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Plasmodium vivax metacaspase 1 (PvMCA1) catalytic domain is conserved in field isolates from Brazilian Amazon
In the present study, we investigated the genetic diversity of Plasmodium vivax metacaspase 1 (PvMCA1) catalytic domain in two municipalities of the main malaria hotspot in Brazil, i.e., the Juruá Valley, and observed complete sequence identity among all P. vivax field isolates and the Sal-1 referen...
Autores principales: | , , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Instituto Oswaldo Cruz, Ministério da Saúde
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8186469/ https://www.ncbi.nlm.nih.gov/pubmed/34076074 http://dx.doi.org/10.1590/0074-02760200584 |
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author | de Souza, Hugo Amorim dos Santos Escafa, Victor Fernandes Blanco, Carolina Moreira Baptista, Bárbara de Oliveira de Barros, Jenifer Peixoto Riccio, Evelyn Ketty Pratt Rodrigues, Aline Beatriz Mello de Melo, Gisely Cardoso de Lacerda, Marcus Vinícius Guimarães de Souza, Rodrigo Medeiros Lima-Junior, Josué da Costa Guimarães, Ana Carolina Ramos da Mota, Fabio Faria da Silva, João Hermínio Martins Daniel-Ribeiro, Cláudio Tadeu Pratt-Riccio, Lilian Rose Totino, Paulo Renato Rivas |
author_facet | de Souza, Hugo Amorim dos Santos Escafa, Victor Fernandes Blanco, Carolina Moreira Baptista, Bárbara de Oliveira de Barros, Jenifer Peixoto Riccio, Evelyn Ketty Pratt Rodrigues, Aline Beatriz Mello de Melo, Gisely Cardoso de Lacerda, Marcus Vinícius Guimarães de Souza, Rodrigo Medeiros Lima-Junior, Josué da Costa Guimarães, Ana Carolina Ramos da Mota, Fabio Faria da Silva, João Hermínio Martins Daniel-Ribeiro, Cláudio Tadeu Pratt-Riccio, Lilian Rose Totino, Paulo Renato Rivas |
author_sort | de Souza, Hugo Amorim dos Santos |
collection | PubMed |
description | In the present study, we investigated the genetic diversity of Plasmodium vivax metacaspase 1 (PvMCA1) catalytic domain in two municipalities of the main malaria hotspot in Brazil, i.e., the Juruá Valley, and observed complete sequence identity among all P. vivax field isolates and the Sal-1 reference strain. Analysis of PvMCA1 catalytic domain in different P. vivax genomic sequences publicly available also revealed a high degree of conservation worldwide, with very few amino acid substitutions that were not related to putative histidine and cysteine catalytic residues, whose involvement with the active site of protease was herein predicted by molecular modeling. The genetic conservation presented by PvMCA1 may contribute to its eligibility as a druggable target candidate in vivax malaria. |
format | Online Article Text |
id | pubmed-8186469 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Instituto Oswaldo Cruz, Ministério da Saúde |
record_format | MEDLINE/PubMed |
spelling | pubmed-81864692021-06-17 Plasmodium vivax metacaspase 1 (PvMCA1) catalytic domain is conserved in field isolates from Brazilian Amazon de Souza, Hugo Amorim dos Santos Escafa, Victor Fernandes Blanco, Carolina Moreira Baptista, Bárbara de Oliveira de Barros, Jenifer Peixoto Riccio, Evelyn Ketty Pratt Rodrigues, Aline Beatriz Mello de Melo, Gisely Cardoso de Lacerda, Marcus Vinícius Guimarães de Souza, Rodrigo Medeiros Lima-Junior, Josué da Costa Guimarães, Ana Carolina Ramos da Mota, Fabio Faria da Silva, João Hermínio Martins Daniel-Ribeiro, Cláudio Tadeu Pratt-Riccio, Lilian Rose Totino, Paulo Renato Rivas Mem Inst Oswaldo Cruz Short Communication In the present study, we investigated the genetic diversity of Plasmodium vivax metacaspase 1 (PvMCA1) catalytic domain in two municipalities of the main malaria hotspot in Brazil, i.e., the Juruá Valley, and observed complete sequence identity among all P. vivax field isolates and the Sal-1 reference strain. Analysis of PvMCA1 catalytic domain in different P. vivax genomic sequences publicly available also revealed a high degree of conservation worldwide, with very few amino acid substitutions that were not related to putative histidine and cysteine catalytic residues, whose involvement with the active site of protease was herein predicted by molecular modeling. The genetic conservation presented by PvMCA1 may contribute to its eligibility as a druggable target candidate in vivax malaria. Instituto Oswaldo Cruz, Ministério da Saúde 2021-05-31 /pmc/articles/PMC8186469/ /pubmed/34076074 http://dx.doi.org/10.1590/0074-02760200584 Text en https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License |
spellingShingle | Short Communication de Souza, Hugo Amorim dos Santos Escafa, Victor Fernandes Blanco, Carolina Moreira Baptista, Bárbara de Oliveira de Barros, Jenifer Peixoto Riccio, Evelyn Ketty Pratt Rodrigues, Aline Beatriz Mello de Melo, Gisely Cardoso de Lacerda, Marcus Vinícius Guimarães de Souza, Rodrigo Medeiros Lima-Junior, Josué da Costa Guimarães, Ana Carolina Ramos da Mota, Fabio Faria da Silva, João Hermínio Martins Daniel-Ribeiro, Cláudio Tadeu Pratt-Riccio, Lilian Rose Totino, Paulo Renato Rivas Plasmodium vivax metacaspase 1 (PvMCA1) catalytic domain is conserved in field isolates from Brazilian Amazon |
title |
Plasmodium vivax metacaspase 1 (PvMCA1) catalytic domain is conserved in field isolates from Brazilian Amazon |
title_full |
Plasmodium vivax metacaspase 1 (PvMCA1) catalytic domain is conserved in field isolates from Brazilian Amazon |
title_fullStr |
Plasmodium vivax metacaspase 1 (PvMCA1) catalytic domain is conserved in field isolates from Brazilian Amazon |
title_full_unstemmed |
Plasmodium vivax metacaspase 1 (PvMCA1) catalytic domain is conserved in field isolates from Brazilian Amazon |
title_short |
Plasmodium vivax metacaspase 1 (PvMCA1) catalytic domain is conserved in field isolates from Brazilian Amazon |
title_sort | plasmodium vivax metacaspase 1 (pvmca1) catalytic domain is conserved in field isolates from brazilian amazon |
topic | Short Communication |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8186469/ https://www.ncbi.nlm.nih.gov/pubmed/34076074 http://dx.doi.org/10.1590/0074-02760200584 |
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