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Published online ahead of print on 21 April 2009 as doi:10.1099/mic.0.025213-0
Microbiology 2009;155:1451.

Microbiology (2009), DOI 10.1099/mic.0.025213-0
© 2009 Society for General Microbiology
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Microbiology 0 (2009), mic.0.025213; DOI  10.1099/mic.0.025213-0
© 2009 Society for General Microbiology

Impact of lgt mutation on lipoprotein biosynthesis and in vitro phenotypes of Streptococcus agalactiae

B. A. Bray1, I. C. Sutcliffe2 and D. J. Harrington3,4

1 University of Bradford, UK;
2 Northumbria University, UK;
3 University of Bradford

ABSTRACT

Although Streptococcus agalactiae, the Group B Streptococcus, is a leading cause of invasive neonatal disease worldwide the molecular basis of its virulence is still poorly understood. To investigate the role of lipoproteins in the physiology and interaction of this pathogen with host cells, we generated a mutant S. agalactiae strain (A909{Delta}Lgt) deficient in the Lgt enzyme and thus unable to lipidate lipoprotein precursors (pro-lipoproteins). The loss of pro-lipoprotein lipidation did not affect the viability of S. agalactiae nor its growth in several different growth media including cation-depleted media. The processing of two well characterized lipoproteins, but not a non-lipoprotein, was clearly shown to be aberrant in A909{Delta}Lgt. The mutant strain was shown to be more sensitive to oxidative stress in vitro although the molecular basis of this increased sensitivity was not apparent. The inactivation of Lgt did result in changes to the bacterial cell envelope, demonstrated by reduced retention of both the Group B carbohydrate and the polysaccharide capsule and a statistically significant reduction (p = 0.0079) in A909{Delta}Lgt adherence to human endothelial cells of foetal origin. These data confirm that failure to correctly process lipoproteins has pleiotropic effects that may be of significance to S. agalactiae colonization and pathogenesis.

4 E-mail: d.harrington{at}bradford.ac.uk






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