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

• Published in: Applied microbiology and biotechnology Vol. 104; no. 11; pp. 5065 - 5080
• Main Authors: de Alcântara, Nayra Rodrigues, de Oliveira, Fábio Muniz, Garcia, Wanius, dos Santos, Otavio Augusto Leitão, Junqueira-Kipnis, Ana Paula, Kipnis, André
• Format: Journal Article
• Language: English
• Published: Berlin/Heidelberg Springer Berlin Heidelberg 01.06.2020; Springer; Springer Nature B.V
• Subjects: Annotations; Antimicrobial agents; Applied Microbial and Cell Physiology; Bacterial Outer Membrane Proteins - genetics; Bacterial Proteins - genetics; Bacterial Proteins - isolation & purification; Bacterial Proteins - metabolism; Binding; Binding proteins; Biomedical and Life Sciences; Biotechnology; Codification; Deoxyribonucleic acid; DNA; DNA-binding protein; DNA-Binding Proteins - genetics; DNA-Binding Proteins - isolation & purification; DNA-Binding Proteins - metabolism; DNA-ligand interactions; Dps protein; Drug resistance in microorganisms; E coli; Escherichia coli; Escherichia coli - drug effects; Escherichia coli - genetics; Escherichia coli Proteins - genetics; Ferroxidase; Gene expression; Genome, Bacterial; Genomes; Genomics; Health aspects; Homeostasis; Hydrogen peroxide; Hydrogen Peroxide - pharmacology; Hydroxyl radicals; Infection; Iron; Life Sciences; Microbial Genetics and Genomics; Microbiology; Microorganisms; Mycobacterium abscessus; Mycobacterium abscessus - drug effects; Mycobacterium abscessus - genetics; Mycobacterium abscessus - metabolism; Oligomers; Oxidative stress; Protein binding; Proteins; Public health; Sequence Analysis, DNA; Soft tissues; Storage proteins; Stress, Physiological; Tuberculosis; Resistance; Fenton reaction; Iron; Dps; Ferritin; Mycobacterium abscessus
• ISSN: 0175-7598; 1432-0614
• DOI: 10.1007/s00253-020-10586-z

Mycobacterium abscessus subsp. massiliense ( Mycma ) belongs to the Mycobacterium abscessu s 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 (H 2 O 2 ). Additionally, the expression of rMaDps by E. coli conferred greater resistance to H 2 O 2 . Thus, this study is the first to identify and characterize a Dps from M. abscessu s. Key Points Mycobacterium abscessus subsp. massiliense express a miniferritin protein (Dps). Mycma Dps binds to DNA and protects against oxidative stress.