Deletion of a novel L-cystine/L-cysteine-binding lipoprotein compromises in vivo fitness and pathogenesis of Streptococcus pneumoniae

This dataset contains experimental data generated while characterizing a previously uncharacterized and highly conserved amino acid-binding lipoprotein from Streptococcus pneumoniae. The gene encoding the protein was cloned, expressed in Escherichia coli, and purified for biochemical analyses. Ligand-binding experiments were performed using tryptophan fluorescence spectroscopy with standard amino acids. To investigate the biological role of the protein, an isogenic gene deletion mutant and its genetically complemented strain were generated. In vitro experiments included growth kinetics, cell adhesion and macrophage uptake assays. Additional datasets were generated using mouse infection models to examine the contribution of the lipoprotein in pneumococcal virulence and pathogenesis. Active mouse protection experiments were performed to assess its vaccine potential. Our dataset includes raw and associated experimental readouts obtained from biochemical, microbiological, cellular and animal studies.