Porcine parvovirus VP1/VP2 on a time series epitope mapping: exploring the effects of high hydrostatic pressure on the immune recognition of antigens.
Autor(a) principal: | |
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Data de Publicação: | 2019 |
Outros Autores: | , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) |
Texto Completo: | http://www.alice.cnptia.embrapa.br/alice/handle/doc/1113864 |
Resumo: | Abstract: Porcine parvovirus (PPV) is a DNA virus that causes reproductive failure in gilts and sows, resulting in embryonic and fetal losses worldwide. Epitope mapping of PPV is important for eveloping new vaccines. In this study, we used spot synthesis analysis for epitope mapping of the capsid proteins of PPV (NADL-2 strain) and correlated the findings with predictive data from immunoinformatics. The virus was exposed to three conditions prior to inoculation in pigs: native (untreated), high hydrostatic pressure (350 MPa for 1 h) at room temperature and high hydrostatic pressure (350 MPa for 1 h) at − 18 °C, and was compared with a commercial vaccine produced using inactivated PPV. The screening of serum samples detected 44 positive spots corresponding to 20 antigenic sites. Each type of inoculated antigen elicited a distinct epitope set. In silico prediction located linear and discontinuous epitopes in B cells that coincided with several epitopes detected in spot synthesis of sera from pigs that received different preparations of inoculum. The conditions tested elicited antibodies against the VP1/VP2 antigen that differed in relation to the response time and the profile of structurally available regions that were recognized. |
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Porcine parvovirus VP1/VP2 on a time series epitope mapping: exploring the effects of high hydrostatic pressure on the immune recognition of antigens.Epitope predictionPorcine parvovirusSpot synthesisVirologiaSuinoculturaParvoviroseEpitope mappingUngulate protoparvovirus 1Abstract: Porcine parvovirus (PPV) is a DNA virus that causes reproductive failure in gilts and sows, resulting in embryonic and fetal losses worldwide. Epitope mapping of PPV is important for eveloping new vaccines. In this study, we used spot synthesis analysis for epitope mapping of the capsid proteins of PPV (NADL-2 strain) and correlated the findings with predictive data from immunoinformatics. The virus was exposed to three conditions prior to inoculation in pigs: native (untreated), high hydrostatic pressure (350 MPa for 1 h) at room temperature and high hydrostatic pressure (350 MPa for 1 h) at − 18 °C, and was compared with a commercial vaccine produced using inactivated PPV. The screening of serum samples detected 44 positive spots corresponding to 20 antigenic sites. Each type of inoculated antigen elicited a distinct epitope set. In silico prediction located linear and discontinuous epitopes in B cells that coincided with several epitopes detected in spot synthesis of sera from pigs that received different preparations of inoculum. The conditions tested elicited antibodies against the VP1/VP2 antigen that differed in relation to the response time and the profile of structurally available regions that were recognized.ANCELMO RABELO DE SOUZA, UNICAMP; MARRIAM YAMIN, UNICAMP; DANIELLE GAVA, CNPSA; JANICE REIS CIACCI ZANELLA, CNPSA; MARIA SILVIA VICCARI GATTI, UNICAMP; CARLOS FRANCISCO SAMPAIO BONAFE, UNICAMP; DANIEL FERREIRA DE LIMA NETO, UNICAMP.SOUZA, A. R. deYAMIN, M.GAVA, D.ZANELLA, J. R. C.GATTI, M. S. V.BONAFE, C. S. F.LIMA NETO, D. F. de2019-11-04T18:11:35Z2019-11-04T18:11:35Z2019-11-0420192019-11-04T18:11:35Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleVirology Journal, v. 16, art. 75, 2019.http://www.alice.cnptia.embrapa.br/alice/handle/doc/111386410.1186/s12985-019-1165-1enginfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice)instname:Empresa Brasileira de Pesquisa Agropecuária (Embrapa)instacron:EMBRAPA2019-11-04T18:11:41Zoai:www.alice.cnptia.embrapa.br:doc/1113864Repositório InstitucionalPUBhttps://www.alice.cnptia.embrapa.br/oai/requestcg-riaa@embrapa.bropendoar:21542019-11-04T18:11:41Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) - Empresa Brasileira de Pesquisa Agropecuária (Embrapa)false |
dc.title.none.fl_str_mv |
Porcine parvovirus VP1/VP2 on a time series epitope mapping: exploring the effects of high hydrostatic pressure on the immune recognition of antigens. |
title |
Porcine parvovirus VP1/VP2 on a time series epitope mapping: exploring the effects of high hydrostatic pressure on the immune recognition of antigens. |
spellingShingle |
Porcine parvovirus VP1/VP2 on a time series epitope mapping: exploring the effects of high hydrostatic pressure on the immune recognition of antigens. SOUZA, A. R. de Epitope prediction Porcine parvovirus Spot synthesis Virologia Suinocultura Parvovirose Epitope mapping Ungulate protoparvovirus 1 |
title_short |
Porcine parvovirus VP1/VP2 on a time series epitope mapping: exploring the effects of high hydrostatic pressure on the immune recognition of antigens. |
title_full |
Porcine parvovirus VP1/VP2 on a time series epitope mapping: exploring the effects of high hydrostatic pressure on the immune recognition of antigens. |
title_fullStr |
Porcine parvovirus VP1/VP2 on a time series epitope mapping: exploring the effects of high hydrostatic pressure on the immune recognition of antigens. |
title_full_unstemmed |
Porcine parvovirus VP1/VP2 on a time series epitope mapping: exploring the effects of high hydrostatic pressure on the immune recognition of antigens. |
title_sort |
Porcine parvovirus VP1/VP2 on a time series epitope mapping: exploring the effects of high hydrostatic pressure on the immune recognition of antigens. |
author |
SOUZA, A. R. de |
author_facet |
SOUZA, A. R. de YAMIN, M. GAVA, D. ZANELLA, J. R. C. GATTI, M. S. V. BONAFE, C. S. F. LIMA NETO, D. F. de |
author_role |
author |
author2 |
YAMIN, M. GAVA, D. ZANELLA, J. R. C. GATTI, M. S. V. BONAFE, C. S. F. LIMA NETO, D. F. de |
author2_role |
author author author author author author |
dc.contributor.none.fl_str_mv |
ANCELMO RABELO DE SOUZA, UNICAMP; MARRIAM YAMIN, UNICAMP; DANIELLE GAVA, CNPSA; JANICE REIS CIACCI ZANELLA, CNPSA; MARIA SILVIA VICCARI GATTI, UNICAMP; CARLOS FRANCISCO SAMPAIO BONAFE, UNICAMP; DANIEL FERREIRA DE LIMA NETO, UNICAMP. |
dc.contributor.author.fl_str_mv |
SOUZA, A. R. de YAMIN, M. GAVA, D. ZANELLA, J. R. C. GATTI, M. S. V. BONAFE, C. S. F. LIMA NETO, D. F. de |
dc.subject.por.fl_str_mv |
Epitope prediction Porcine parvovirus Spot synthesis Virologia Suinocultura Parvovirose Epitope mapping Ungulate protoparvovirus 1 |
topic |
Epitope prediction Porcine parvovirus Spot synthesis Virologia Suinocultura Parvovirose Epitope mapping Ungulate protoparvovirus 1 |
description |
Abstract: Porcine parvovirus (PPV) is a DNA virus that causes reproductive failure in gilts and sows, resulting in embryonic and fetal losses worldwide. Epitope mapping of PPV is important for eveloping new vaccines. In this study, we used spot synthesis analysis for epitope mapping of the capsid proteins of PPV (NADL-2 strain) and correlated the findings with predictive data from immunoinformatics. The virus was exposed to three conditions prior to inoculation in pigs: native (untreated), high hydrostatic pressure (350 MPa for 1 h) at room temperature and high hydrostatic pressure (350 MPa for 1 h) at − 18 °C, and was compared with a commercial vaccine produced using inactivated PPV. The screening of serum samples detected 44 positive spots corresponding to 20 antigenic sites. Each type of inoculated antigen elicited a distinct epitope set. In silico prediction located linear and discontinuous epitopes in B cells that coincided with several epitopes detected in spot synthesis of sera from pigs that received different preparations of inoculum. The conditions tested elicited antibodies against the VP1/VP2 antigen that differed in relation to the response time and the profile of structurally available regions that were recognized. |
publishDate |
2019 |
dc.date.none.fl_str_mv |
2019-11-04T18:11:35Z 2019-11-04T18:11:35Z 2019-11-04 2019 2019-11-04T18:11:35Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
Virology Journal, v. 16, art. 75, 2019. http://www.alice.cnptia.embrapa.br/alice/handle/doc/1113864 10.1186/s12985-019-1165-1 |
identifier_str_mv |
Virology Journal, v. 16, art. 75, 2019. 10.1186/s12985-019-1165-1 |
url |
http://www.alice.cnptia.embrapa.br/alice/handle/doc/1113864 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.source.none.fl_str_mv |
reponame:Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) instname:Empresa Brasileira de Pesquisa Agropecuária (Embrapa) instacron:EMBRAPA |
instname_str |
Empresa Brasileira de Pesquisa Agropecuária (Embrapa) |
instacron_str |
EMBRAPA |
institution |
EMBRAPA |
reponame_str |
Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) |
collection |
Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) |
repository.name.fl_str_mv |
Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) - Empresa Brasileira de Pesquisa Agropecuária (Embrapa) |
repository.mail.fl_str_mv |
cg-riaa@embrapa.br |
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1817695570710495232 |