The Peptide Methionine Sulfoxide Reductase (MsrAB) of Repairs Oxidatively Damaged Outer Membrane and Periplasmic Proteins Involved in Nutrient Acquisition and Virulence.

Sulfoxide-damage repair mechanisms are emerging as essential for the virulence of bacterial pathogens, and in the human respiratory pathogen the periplasmic MsrAB peptide methionine sulfoxide reductase is necessary for resistance to reactive chlorine species such as hypochlorite. Additionally, this enzyme has a role in modulating the host immune response to infection. Here, we have analysed the enzymatic properties of MsrAB, which revealed that both domains of the protein are catalytically active, with the turnover number of the MsrA domain being 50% greater than that for the MsrB domain.

Draft Genome Sequences of Three Nontypeable Strains of , C188, R535, and 1200, Isolated from Different Types of Disease.

Nontypeable is a persistent human respiratory pathogen known to be involved in a range of acute and chronic respiratory diseases. Here, we report the genome sequences of three strains isolated from sputum, otitis media, and blood. Comparative analyses revealed significant differences in the gene contents including the presence of genes mediating antibiotic resistance.