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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Mycobacterium tuberculosis CysA2 is a dual sulfurtransferase with activity against thiosulfate and 3-mercaptopyruvate and interacts with mammalian cells

Full text
Author(s):
Meza, A. N. [1, 2] ; Cambui, C. C. N. [1] ; Moreno, A. C. R. [3] ; Fessel, M. R. [1] ; Balan, A. [1]
Total Authors: 5
Affiliation:
[1] Univ Sao Paulo, LBEA, Inst Biomed Sci, Dept Microbiol, Appl Struct Biol Lab, Sao Paulo, SP - Brazil
[2] Univ Estadual Campinas, UNICAMP, Postgrad Program Genet & Mol Biol, Inst Biol, Campinas, SP - Brazil
[3] Univ Sao Paulo, Biomed Sci Inst, Dept Microbiol, Vaccine Dev Lab, Sao Paulo, SP - Brazil
Total Affiliations: 3
Document type: Journal article
Source: SCIENTIFIC REPORTS; v. 9, NOV 14 2019.
Web of Science Citations: 0
Abstract

Cyanide is a toxic compound that is converted to the non-toxic thiocyanate by a rhodanese enzyme. Rhodaneses belong to the family of transferases (sulfurtransferases), which are largely studied. The sulfur donor defines the subfamily of these enzymes as thiosulfate:cyanide sulfurtransferases or rhodaneses (TSTs) or 3-mercaptopyruvate sulfurtransfeases (MSTs). In Mycobacterium tuberculosis, the causative agent of tuberculosis, the gene Rv0815c encodes the protein CysA2, a putative uncharacterized thiosulfate:cyanide sulfurtransferase that belongs to the essential sulfur assimilation pathway in the bacillus and is secreted during infection. In this work, we characterized the functional and structural properties of CysA2 and its kinetic parameters. The recombinant CysA2 is a alpha/beta protein with two rhodanese-like domains that maintains the functional motifs and a catalytic cysteine. Sulfurtransferase activity was determined using thiosulfate and 3-mercaptopyruvate as sulfur donors. The assays showed K-m values of 2.89 mM and 7.02 mM for thiosulfate and 3-mercaptopyruvate, respectively, indicating the protein has dual activity as TST and MST. Immunological assays revealed that CysA2 interacted with pulmonary cells, and it was capable to activate macrophages and dendritic cells, indicating the stimulation of the immune response, which is important for its use as an antigen for vaccine development and immunodiagnostic. (AU)

FAPESP's process: 14/20921-6 - Identification and development of new molecules against Mycobacterium tuberculosis based inhibition of protein metabolism of sulfur -Based methodology using fragments
Grantee:Andreia Navarro Cerone
Support type: Scholarships in Brazil - Doctorate
FAPESP's process: 15/14514-1 - Functional and structural studies of ABC transporters from Mycobacterium tuberculosis and Xanthomonas citri
Grantee:Andrea Balan Fernandes
Support type: Regular Research Grants
FAPESP's process: 16/03196-1 - Expression, purification and kinetics and immunogenic characterization of CysA2, a putative rhodanese-like protein involved in the sulfur metabolism from Mycobacterium Tuberculosis
Grantee:Caio Cesar Nogueira Cambui
Support type: Scholarships in Brazil - Scientific Initiation
FAPESP's process: 18/20162-9 - Investigating the Pathogenesis and Drug Resistance in Microorganisms - Characterization and Control of ATP-Binding Cassette Transporters
Grantee:Andrea Balan Fernandes
Support type: Regular Research Grants