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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.)

Dps protein is related to resistance of Mycobacterium abscessus subsp. massiliense against stressful conditions

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Author(s):
de Alcantara, Nayra Rodrigues [1] ; de Oliveira, Fabio Muniz [1] ; Garcia, Wanius [2] ; Leitao dos Santos, Otavio Augusto [2] ; Junqueira-Kipnis, Ana Paula [1] ; Kipnis, Andre [1]
Total Authors: 6
Affiliation:
[1] Univ Fed Goias, Inst Patol Trop & Saude Publ, Goiania, Go - Brazil
[2] Univ Fed ABC, Ctr Ciencias Nat & Humanas, Santo Andre, SP - Brazil
Total Affiliations: 2
Document type: Journal article
Source: Applied Microbiology and Biotechnology; v. 104, n. 11 APR 2020.
Web of Science Citations: 0
Abstract

Mycobacterium abscessus subsp. massiliense (Mycma) belongs to the Mycobacterium abscessus complex and is a rapidly growing non-tuberculous mycobacterium. The chronic pulmonary, skin, and soft tissue infections that it causes may be difficult to treat due to its intrinsic resistance to the commonly used antimicrobial drugs, making it a serious world public health problem. Iron is an essential nutrient for the growth of microorganisms; nonetheless, it can be toxic when in excess. Thus, bacteria require an iron homeostasis mechanism to succeed in different environments. DNA-binding proteins from starved cells (Dps) are miniferritins with the property to act as additional iron storage proteins but also can bind to DNA, protecting it against hydroxyl radical. Annotation of the Mycma genome revealed the gene mycma\_03135 with 79% sequential identity when compared to MSMEG\_3242 gene from M. smegmatis mc(2) 155, which codifies for a known Dps. Recombinant Dps from M. abscessus (rMaDps) was produced in Escherichia coli, purified in soluble form and shown to form high mass oligomers in solution with ferroxidase activity, DNA binding, and protection against damage. The expression of the mycma\_03135 gene was induced during Mycma growth in the presence of hydrogen peroxide (H2O2). Additionally, the expression of rMaDps by E. coli conferred greater resistance to H2O2. Thus, this study is the first to identify and characterize a Dps from M. abscessus. (AU)

FAPESP's process: 17/17275-3 - Studies of the mode of action of two lytic polysaccharide monooxygenases from insect (order: isoptera): molecular structure, bioinorganic chemistry and biotechnological applications
Grantee:Wanius José Garcia da Silva
Support Opportunities: Regular Research Grants