Revisiting the role of cholesterol in regulating the pore-formation mechanism of <i>Vibrio cholerae</i> cytolysin, a membrane-damaging β-barrel pore-forming toxin

Kathuria, Reema; Mondal, Anish Kumar; Sharma, Rohan; Bhattacharyya, Samarjit; Chattopadhyay, Kausik

doi:10.1042/bcj20180387

Cited by 16 publications

(12 citation statements)

References 21 publications

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“…Moreover, the role of β‐prism lectin domain was proposed in enabling VCC assembly through production of entropy during the rearrangement process of the PFT (Ganguly et al., 2014). It was demonstrated that during absence of the nonlipid‐dependent interactions, cholesterol promoted VCC binding with the membrane lipid bilayer (Kathuria et al., 2018). Furthermore, biological assays of outer membrane vesicles (OMVs) from the V. cholerae strain V:5/04 established that OMV‐associated VCC induced toxicity in mammalian cells, thereby leading to autophagy (Elluri et al., 2014).…”

Section: Pft Mechanism In Foodborne Pathogensmentioning

confidence: 99%

Pore‐forming toxins of foodborne pathogens

Banerji

Karkee

Kanojiya

et al. 2021

Comp Rev Food Sci Food Safe

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Pore‐forming toxins (PFTs) are water‐soluble molecules that have been identified as the most crucial virulence factors during bacterial pathogenesis. PFTs disrupt the host cell membrane to internalize or to deliver other bacterial or virulence factors for establishing infections. Disruption of the host cell membrane by PFTs can lead to uncontrollable exchanges between the extracellular and the intracellular matrix, thereby disturbing the cellular homeostasis. Recent studies have provided insights into the molecular mechanism of PFTs during pathogenesis. Evidence also suggests the activation of several signal transduction pathways in the host cell on recognition of PFTs. Additionally, numerous distinctive host defense mechanisms as well as membrane repair mechanisms have been reported; however, studies reveal that PFTs aid in host immune evasion of the bacteria through numerous pathways. PFTs have been primarily associated with foodborne pathogens. Infection and death from diseases by consuming contaminated food are a constant threat to public health worldwide, affecting socioeconomic development. Moreover, the emergence of new foodborne pathogens has led to the rise of bacterial antimicrobial resistance affecting the population. Hence, this review focuses on the role of PFTs secreted by foodborne pathogens. The review highlights the molecular mechanism of foodborne bacterial PFTs, assisting bacterial survival from the host immune responses and understanding the downstream mechanism in the activation of various signaling pathways in the host upon PFT recognition. PFT research is a remarkable and an important field for exploring novel and broad applications of antimicrobial compounds as therapeutics.

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Section: Pft Mechanism In Foodborne Pathogensmentioning

confidence: 99%

Pore‐forming toxins of foodborne pathogens

Banerji

Karkee

Kanojiya

et al. 2021

Comp Rev Food Sci Food Safe

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“…PFPs present different mechanisms to target their objective. The most common ones are the interaction of a specific lipid, like cholesterol (Chol) [53,[60][61][62][63][64][65][66][67][68][69][70][71][72][73] or sphingomyelin (SM) [12,25,26,44,69,[74][75][76][77][78][79][80][81][82][83][84][85][86][87][88][89][90][91], or recognition of a specific membrane protein receptor [32,[92][93][94][95][96]. It is common to find collections of highly prey-specific toxins as part of multigene families resulting in an extended range of different targets [97].…”

Section: Pore-forming Proteinsmentioning

confidence: 99%

Functional and Structural Variation among Sticholysins, Pore-Forming Proteins from the Sea Anemone Stichodactyla helianthus

Rivera-de-Torre

Palacios-Ortega

Slotte

et al. 2020

IJMS

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Venoms constitute complex mixtures of many different molecules arising from evolution in processes driven by continuous prey–predator interactions. One of the most common compounds in these venomous cocktails are pore-forming proteins, a family of toxins whose activity relies on the disruption of the plasmatic membranes by forming pores. The venom of sea anemones, belonging to the oldest lineage of venomous animals, contains a large amount of a characteristic group of pore-forming proteins known as actinoporins. They bind specifically to sphingomyelin-containing membranes and suffer a conformational metamorphosis that drives them to make pores. This event usually leads cells to death by osmotic shock. Sticholysins are the actinoporins produced by Stichodactyla helianthus. Three different isotoxins are known: Sticholysins I, II, and III. They share very similar amino acid sequence and three-dimensional structure but display different behavior in terms of lytic activity and ability to interact with cholesterol, an important lipid component of vertebrate membranes. In addition, sticholysins can act in synergy when exerting their toxin action. The subtle, but important, molecular nuances that explain their different behavior are described and discussed throughout the text. Improving our knowledge about sticholysins behavior is important for eventually developing them into biotechnological tools.

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“…The mature active form of VCC is a monomeric ∼65 kDa protein. Upon interacting with the target eukaryotic cell membranes, or cholesterol-containing membrane lipid bilayer, it assembles into heptameric transmembrane β-barrel pores ( De and Olson, 2011 ; Kathuria et al, 2018 ). Specific binding of VCC with membrane phospholipids and cholesterol regulates the efficacy of its membrane-binding step ( Rai and Chattopadhyay, 2015 ; Kathuria et al, 2018 ).…”

Section: Introductionmentioning

confidence: 99%

“…Upon interacting with the target eukaryotic cell membranes, or cholesterol-containing membrane lipid bilayer, it assembles into heptameric transmembrane β-barrel pores ( De and Olson, 2011 ; Kathuria et al, 2018 ). Specific binding of VCC with membrane phospholipids and cholesterol regulates the efficacy of its membrane-binding step ( Rai and Chattopadhyay, 2015 ; Kathuria et al, 2018 ). In addition, VCC employs a specific lectin-like activity to recognize and bind to the cell-surface glycans present in the biomembranes ( Rai et al, 2013 ).…”

Section: Introductionmentioning

confidence: 99%

Curcumin Inhibits Membrane-Damaging Pore-Forming Function of the β-Barrel Pore-Forming Toxin Vibrio cholerae Cytolysin

et al. 2022

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Vibrio cholerae cytolysin (VCC) is a β-barrel pore-forming toxin (β-PFT). Upon encountering the target cells, VCC forms heptameric β-barrel pores and permeabilizes the cell membranes. Structure-function mechanisms of VCC have been extensively studied in the past. However, the existence of any natural inhibitor for VCC has not been reported yet. In the present study, we show that curcumin can compromise the membrane-damaging activity of VCC. Curcumin is known to modulate a wide variety of biological processes and functions. However, the application of curcumin in the physiological scenario often gets limited due to its extremely poor solubility in the aqueous environment. Interestingly, we find that VCC can associate with the insoluble fraction of curcumin in the aqueous medium and thus gets separated from the solution phase. This, in turn, reduces the availability of VCC to attack the target membranes and thus blocks the membrane-damaging action of the toxin. We also observe that the soluble aqueous extract of curcumin, generated by the heat treatment, compromises the pore-forming activity of VCC. Interestingly, in the presence of such soluble extract of curcumin, VCC binds to the target membranes and forms the oligomeric assembly. However, such oligomers appear to be non-functional, devoid of the pore-forming activity. The ability of curcumin to bind to VCC and neutralize its membrane-damaging activity suggests that curcumin has the potential to act as an inhibitor of this potent bacterial β-PFT.

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Revisiting the role of cholesterol in regulating the pore-formation mechanism of Vibrio cholerae cytolysin, a membrane-damaging β-barrel pore-forming toxin

Cited by 16 publications

References 21 publications

Pore‐forming toxins of foodborne pathogens

Pore‐forming toxins of foodborne pathogens

Functional and Structural Variation among Sticholysins, Pore-Forming Proteins from the Sea Anemone Stichodactyla helianthus

Curcumin Inhibits Membrane-Damaging Pore-Forming Function of the β-Barrel Pore-Forming Toxin Vibrio cholerae Cytolysin

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