de520 | Article, E-Article |
| format_de540 | Article, E-Article |
| format_dech1 | Article, E-Article |
| format_ded117 | Article, E-Article |
| format_degla1 | E-Article |
| format_del152 | Buch |
| format_del189 | Article, E-Article |
| format_dezi4 | Article |
| format_dezwi2 | Article, E-Article |
| format_finc | Article, E-Article |
| format_nrw | Article, E-Article |
| geogr_code | not assigned |
| geogr_code_person | not assigned |
| id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTEyOC9jZGxpLjguMi4yOTctMzAyLjIwMDE |
| imprint | American Society for Microbiology, 2001 |
| imprint_str_mv | American Society for Microbiology, 2001 |
| institution | DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4 |
| issn | 1071-412X, 1098-6588 |
| issn_str_mv | 1071-412X, 1098-6588 |
| language | English |
| last_indexed | 2024-03-01T17:15:39.386Z |
| match_str | yoo2001asingleaminoacidchangewithinantigenicdomainiiofthespikeproteinofbovinecoronavirusconfersresistancetovirusneutralization |
| mega_collection | American Society for Microbiology (CrossRef) |
| physical | 297-302 |
| publishDate | 2001 |
| publishDateSort | 2001 |
| publisher | American Society for Microbiology |
| record_format | ai |
| recordtype | ai |
| series | Clinical Diagnostic Laboratory Immunology |
| source_id | 49 |
| spelling | Yoo, Dongwan Deregt, Dirk 1071-412X 1098-6588 American Society for Microbiology Microbiology (medical) Clinical Biochemistry Immunology Immunology and Allergy http://dx.doi.org/10.1128/cdli.8.2.297-302.2001 <jats:title>ABSTRACT</jats:title><jats:p>The spike glycoprotein is a major neutralizing antigen of bovine coronavirus (BCV). Conformational neutralizing epitopes of group A and group B monoclonal antibodies (MAbs) have previously been mapped to two domains at amino acids 351 to 403 (domain I) and amino acids 517 to 621 (domain II). To further map antigenic sites, neutralization escape mutants of BCV were selected with a group A MAb which has both in vitro and in vivo virus-neutralizing ability. The escape mutants were demonstrated to be neutralization resistant to the selecting group A MAb and remained sensitive to neutralization by a group B MAb. In radioimmunoprecipitation assays, the spike proteins of neutralization escape mutants were shown to have lost their reactivities with the selecting group A MAb. Sequence analysis of the spike protein genes of the escape mutants identified a single nucleotide substitution of C to T at position 1583, resulting in the change of alanine to valine at amino acid position 528 (A528V). The mutation occurs in domain II and in a location which corresponds to the hypervariable region of the spike protein of the coronavirus mouse hepatitis virus. Experimental introduction of the A528V mutation into the wild-type spike protein resulted in the loss of MAb binding of the mutant protein, confirming that the single point mutation was responsible for the escape of BCV from immunological selective pressure.</jats:p> A Single Amino Acid Change within Antigenic Domain II of the Spike Protein of Bovine Coronavirus Confers Resistance to Virus Neutralization Clinical Diagnostic Laboratory Immunology |
| spellingShingle | Yoo, Dongwan, Deregt, Dirk, Clinical Diagnostic Laboratory Immunology, A Single Amino Acid Change within Antigenic Domain II of the Spike Protein of Bovine Coronavirus Confers Resistance to Virus Neutralization, Microbiology (medical), Clinical Biochemistry, Immunology, Immunology and Allergy |
| title | A Single Amino Acid Change within Antigenic Domain II of the Spike Protein of Bovine Coronavirus Confers Resistance to Virus Neutralization |
| title_full | A Single Amino Acid Change within Antigenic Domain II of the Spike Protein of Bovine Coronavirus Confers Resistance to Virus Neutralization |
| title_fullStr | A Single Amino Acid Change within Antigenic Domain II of the Spike Protein of Bovine Coronavirus Confers Resistance to Virus Neutralization |
| title_full_unstemmed | A Single Amino Acid Change within Antigenic Domain II of the Spike Protein of Bovine Coronavirus Confers Resistance to Virus Neutralization |
| title_short | A Single Amino Acid Change within Antigenic Domain II of the Spike Protein of Bovine Coronavirus Confers Resistance to Virus Neutralization |
| title_sort | a single amino acid change within antigenic domain ii of the spike protein of bovine coronavirus confers resistance to virus neutralization |
| title_unstemmed | A Single Amino Acid Change within Antigenic Domain II of the Spike Protein of Bovine Coronavirus Confers Resistance to Virus Neutralization |
| topic | Microbiology (medical), Clinical Biochemistry, Immunology, Immunology and Allergy |
| url | http://dx.doi.org/10.1128/cdli.8.2.297-302.2001 |