Association of ActA to peptidoglycan revealed by cell wall proteomics of intracellular Listeria monocytogenes.

García-del, F Portillo; D'Orazio, Valentina; Mg, Pucciarelli

doi:10.1074/jbc.a111.230441

Cited by 8 publications

(14 citation statements)

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“…Interestingly, although anchored to the membrane, ActA was shown to be specifically co-purified with the peptidoglycan fraction isolated from intracellular bacteria (García-del Portillo et al, 2011). …”

Section: Regulation Of Cell Surface-associated Mechanismsmentioning

confidence: 99%

How Listeria monocytogenes organizes its surface for virulence

Carvalho

Sousa

Cabanes

2014

Front. Cell. Infect. Microbiol.

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Listeria monocytogenes is a Gram-positive pathogen responsible for the manifestation of human listeriosis, an opportunistic foodborne disease with an associated high mortality rate. The key to the pathogenesis of listeriosis is the capacity of this bacterium to trigger its internalization by non-phagocytic cells and to survive and even replicate within phagocytes. The arsenal of virulence proteins deployed by L. monocytogenes to successfully promote the invasion and infection of host cells has been progressively unveiled over the past decades. A large majority of them is located at the cell envelope, which provides an interface for the establishment of close interactions between these bacterial factors and their host targets. Along the multistep pathways carrying these virulence proteins from the inner side of the cytoplasmic membrane to their cell envelope destination, a multiplicity of auxiliary proteins must act on the immature polypeptides to ensure that they not only maturate into fully functional effectors but also are placed or guided to their correct position in the bacterial surface. As the major scaffold for surface proteins, the cell wall and its metabolism are critical elements in listerial virulence. Conversely, the crucial physical support and protection provided by this structure make it an ideal target for the host immune system. Therefore, mechanisms involving fine modifications of cell envelope components are activated by L. monocytogenes to render it less recognizable by the innate immunity sensors or more resistant to the activity of antimicrobial effectors. This review provides a state-of-the-art compilation of the mechanisms used by L. monocytogenes to organize its surface for virulence, with special focus on those proteins that work “behind the frontline”, either supporting virulence effectors or ensuring the survival of the bacterium within its host.

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Section: Regulation Of Cell Surface-associated Mechanismsmentioning

confidence: 99%

How Listeria monocytogenes organizes its surface for virulence

Carvalho

Sousa

Cabanes

2014

Front. Cell. Infect. Microbiol.

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“…Protein identifications were accepted if they could be established at >95.0% probability and contained at least two identified peptides. For a further description of the experimental details of the procedure, see García-del Portillo et al (2011).…”

Section: Proteomic Analysismentioning

confidence: 99%

An RpoS-dependent sRNA regulates the expression of a chaperone involved in protein folding

Silva

Ortega

Viegas

et al. 2013

RNA

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Small noncoding RNAs (sRNAs) are usually expressed in the cell to face a variety of stresses. In this report we disclose the first target for SraL (also known as RyjA), a sRNA present in many bacteria, which is highly induced in stationary phase. We also demonstrate that this sRNA is directly transcribed by the major stress σ factor σ S (RpoS) in Salmonella enterica serovar Typhimurium. We show that SraL sRNA down-regulates the expression of the chaperone Trigger Factor (TF), encoded by the tig gene. TF is one of the three major chaperones that cooperate in the folding of the newly synthesized cytosolic proteins and is the only ribosome-associated chaperone known in bacteria. By use of bioinformatic tools and mutagenesis experiments, SraL was shown to directly interact with the 5 ′ UTR of the tig mRNA a few nucleotides upstream of the Shine-Dalgarno region. Namely, point mutations in the sRNA (SraL * ) abolished the repression of tig mRNA and could only down-regulate a tig transcript target with the respective compensatory mutations. We have also validated in vitro that SraL forms a stable duplex with the tig mRNA. This work constitutes the first report of a small RNA affecting protein folding. Taking into account that both SraL and TF are very well conserved in enterobacteria, this work will have important repercussions in the field.

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“…Future studies, for instance using cryo‐electron tomography, may elucidate the stressosome structure in vivo and further assess the contribution of membrane anchor proteins and RsbR paralogues in stressosome activation. Earlier MS‐based proteomics studies characterised the Listeria proteome of both extra‐ and intracellular bacteria in detail with a particular focus on the cell wall proteome containing many important virulence factors and proteins that interact with the host (Calvo et al, ; Garcia‐del‐Portillo et al, ; Quereda et al, ). Together, two decades of Listeria omics profiling by the Cossart laboratory and other groups resulted in more than 600 genome, transcriptome and proteome datasets that are integrated and available on listeriomics.pasteur.fr (Bécavin et al, ), an invaluable resource to decipher key regulatory mechanisms of Listeria gene expression by a systems biology approach.…”

Section: Listeria Transition From the Environment To The Mammalian Hostmentioning

confidence: 99%

Three decades of listeriology through the prism of technological advances

Impens

Dussurget

2020

Cellular Microbiology

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Decades of breakthroughs resulting from cross feeding of microbiological research and technological innovation have promoted Listeria monocytogenes to the rank of model microorganism to study host–pathogen interactions. The extraordinary capacity of this bacterium to interfere with a vast array of host cellular processes uncovered new concepts in microbiology, cell biology and infection biology. Here, we review technological advances that revealed how bacteria and host interact in space and time at the molecular, cellular, tissue and whole body scales, ultimately revolutionising our understanding of Listeria pathogenesis. With the current bloom of multidisciplinary integrative approaches, Listeria entered a new microbiology era.

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Association of ActA to peptidoglycan revealed by cell wall proteomics of intracellular Listeria monocytogenes.

Cited by 8 publications

References 0 publications

How Listeria monocytogenes organizes its surface for virulence

How Listeria monocytogenes organizes its surface for virulence

An RpoS-dependent sRNA regulates the expression of a chaperone involved in protein folding

Three decades of listeriology through the prism of technological advances

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