LytA, major autolysin of Streptococcus pneumoniae, requires access to nascent peptidoglycan.

The Journal of Biological Chemistry
Peter MellrothBirgitta Henriques-Normark

Abstract

The pneumococcal autolysin LytA is a virulence factor involved in autolysis as well as in fratricidal- and penicillin-induced lysis. In this study, we used biochemical and molecular biological approaches to elucidate which factors control the cytoplasmic translocation and lytic activation of LytA. We show that LytA is mainly localized intracellularly, as only a small fraction was found attached to the extracellular cell wall. By manipulating the extracellular concentration of LytA, we found that the cells were protected from lysis during exponential growth, but not in the stationary phase, and that a defined threshold concentration of extracellular LytA dictates the onset of autolysis. Stalling growth through nutrient depletion, or the specific arrest of cell wall synthesis, sensitized cells for LytA-mediated lysis. Inhibition of cell wall association via the choline binding domain of an exogenously added enzymatically inactive form of LytA revealed a potential substrate for the amidase domain within the cell wall where the formation of nascent peptidoglycan occurs.

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Citations

Nov 15, 2012·The Journal of Biological Chemistry·Diogo V da SilvaRobert Daniels
Feb 20, 2014·Proceedings of the National Academy of Sciences of the United States of America·Murat BalabanBirgitta Henriques-Normark
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Methods Mentioned

BETA
PCR
Bioscreen
dot blot

Software Mentioned

Image lab

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