Listeriolysin O: the Swiss army knife of Listeria

Hamon, Mélanie; Ribet, David; Stavru, Fabrizia; Cossart, Pascale

doi:10.1016/j.tim.2012.04.006

Cited by 252 publications

(249 citation statements)

References 101 publications

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“…In this approach, we infected BMMs with the Gram-positive, cytosol-invading pathogen Listeria monocytogenes in the absence or presence of L. pneumophila LPS. This pathogen enters the cytosol by forming pores in phagosomes with the toxin, Listeriolysin O (LLO) (22). We found that the codelivery of L. pneumophila LPS with WT L. monocytogenes increased L. monocytogenes-induced cell death in WT but not Gbp chr3−/− BMMs (Fig.…”

Section: Gbp Chr3 Proteins Promote the Induction Of Caspase-11 Pyroptmentioning

confidence: 92%

Guanylate binding proteins promote caspase-11–dependent pyroptosis in response to cytoplasmic LPS

Pilla

Hagar

Haldar

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

294

364

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Significance A major component of the cell envelope of Gram-negative bacteria is LPS, also known as endotoxin. LPS produced during bacterial infections triggers inflammation, which can lead to septic shock and death. Our immune system can recognize LPS both outside and inside of cells. The recognition of extracellular and vacuolar LPS by LPS binding proteins is well described, but little is known about the recognition of cytoplasmic LPS. Here, we show that cytoplasmic LPS derived from the intracellular bacterial pathogen Legionella activated a proinflammatory immune response. We further identified host guanylate binding proteins as critical mediators of immunity triggered by cytoplasmic LPS. These findings are likely to advance our understanding of how cells can sense intracellular LPS.

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Section: Gbp Chr3 Proteins Promote the Induction Of Caspase-11 Pyroptmentioning

confidence: 92%

Guanylate binding proteins promote caspase-11–dependent pyroptosis in response to cytoplasmic LPS

Pilla

Hagar

Haldar

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

294

364

View full text Add to dashboard Cite

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“…The pore-forming domain is delivered to mitochondria of epithelial cells and induces apoptosis (221). i LLO is the subject of a recent, detailed review (222). j ETA is a fusion of a PFT and a toxin that inhibits protein translation; although there is a fair body of in vivo data, it is unclear which of ETA's effects are caused by its PFT function.…”

Section: Pft Effects and Cellular Defense Mechanismsmentioning

confidence: 99%

Role of Pore-Forming Toxins in Bacterial Infectious Diseases

Los

Randis

Aroian

et al. 2013

Microbiol Mol Biol Rev

344

351

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SUMMARY Pore-forming toxins (PFTs) are the most common bacterial cytotoxic proteins and are required for virulence in a large number of important pathogens, including Streptococcus pneumoniae , group A and B streptococci, Staphylococcus aureus , Escherichia coli , and Mycobacterium tuberculosis . PFTs generally disrupt host cell membranes, but they can have additional effects independent of pore formation. Substantial effort has been devoted to understanding the molecular mechanisms underlying the functions of certain model PFTs. Likewise, specific host pathways mediating survival and immune responses in the face of toxin-mediated cellular damage have been delineated. However, less is known about the overall functions of PFTs during infection in vivo . This review focuses on common themes in the area of PFT biology, with an emphasis on studies addressing the roles of PFTs in in vivo and ex vivo models of colonization or infection. Common functions of PFTs include disruption of epithelial barrier function and evasion of host immune responses, which contribute to bacterial growth and spreading. The widespread nature of PFTs make this group of toxins an attractive target for the development of new virulence-targeted therapies that may have broad activity against human pathogens.

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“…These pathogens are able to cause acute or chronic damage to the host (95,96) or are linked to (postinfectious) complications (97)(98)(99)(100)(101)(102)(103)(104)(105)(106)(107).…”

Section: Cas9 As a Regulator Of Bacterial Virulencementioning

confidence: 99%

The Role of CRISPR-Cas Systems in Virulence of Pathogenic Bacteria

Louwen

Staals

Endtz

et al. 2014

Microbiol Mol Biol Rev

208

178

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SUMMARY Clustered regularly interspaced short palindromic repeats (CRISPR) and CRISPR-associated (Cas) genes are present in many bacterial and archaeal genomes. Since the discovery of the typical CRISPR loci in the 1980s, well before their physiological role was revealed, their variable sequences have been used as a complementary typing tool in diagnostic, epidemiologic, and evolutionary analyses of prokaryotic strains. The discovery that CRISPR spacers are often identical to sequence fragments of mobile genetic elements was a major breakthrough that eventually led to the elucidation of CRISPR-Cas as an adaptive immunity system. Key elements of this unique prokaryotic defense system are small CRISPR RNAs that guide nucleases to complementary target nucleic acids of invading viruses and plasmids, generally followed by the degradation of the invader. In addition, several recent studies have pointed at direct links of CRISPR-Cas to regulation of a range of stress-related phenomena. An interesting example concerns a pathogenic bacterium that possesses a CRISPR-associated ribonucleoprotein complex that may play a dual role in defense and/or virulence. In this review, we describe recently reported cases of potential involvement of CRISPR-Cas systems in bacterial stress responses in general and bacterial virulence in particular.

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Listeriolysin O: the Swiss army knife of Listeria

Cited by 252 publications

References 101 publications

Guanylate binding proteins promote caspase-11–dependent pyroptosis in response to cytoplasmic LPS

Guanylate binding proteins promote caspase-11–dependent pyroptosis in response to cytoplasmic LPS

Role of Pore-Forming Toxins in Bacterial Infectious Diseases

The Role of CRISPR-Cas Systems in Virulence of Pathogenic Bacteria

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