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1 Department of Medical Microbiology, University of Amsterdam, 1100 DD Amsterdam, The Netherlands
2 Division of Infectious Diseases and Food Chain Quality, Cluster of Endemic Diseases, Institute of Animal Science and Health, 8200 AB Lelystad, The Netherlands
3 Laboratory for Vaccine Research, RIVM, National Institute of Public Health and the Environment, 3720 BA Bilthoven, The Netherlands
4 Institute of Pharmacy, Chemistry and Biomedical Sciences, University of Sunderland, UK
Correspondence
Astrid de Greeff
a.degreeff{at}id.wag-ur.nl
This paper reports the complete coding sequence for a proliprotein signal peptidase (SP-ase) of Streptococcus suis, Lsp. This is believed to be the first SP-ase described for S. suis. SP-ase II is involved in the removal of the signal peptide from glyceride-modified prolipoproteins. By using in vitro transcription/translation systems, it was shown that the lsp gene was transcribed in vitro. Functionality of Lsp in Escherichia coli was demonstrated by using an in vitro globomycin resistance assay, to show that expression of Lsp in E. coli increased the globomycin resistance. An isogenic mutant of S. suis serotype 2 unable to produce Lsp was constructed and shown to process lipoproteins incorrectly, including an S. suis homologue of the pneumococcal PsaA lipoprotein. Five piglets were inoculated with a mixture of both strains in an experimental infection, to determine the virulence of the mutant strain relative to that of the wild-type strain in a competitive challenge experiment. The data showed that both strains were equally virulent, indicating that the knockout mutant of lsp is not attenuated in vivo.
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