Microbial Musings – Winter 2022

and assessing peptides found in cell- free supernatant using mass spectrometry. They find a 16 amino peptide that shares similarity with other Mitis group streptococci, although there is significant sequence diversity amongst the different species. This CSP is released from early to mid- log phase as judged by the activation of expression of the comX gene that is switched on by the quorum- sensing pathway being activated. They show that synthetic CSP from their strain- induced competence, but this was not observed using a distinct CSP from a related strain, demonstrating high specificity of this sensing mechanism. To see which other genes are switched on they isolated RNA from matched cultures with added synthetic CSP or a DMSO control and used RNAseq to determine the differentially expressed genes. They find many of the genes they would have predicted to be involved in competence development, as expected, but also other genes involved in biofilm production and virulence. However, they directly assess biofilm formation in response to different concentrations of CSP and see no direct impact on this phenotype, suggesting there is additional regulatory control of biofilm formation, and they propose the differential regulation of some of the genes involved in this pathway by CSP might have become relevant during growth in the natural polymicrobial oral cavity.

[1]  Ashraf Zarkan,et al.  Bacterial survivors: evaluating the mechanisms of antibiotic persistence. , 2022, Microbiology.

[2]  P. Andrew,et al.  Streptococcus pneumoniae: ‘captain of the men of death’ and financial burden , 2022, Microbiology.

[3]  G. H. Thomas,et al.  Peptide transport in Bacillus subtilis - structure and specificity in the extracellular solute binding proteins OppA and DppE. , 2022, Microbiology.

[4]  D. Padfield,et al.  A comprehensive list of bacterial pathogens infecting humans. , 2022, Microbiology.

[5]  A. Edwards,et al.  Human serum induces daptomycin tolerance in Enterococcus faecalis and viridans group streptococci , 2022, bioRxiv.

[6]  Zhenyu Cheng,et al.  The identification of Pseudomonas aeruginosa persisters using flow cytometry. , 2022, Microbiology.

[7]  P. Miura,et al.  Investigating the Streptococcus sinensis competence regulon through a combination of transcriptome analysis and phenotypic evaluation. , 2022, Microbiology.

[8]  R. Sawers,et al.  FocA and its central role in fine-tuning pH homeostasis of enterobacterial formate metabolism. , 2022, Microbiology.

[9]  Yftah Tal‐Gan,et al.  Modulating streptococcal phenotypes using signal peptide analogues , 2022, Open Biology.

[10]  R. Sawers,et al.  The FocA channel functions to maintain intracellular formate homeostasis during Escherichia coli fermentation. , 2022, Microbiology.

[11]  A. Edwards,et al.  Polymyxin and lipopeptide antibiotics: membrane-targeting drugs of last resort , 2022, Microbiology.

[12]  R. Sawers,et al.  A single amino acid exchange converts FocA into a unidirectional efflux channel for formate , 2022, Microbiology.

[13]  A. Edwards,et al.  Human serum triggers antibiotic tolerance in Staphylococcus aureus , 2021, Nature Communications.

[14]  G. Thomas Griffith, Frederick (1877–1941), microbiologist , 2018, Oxford Dictionary of National Biography.

[15]  G. Thomas,et al.  MpaA is a murein-tripeptide-specific zinc carboxypeptidase that functions as part of a catabolic pathway for peptidoglycan-derived peptides in γ-proteobacteria. , 2012, The Biochemical journal.

[16]  K. Yuen,et al.  Streptococcus pyogenes and re-emergence of scarlet fever as a public health problem , 2012, Emerging Microbes & Infections.

[17]  Richard S. P. Horler,et al.  Compensating Stereochemical Changes Allow Murein Tripeptide to Be Accommodated in a Conventional Peptide-binding Protein* , 2011, The Journal of Biological Chemistry.

[18]  E J Dodson,et al.  Peptide binding in OppA, the crystal structures of the periplasmic oligopeptide binding protein in the unliganded form and in complex with lysyllysine. , 1997, Biochemistry.

[19]  C. Higgins,et al.  The crystal structures of the oligopeptide-binding protein OppA complexed with tripeptide and tetrapeptide ligands. , 1995, Structure.

[20]  R. D. de Groot Structure, function and evolution of the hemagglutinin-esterase proteins of corona- and toroviruses , 2006, Glycoconjugate Journal.