Plasmodium vivax metacaspase 1 (PvMCA1) catalytic domain is conserved in field isolates from Brazilian Amazon

• Published in: Memórias do Instituto Oswaldo Cruz Vol. 116; p. e200584
• Main Authors: 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, Melo, Gisely Cardoso de, Lacerda, Marcus Vinícius Guimarães de, 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
• Format: Journal Article
• Language: English; Portuguese
• Published: Instituto Oswaldo Cruz, Ministério da Saúde 01.01.2021; Fundação Oswaldo Cruz (FIOCRUZ)
• Subjects: genetic diversity; metacaspase; P. vivax; PARASITOLOGY; Short Communication; TROPICAL MEDICINE; P. vivax; genetic diversity; metacaspase
• ISSN: 0074-0276; 1678-8060; 1678-8060
• DOI: 10.1590/0074-02760200584

In the present study, we investigated the genetic diversity of Plasmodium vivax metacaspase 1 ( Pv MCA1) 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 Pv MCA1 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 Pv MCA1 may contribute to its eligibility as a druggable target candidate in vivax malaria.