Cysteine protease SpeB expression in group A streptococci is influenced by the nutritional environment but SpeB does not contribute to obtaining essential nutrients.
Group A streptococcal (GAS) cysteine protease is a major virulence factor involved in the pathogenesis of purulent and invasive infections. The secreted enzyme cleaves a number of different bacterial and host proteins which could contribute to different stages of the infective processes. It has been proposed that, among these functions, SpeB plays a role in obtaining nutrients during late growth phases. In the present study, speB mutants of various GAS serotypes were found to exhibit unaltered growth characteristics in several complex and chemically defined media (CDM). When amino acid-depleted CDM was prepared, neither SpeB activity on whole proteins added to the medium during incubation nor the addition of SpeB-digested proteins was able to support bacterial growth. SpeB also was unable to liberate iron from iron-containing protein sources added to iron-deficient CDM. However, SpeB levels in culture supernatants changed in response to the protein and glucose content of the media. Using a speB promoter-luciferase reporter, speB expression levels were found to correspond to peptide concentrations in the culture media. The effect appeared to be specific for peptides since addition of peptides derived from various proteins had an affect on expression, while addition of the whole proteins had no effect. Addition of glucose to CDM had no effect on speB expression, while glucose addition to complex medium decreased speB expression. Overall, SpeB did not appear to be directly involved in providing the bacteria with nutritional factors but expression of the speB gene responded to ratios of peptides and carbohydrates in the culture medium.
Podbielski
A
A
Institute of Medical Microbiology and Hygiene, Department of Microbiology and Immunology, Ulm, Germany. andreas.podbielski@medizin.uni-ulm.de
Woischnik
M
M
Kreikemeyer
B
B
Bettenbrock
K
K
Buttaro
B A
BA
D000596:Amino Acids / Q000494:pharmacology; D001426:Bacterial Proteins / Q000096:biosynthesis* / Q000235:genetics / Q000502:physiology; D003470:Culture Media / Q000494:pharmacology*; D003546:Cysteine Endopeptidases / Q000096:biosynthesis* / Q000235:genetics / Q000502:physiology; D004790:Enzyme Induction; D004792:Enzyme Precursors / Q000378:metabolism; D015964:Gene Expression Regulation, Bacterial / Q000187:drug effects*; D017930:Genes, Reporter; D005947:Glucose / Q000494:pharmacology; D007501:Iron / Q000378:metabolism / Q000494:pharmacology; D010455:Peptides / Q000494:pharmacology; D011506:Proteins / Q000494:pharmacology; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis; D012703:Serotyping; D013297:Streptococcus pyogenes / Q000145:classification / Q000201:enzymology* / Q000235:genetics / Q000472:pathogenicity; D014774:Virulence
D000596:Amino Acids; D001426:Bacterial Proteins; D003470:Culture Media; D004792:Enzyme Precursors; D010455:Peptides; D011506:Proteins; D011993:Recombinant Fusion Proteins; D007501:Iron; D003546:Cysteine Endopeptidases; C042477:streptopain; D005947:Glucose