Author | Schwarz, Marcos Gustavo Araujo | |
Author | Luzes, Bianca Gallart Cinelli | |
Author | Correa, Paloma Rezende | |
Author | Gonçalves, Antônio José da Silva | |
Author | Machado, Lucas de Almeida | |
Author | Guimarães, Ana Carolina Ramos | |
Author | Lima, Leila Mendonça | |
Access date | 2021-04-12T18:46:49Z | |
Available date | 2021-04-12T18:46:49Z | |
Document date | 2021 | |
Citation | SCHWARZ, Marcos Gustavo Araujo et al. Mycobacterium tuberculosis and M. bovis BCG Moreau Fumarate Reductase Operons Produce Different Polypeptides That May Be Related to Non-canonical Functions. Front. Microbiol., v. 11, Article 624121, 15p, Jan. 2021. | pt_BR |
ISSN | 2235-2988 | pt_BR |
URI | https://www.arca.fiocruz.br/handle/icict/46653 | |
Language | eng | pt_BR |
Publisher | Frontiers Media | pt_BR |
Rights | open access | |
Subject in Portuguese | Perda do Terminal N | pt_BR |
Subject in Portuguese | M. bovis BCG Moreau | pt_BR |
Subject in Portuguese | Dodecina menos estável | pt_BR |
Subject in Portuguese | Ligação de flavina inferior | pt_BR |
Title | M. bovis BCG Moreau N-Terminal Loss Leads to a Less Stable Dodecin With Lower Flavin Binding Capacity | pt_BR |
Type | Article | |
DOI | 10.3389/fcimb.2021.658888 | |
Abstract | Tuberculosis still remains a concerning health problem worldwide. Its etiologic agent, Mycobacterium tuberculosis, continues to be the focus of research to unravel new prophylactic and therapeutic strategies against this disease. The only vaccine in use against tuberculosis is based on the in vitro attenuated strain, M. bovis BCG. Dodecin is a dodecameric complex important for flavin homeostasis in Archea and Eubacteria, and the M. tuberculosis protein is described as thermo- and halostable. M. bovis BCG Moreau, the Brazilian vaccine strain, has a single nucleotide polymorphism in the dodecin start codon, leading to a predicted loss of seven amino acids at the protein N-terminal end. In this work we aimed to characterize the effect of this mutation in the BCG Moreau protein features. Our recombinant protein assays show that the predicted BCG homolog is less thermostable than M.tb’s but maintains its dodecamerization ability, although with a lower riboflavin-binding capacity. These data are corroborated by structural analysis after comparative modeling, showing that the predicted BCG dodecin complex has a lower interaction energy among its monomers and also a distinct electrostatic surface near the flavin binding pocket. However, western blotting assays with the native proteins were unable to detect significant differences between the BCG Moreau and M.tb orthologs, indicating that other factors may be modulating protein structure/function in the bacterial context. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Genômica Funcional e Bioinformática. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Genômica Funcional e Bioinformática. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Genômica Funcional e Bioinformática. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório Interdisciplinar de Pesquisas Médicas. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Genômica Funcional e Bioinformática. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Genômica Funcional e Bioinformática. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Genômica Funcional e Bioinformática. Rio de Janeiro, RJ, Brasil. | pt_BR |
Subject | M. bovis BCG Moreau | pt_BR |
Subject | N-Terminal Loss | pt_BR |
Subject | Dodecin | pt_BR |
Subject | Lower Flavin | pt_BR |
Subject | Binding Capacity | pt_BR |