Psp Stress Response Proteins Form a Complex with Mislocalized Secretins in the <italic toggle="yes">Yersinia enterocolitica</italic> Cytoplasmic Membrane

ABSTRACT The bacterial phage shock protein system (Psp) is a conserved extracytoplasmic stress response that is essential for the virulence of some pathogens, including Yersinia enterocolitica. It is induced by events that can compromise inner membrane (IM) integrity, including the mislocalization o...

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Autores principales:	Disha Srivastava, Amal Moumene, Josué Flores-Kim, Andrew J. Darwin
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2017
Materias:	secretin Yersinia protein interactions stress response Microbiology QR1-502
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spelling	oai:doaj.org-article:fcc2a74489374bbf92ed86abdce7d73b2021-11-15T15:51:50ZPsp Stress Response Proteins Form a Complex with Mislocalized Secretins in the <italic toggle="yes">Yersinia enterocolitica</italic> Cytoplasmic Membrane10.1128/mBio.01088-172150-7511https://doaj.org/article/fcc2a74489374bbf92ed86abdce7d73b2017-11-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mBio.01088-17https://doaj.org/toc/2150-7511ABSTRACT The bacterial phage shock protein system (Psp) is a conserved extracytoplasmic stress response that is essential for the virulence of some pathogens, including Yersinia enterocolitica. It is induced by events that can compromise inner membrane (IM) integrity, including the mislocalization of outer membrane pore-forming proteins called secretins. In the absence of the Psp system, secretin mislocalization permeabilizes the IM and causes rapid cell death. The Psp proteins PspB and PspC form an integral IM complex with two independent roles. First, the PspBC complex is required to activate the Psp response in response to some inducing triggers, including a mislocalized secretin. Second, PspBC are sufficient to counteract mislocalized secretin toxicity. Remarkably, secretin mislocalization into the IM induces psp gene expression without significantly affecting the expression of any other genes. Furthermore, psp null strains are killed by mislocalized secretins, whereas no other null mutants have been found to share this specific secretin sensitivity. This suggests an exquisitely specific relationship between secretins and the Psp system, but there has been no mechanism described to explain this. In this study, we addressed this deficiency by using a coimmunoprecipitation approach to show that the Psp proteins form a specific complex with mislocalized secretins in the Y. enterocolitica IM. Importantly, analysis of different secretin mutant proteins also revealed that this interaction is absolutely dependent on a secretin adopting a multimeric state. Therefore, the Psp system has evolved with the ability to detect and detoxify dangerous secretin multimers while ignoring the presence of innocuous monomers. IMPORTANCE The phage shock protein (Psp) response has been linked to important phenotypes in diverse bacteria, including those related to antibiotic resistance, biofilm formation, and virulence. This has generated widespread interest in understanding various aspects of its function. Outer membrane secretin proteins are essential components of export systems required for the virulence of many bacterial pathogens. However, secretins can mislocalize into the inner membrane, and this induces the Psp response in a highly specific manner and kills Psp-defective strains with similar specificity. There has been no mechanism described to explain this exquisitely specific relationship between secretins and the Psp system. Therefore, this study provides a critical advance by discovering that Psp effector proteins form a complex with secretins in the Yersinia enterocolitica inner membrane. Remarkably, this interaction is absolutely dependent on a secretin adopting its multimeric state. Therefore, the Psp system detects and detoxifies dangerous secretin multimers, while ignoring the presence of innocuous secretin monomers.Disha SrivastavaAmal MoumeneJosué Flores-KimAndrew J. DarwinAmerican Society for MicrobiologyarticlesecretinYersiniaprotein interactionsstress responseMicrobiologyQR1-502ENmBio, Vol 8, Iss 5 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	secretin Yersinia protein interactions stress response Microbiology QR1-502
spellingShingle	secretin Yersinia protein interactions stress response Microbiology QR1-502 Disha Srivastava Amal Moumene Josué Flores-Kim Andrew J. Darwin Psp Stress Response Proteins Form a Complex with Mislocalized Secretins in the <italic toggle="yes">Yersinia enterocolitica</italic> Cytoplasmic Membrane
description	ABSTRACT The bacterial phage shock protein system (Psp) is a conserved extracytoplasmic stress response that is essential for the virulence of some pathogens, including Yersinia enterocolitica. It is induced by events that can compromise inner membrane (IM) integrity, including the mislocalization of outer membrane pore-forming proteins called secretins. In the absence of the Psp system, secretin mislocalization permeabilizes the IM and causes rapid cell death. The Psp proteins PspB and PspC form an integral IM complex with two independent roles. First, the PspBC complex is required to activate the Psp response in response to some inducing triggers, including a mislocalized secretin. Second, PspBC are sufficient to counteract mislocalized secretin toxicity. Remarkably, secretin mislocalization into the IM induces psp gene expression without significantly affecting the expression of any other genes. Furthermore, psp null strains are killed by mislocalized secretins, whereas no other null mutants have been found to share this specific secretin sensitivity. This suggests an exquisitely specific relationship between secretins and the Psp system, but there has been no mechanism described to explain this. In this study, we addressed this deficiency by using a coimmunoprecipitation approach to show that the Psp proteins form a specific complex with mislocalized secretins in the Y. enterocolitica IM. Importantly, analysis of different secretin mutant proteins also revealed that this interaction is absolutely dependent on a secretin adopting a multimeric state. Therefore, the Psp system has evolved with the ability to detect and detoxify dangerous secretin multimers while ignoring the presence of innocuous monomers. IMPORTANCE The phage shock protein (Psp) response has been linked to important phenotypes in diverse bacteria, including those related to antibiotic resistance, biofilm formation, and virulence. This has generated widespread interest in understanding various aspects of its function. Outer membrane secretin proteins are essential components of export systems required for the virulence of many bacterial pathogens. However, secretins can mislocalize into the inner membrane, and this induces the Psp response in a highly specific manner and kills Psp-defective strains with similar specificity. There has been no mechanism described to explain this exquisitely specific relationship between secretins and the Psp system. Therefore, this study provides a critical advance by discovering that Psp effector proteins form a complex with secretins in the Yersinia enterocolitica inner membrane. Remarkably, this interaction is absolutely dependent on a secretin adopting its multimeric state. Therefore, the Psp system detects and detoxifies dangerous secretin multimers, while ignoring the presence of innocuous secretin monomers.
format	article
author	Disha Srivastava Amal Moumene Josué Flores-Kim Andrew J. Darwin
author_facet	Disha Srivastava Amal Moumene Josué Flores-Kim Andrew J. Darwin
author_sort	Disha Srivastava
title	Psp Stress Response Proteins Form a Complex with Mislocalized Secretins in the <italic toggle="yes">Yersinia enterocolitica</italic> Cytoplasmic Membrane
title_short	Psp Stress Response Proteins Form a Complex with Mislocalized Secretins in the <italic toggle="yes">Yersinia enterocolitica</italic> Cytoplasmic Membrane
title_full	Psp Stress Response Proteins Form a Complex with Mislocalized Secretins in the <italic toggle="yes">Yersinia enterocolitica</italic> Cytoplasmic Membrane
title_fullStr	Psp Stress Response Proteins Form a Complex with Mislocalized Secretins in the <italic toggle="yes">Yersinia enterocolitica</italic> Cytoplasmic Membrane
title_full_unstemmed	Psp Stress Response Proteins Form a Complex with Mislocalized Secretins in the <italic toggle="yes">Yersinia enterocolitica</italic> Cytoplasmic Membrane
title_sort	psp stress response proteins form a complex with mislocalized secretins in the <italic toggle="yes">yersinia enterocolitica</italic> cytoplasmic membrane
publisher	American Society for Microbiology
publishDate	2017
url	https://doaj.org/article/fcc2a74489374bbf92ed86abdce7d73b
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Psp Stress Response Proteins Form a Complex with Mislocalized Secretins in the <italic toggle="yes">Yersinia enterocolitica</italic> Cytoplasmic Membrane

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