Lipoprotein signal peptidase of Streptococcus suis serotype 2

Astrid de Greeff*, Andrea Hamilton, Iain C. Sutcliffe, Herma Buys, Loek van Alphen, Hilde E. Smith

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

27 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)1399-1407
Number of pages9
Issue number6
Publication statusPublished - 1 Jun 2003
Externally publishedYes


Dive into the research topics of 'Lipoprotein signal peptidase of Streptococcus suis serotype 2'. Together they form a unique fingerprint.

Cite this