CD31 (PECAM-1) Serves as the Endothelial Cell-Specific Receptor of Clostridium perfringens β-Toxin

Bruggisser, Julia; Tarek, Basma; Wyder, Marianne; Müller, Philipp; Ballmoos, Christoph von; Witz, Guillaume; Enzmann, Gaby; Deutsch, Urban; Engelhardt, Britta; Posthaus, Horst

doi:10.1016/j.chom.2020.05.003

Cited by 36 publications

(41 citation statements)

References 64 publications

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“…Top right, single color channel for CellTracker-orange labeled cells. Bottom left, single channel for CD31-AF647 labeled blood vessels ( Bruggisser et al., 2020 ). Bottom right, all 3 channels combined.…”

Section: Step-by-step Methods Detailsmentioning

confidence: 99%

An optimized confocal intravital microscopy protocol for long-term live imaging of murine F-actin organization during naïve lymphocyte migration

Yan

Kehrl

2021

STAR Protocols

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Summary Actin plays a crucial role during cell motility, but the organization of F-actin filaments during lymphocyte migration has not been visualized in vivo . Here, we present a 4D imaging platform using high-resolution confocal intravital microscopy to precisely determine the F-actin filament profile during lymphocyte transendothelial migration and interstitial migration. This protocol allows prolonged live imaging by laser scanning microscopy with advanced spatial resolution compared with the traditional multi-photon intravital microscopy techniques. For complete details on the use and execution of this protocol, please refer to Yan et al. (2019) .

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Section: Step-by-step Methods Detailsmentioning

confidence: 99%

An optimized confocal intravital microscopy protocol for long-term live imaging of murine F-actin organization during naïve lymphocyte migration

Yan

Kehrl

2021

STAR Protocols

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“…PVL targets neutrophils, even monocytes, and macrophages by binding to the C5a receptor (C5aRs) [120]. CD31 or PECAM-1 on endothelial cells is the specific membrane receptor for Clostridium perfringens β-toxin and essential for interaction [121]. In most cases, cholesterol on the target membranes has been shown as the receptor for the CDCs.…”

Section: Diversification Of Interaction Of Pfts With Membrane Componentsmentioning

confidence: 99%

Structural Basis of the Pore-Forming Toxin/Membrane Interaction

Mengist

et al. 2021

Toxins

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With the rapid growth of antibiotic-resistant bacteria, it is urgent to develop alternative therapeutic strategies. Pore-forming toxins (PFTs) belong to the largest family of virulence factors of many pathogenic bacteria and constitute the most characterized classes of pore-forming proteins (PFPs). Recent studies revealed the structural basis of several PFTs, both as soluble monomers, and transmembrane oligomers. Upon interacting with host cells, the soluble monomer of bacterial PFTs assembles into transmembrane oligomeric complexes that insert into membranes and affect target cell-membrane permeability, leading to diverse cellular responses and outcomes. Herein we have reviewed the structural basis of pore formation and interaction of PFTs with the host cell membrane, which could add valuable contributions in comprehensive understanding of PFTs and searching for novel therapeutic strategies targeting PFTs and interaction with host receptors in the fight of bacterial antibiotic-resistance.

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Section: Cytolysin/hemolysinmentioning

confidence: 99%

“…Indeed, HlyA belongs to the β-barrel pore-forming toxin family. This family also includes other bacterial hemolysins such as aerolysin from Aeromonas and the β-toxin of Clostridium [ 60 , 61 , 62 ]. Notably, cytolysin/hemolysin in vibrios is produced as an inactive precursor containing both a signal peptide sequence and a pro-region at the amino-terminus [ 63 ].…”

Section: Major Exotoxins Produced By Pathogenic Vibrio mentioning

confidence: 99%

Spatiotemporal Regulation of Vibrio Exotoxins by HlyU and Other Transcriptional Regulators

Kim

2020

Toxins

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After invading a host, bacterial pathogens secrete diverse protein toxins to disrupt host defense systems. To ensure successful infection, however, pathogens must precisely regulate the expression of those exotoxins because uncontrolled toxin production squanders energy. Furthermore, inappropriate toxin secretion can trigger host immune responses that are detrimental to the invading pathogens. Therefore, bacterial pathogens use diverse transcriptional regulators to accurately regulate multiple exotoxin genes based on spatiotemporal conditions. This review covers three major exotoxins in pathogenic Vibrio species and their transcriptional regulation systems. When Vibrio encounters a host, genes encoding cytolysin/hemolysin, multifunctional-autoprocessing repeats-in-toxin (MARTX) toxin, and secreted phospholipases are coordinately regulated by the transcriptional regulator HlyU. At the same time, however, they are distinctly controlled by a variety of other transcriptional regulators. How this coordinated but distinct regulation of exotoxins makes Vibrio species successful pathogens? In addition, anti-virulence strategies that target the coordinating master regulator HlyU and related future research directions are discussed.

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CD31 (PECAM-1) Serves as the Endothelial Cell-Specific Receptor of Clostridium perfringens β-Toxin

Cited by 36 publications

References 64 publications

An optimized confocal intravital microscopy protocol for long-term live imaging of murine F-actin organization during naïve lymphocyte migration

An optimized confocal intravital microscopy protocol for long-term live imaging of murine F-actin organization during naïve lymphocyte migration

Structural Basis of the Pore-Forming Toxin/Membrane Interaction

Spatiotemporal Regulation of Vibrio Exotoxins by HlyU and Other Transcriptional Regulators

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