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

Bray, Beverley, Sutcliffe, Iain and Harrington, Dean (2009) Impact of Lgt mutation on lipoprotein biosynthesis and in vitro phenotypes of Streptococcus agalactiae. Microbiology, 155 (5). pp. 1451-1458. ISSN 1350-0872

Full text not available from this repository. (Request a copy)

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 or its growth in several different 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 also resulted in changes to the bacterial cell envelope, as 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 fetal origin. These data confirm that failure to process lipoproteins correctly has pleiotropic effects that may be of significance to S. agalactiae colonization and pathogenesis

Item Type:	Article
Uncontrolled Keywords:	Gram positive bacteria, Streptococcus agalactiae, Listeria monocytogenes
Subjects:	F100 Chemistry
Department:	Faculties > Health and Life Sciences > Applied Sciences
Depositing User:	EPrint Services
Date Deposited:	26 Feb 2010 15:14
Last Modified:	31 Jul 2021 08:39
URI:	http://nrl.northumbria.ac.uk/id/eprint/406

Downloads