Prediction of Structure and Molecular Interaction with DNA of BvrR, a Virulence-Associated Regulatory Protein of Brucella

• Published in: Molecules (Basel, Switzerland) Vol. 24; no. 17; p. 3137
• Main Authors: Ramírez-González, Edgar A, Moreno-Lafont, Martha C, Méndez-Tenorio, Alfonso, Cancino-Díaz, Mario E, Estrada-García, Iris, López-Santiago, Rubén
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI 29.08.2019; MDPI AG
• Subjects: Amino Acid Motifs; Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; Binding Sites; Brucella - chemistry; Brucella - pathogenicity; BvrR; DNA - chemistry; DNA - metabolism; Gibbs sampling; MD simulation; Molecular Docking Simulation; Molecular Dynamics Simulation; Nucleotide Motifs; Protein Binding; Protein Conformation, alpha-Helical; Protein Conformation, beta-Strand; Protein Interaction Domains and Motifs; protein structure prediction; protein-DNA docking; Structural Homology, Protein; Thermodynamics; Virulence Factors - chemistry; Virulence Factors - metabolism; MD simulation; protein-DNA docking; BvrR; Gibbs sampling; protein structure prediction
• ISSN: 1420-3049; 1420-3049
• DOI: 10.3390/molecules24173137

Brucellosis, also known as "undulant fever" is a zoonotic disease caused by , which is a facultative intracellular bacterium. Despite efforts to eradicate this disease, infection in uncontrolled domestic animals persists in several countries and therefore transmission to humans is common. evasion of the innate immune system depends on its ability to evade the mechanisms of intracellular death in phagocytic cells. The BvrR-BvrS two-component system allows the bacterium to detect adverse conditions in the environment. The BvrS protein has been associated with genes of virulence factors, metabolism, and membrane transport. In this study, we predicted the DNA sequence recognized by BvrR with Gibbs Recursive Sampling and identified the three-dimensional structure of BvrR using I-TASSER suite, and the interaction mechanism between BvrR and DNA with Protein-DNA docking and molecular dynamics (MD) simulation. Based on the Gibbs recursive Sampling analysis, we found the motif AAHTGC (H represents A, C, and T nucleotides) as a possible sequence recognized by BvrR. The docking and EMD simulation results showed that C-terminal effector domain of BvrR protein is likely to interact with AAHTGC sequence. In conclusion, we predicted the structure, recognition motif, and interaction of BvrR with DNA.