New highly antigenic linear B cell epitope peptides from PvAMA-1 as potential vaccine candidates.

Peptide-based vaccines have demonstrated to be an important way to induce long-lived immune responses and, therefore, a promising strategy in the rational of vaccine development. As to malaria, among the classic vaccine targets, the Apical membrane antigen (AMA-1) was proven to have important B cell...

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Autores principales: Raianna F Fantin, Vanessa G Fraga, Camila A Lopes, Isabella C de Azevedo, João L Reis-Cunha, Dhelio B Pereira, Francisco P Lobo, Marcela M de Oliveira, Anderson C Dos Santos, Daniela C Bartholomeu, Ricardo T Fujiwara, Lilian L Bueno
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Publicado: Public Library of Science (PLoS) 2021
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spelling oai:doaj.org-article:5a85fb5fd06b4702bec725159201238e2021-12-02T20:04:33ZNew highly antigenic linear B cell epitope peptides from PvAMA-1 as potential vaccine candidates.1932-620310.1371/journal.pone.0258637https://doaj.org/article/5a85fb5fd06b4702bec725159201238e2021-01-01T00:00:00Zhttps://doi.org/10.1371/journal.pone.0258637https://doaj.org/toc/1932-6203Peptide-based vaccines have demonstrated to be an important way to induce long-lived immune responses and, therefore, a promising strategy in the rational of vaccine development. As to malaria, among the classic vaccine targets, the Apical membrane antigen (AMA-1) was proven to have important B cell epitopes that can induce specific immune response and, hence, became key players for a vaccine approach. The peptides selection was carried out using a bioinformatic approach based on Hidden Markov Models profiles of known antigens and propensity scale methods based on hydrophilicity and secondary structure prediction. The antigenicity of the selected B-cell peptides was assessed by multiple serological assays using sera from acute P.vivax infected subjects. The synthetic peptides were recognized by 45.5%, 48.7% and 32.2% of infected subjects for peptides I, II and III respectively. Moreover, when synthetized together (tripeptide), the reactivity increases up to 62%, which is comparable to the reactivity found against the whole protein PvAMA-1 (57%). Furthermore, IgG reactivity against the tripeptide after depletion was reduced by 42%, indicating that these epitopes may be responsible for a considerable part of the protein immunogenicity. These results represent an excellent perspective regarding future chimeric vaccine constructions that may come to contemplate several targets with the potential to generate the robust and protective immune response that a vivax malaria vaccine needs to succeed.Raianna F FantinVanessa G FragaCamila A LopesIsabella C de AzevedoJoão L Reis-CunhaDhelio B PereiraFrancisco P LoboMarcela M de OliveiraAnderson C Dos SantosDaniela C BartholomeuRicardo T FujiwaraLilian L BuenoPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 16, Iss 11, p e0258637 (2021)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Raianna F Fantin
Vanessa G Fraga
Camila A Lopes
Isabella C de Azevedo
João L Reis-Cunha
Dhelio B Pereira
Francisco P Lobo
Marcela M de Oliveira
Anderson C Dos Santos
Daniela C Bartholomeu
Ricardo T Fujiwara
Lilian L Bueno
New highly antigenic linear B cell epitope peptides from PvAMA-1 as potential vaccine candidates.
description Peptide-based vaccines have demonstrated to be an important way to induce long-lived immune responses and, therefore, a promising strategy in the rational of vaccine development. As to malaria, among the classic vaccine targets, the Apical membrane antigen (AMA-1) was proven to have important B cell epitopes that can induce specific immune response and, hence, became key players for a vaccine approach. The peptides selection was carried out using a bioinformatic approach based on Hidden Markov Models profiles of known antigens and propensity scale methods based on hydrophilicity and secondary structure prediction. The antigenicity of the selected B-cell peptides was assessed by multiple serological assays using sera from acute P.vivax infected subjects. The synthetic peptides were recognized by 45.5%, 48.7% and 32.2% of infected subjects for peptides I, II and III respectively. Moreover, when synthetized together (tripeptide), the reactivity increases up to 62%, which is comparable to the reactivity found against the whole protein PvAMA-1 (57%). Furthermore, IgG reactivity against the tripeptide after depletion was reduced by 42%, indicating that these epitopes may be responsible for a considerable part of the protein immunogenicity. These results represent an excellent perspective regarding future chimeric vaccine constructions that may come to contemplate several targets with the potential to generate the robust and protective immune response that a vivax malaria vaccine needs to succeed.
format article
author Raianna F Fantin
Vanessa G Fraga
Camila A Lopes
Isabella C de Azevedo
João L Reis-Cunha
Dhelio B Pereira
Francisco P Lobo
Marcela M de Oliveira
Anderson C Dos Santos
Daniela C Bartholomeu
Ricardo T Fujiwara
Lilian L Bueno
author_facet Raianna F Fantin
Vanessa G Fraga
Camila A Lopes
Isabella C de Azevedo
João L Reis-Cunha
Dhelio B Pereira
Francisco P Lobo
Marcela M de Oliveira
Anderson C Dos Santos
Daniela C Bartholomeu
Ricardo T Fujiwara
Lilian L Bueno
author_sort Raianna F Fantin
title New highly antigenic linear B cell epitope peptides from PvAMA-1 as potential vaccine candidates.
title_short New highly antigenic linear B cell epitope peptides from PvAMA-1 as potential vaccine candidates.
title_full New highly antigenic linear B cell epitope peptides from PvAMA-1 as potential vaccine candidates.
title_fullStr New highly antigenic linear B cell epitope peptides from PvAMA-1 as potential vaccine candidates.
title_full_unstemmed New highly antigenic linear B cell epitope peptides from PvAMA-1 as potential vaccine candidates.
title_sort new highly antigenic linear b cell epitope peptides from pvama-1 as potential vaccine candidates.
publisher Public Library of Science (PLoS)
publishDate 2021
url https://doaj.org/article/5a85fb5fd06b4702bec725159201238e
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