1887

Abstract

This paper reports the complete coding sequence for a proliprotein signal peptidase (SP-ase) of , Lsp. This is believed to be the first SP-ase described for . SP-ase II is involved in the removal of the signal peptide from glyceride-modified prolipoproteins. By using transcription/translation systems, it was shown that the gene was transcribed . Functionality of Lsp in was demonstrated by using an globomycin resistance assay, to show that expression of Lsp in increased the globomycin resistance. An isogenic mutant of serotype 2 unable to produce Lsp was constructed and shown to process lipoproteins incorrectly, including an 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 is not attenuated .

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2003-06-01
2020-08-10
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