F2F Poster 21st Lancefield International Symposium for Streptococci and Streptococcal Diseases 2022

Identification and characterization of the putative tryptophan substrate-binding protein TrpA in Streptococcus suis (#131)

Muriel Dresen 1 , Désirée Vötsch 1 , Jesús Arenas 2 , Astrid de Greeff 3 , Andreas Nerlich 1 4 , Peter Valentin-Weigand 1
  1. Institute for Microbiology, University of Veterinary Medicine Hannover Foundation, Hanover, Germany
  2. Unit of Microbiology and Immunology, Faculty of Veterinary, University of Zaragoza, Zaragoza, Spain
  3. Wageningen Bioveterinary Research, part of Wageningen University and Research, Lelystad, The Netherlands
  4. Veterinary Centre for Resistance Research (TZR), Department of Veterinary Medicine, Freie Universität Berlin, Berlin, Germany

Streptococcus suis is a common part of the porcine respiratory microbiota. However, S. suis can also become pathogenic and cause life-threatening diseases in pigs as well as humans. A previous study identified the trpA gene (locus SSU1307) to be conditionally essential for in vivo survival by intrathecal infection of pigs with a transposon library of S. suis strain 10. In this work, we investigated the function of trpA encoding a putative tryptophan/tyrosine transport system substrate-binding protein. Therefore, we compared the growth capacities of the isogenic trpA-deficient mutant derivative (10∆trpA) with its parent strain.

Growth experiments in chemically defined media (CDM) revealed that growth of 10∆trpA depended on tryptophan concentration, suggesting that the mutant lacked the capability of high-affinity tryptophan binding and uptake. Complementation as well as the addition of a tryptophan-tripeptide to CDM with low tryptophan concentrations restored this growth defect.

Analyzing the operon structure of this transport system we demonstrated that trpA is co-transcribed with a putative permease and ATPase gene, respectively. Bioinformatics analysis identified a putative tryptophan T-box riboswitch in the 5’ untranslated region in front of this operon. Finally, qRT‑PCR and a reporter assay revealed trpA mRNA induction as well as reporter activation during growth under tryptophan-limited conditions.

In conclusion, our study showed that TrpA, probably functioning as a substrate-binding protein, is part of a putative tryptophan ABC transporter system regulated by a T-box riboswitch. Due to the tryptophan auxotrophy of S. suis, TrpA plays a crucial role for metabolic adaptation and growth of S. suis during infection.