Structural Basis of the Pore-Forming Toxin/Membrane Interaction

Li, Yajuan; Li, Yuelong; Mengist, Hylemariam Mihiretie; Shi, Cuixiao; Zhang, Caiying; Wang, Bo; Li, Tingting; Huang, Yandong; Xu, Yuanhong; Jin, Tengchuan

doi:10.3390/toxins13020128

Cited by 27 publications

(29 citation statements)

References 142 publications

(136 reference statements)

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“…PFTs can be further divided into different families (Tables 1 and 2), classified according to sequence and structural similarity of the pore and the presence of a conserved mechanism of membrane insertion [3,4]. The stoichiometry and, thus, final lumen size of pores formed by members of different families can vary significantly.…”

Section: Mechanism Of Pore-formationmentioning

confidence: 99%

“…For many PFTs, binding to the target membrane is via surface glycans. These are typically glycans that are conjugated to membrane proteins although, in some instances, PFTs bind to protein glycosyl phosphatidyl inositol (GPI) membrane anchors [3,4].…”

Section: Pft Specificity For Glycan Receptorsmentioning

confidence: 99%

“…It should be noted that while PFTs are also produced by archaea and eukaryotes, this review will focus solely on bacterial toxins; for readers interested in PFTs produced by these other systems they are referred to the following articles [3][4][5].…”

Section: Introductionmentioning

confidence: 99%

“…Biological membranes often provide the first line of defence against external assaults, and are the targets of some of the most potent antibiotics and protein toxins [2]. Pore-forming toxins (PFTs) are key proteinaceous agents that target the plasma membrane, and they form the largest class of bacterial protein toxins [3–5] (Tables 1 and 2). In this review we summarise the variety of PFTs produced by bacteria, describing the mechanism of pore-formation, where known, as well as recent advances in the determination of their mode of action and the cellular responses they elicit in both their eukaryotic and prokaryotic targets.…”

Section: Introductionmentioning

confidence: 99%

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Bacterial pore-forming toxins

Ulhuq

Mariano

2022

Microbiology

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Pore-forming toxins (PFTs) are widely distributed in both Gram-negative and Gram-positive bacteria. PFTs can act as virulence factors that bacteria utilise in dissemination and host colonisation or, alternatively, they can be employed to compete with rival microbes in polymicrobial niches. PFTs transition from a soluble form to become membrane-embedded by undergoing large conformational changes. Once inserted, they perforate the membrane, causing uncontrolled efflux of ions and/or nutrients and dissipating the protonmotive force (PMF). In some instances, target cells intoxicated by PFTs display additional effects as part of the cellular response to pore formation. Significant progress has been made in the mechanistic description of pore formation for the different PFTs families, but in several cases a complete understanding of pore structure remains lacking. PFTs have evolved recognition mechanisms to bind specific receptors that define their host tropism, although this can be remarkably diverse even within the same family. Here we summarise the salient features of PFTs and highlight where additional research is necessary to fully understand the mechanism of pore formation by members of this diverse group of protein toxins.

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Section: Mechanism Of Pore-formationmentioning

confidence: 99%

Section: Pft Specificity For Glycan Receptorsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Bacterial pore-forming toxins

Ulhuq

Mariano

2022

Microbiology

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“…PFPs enable bacteria to fight for resources by killing competing species, while in humans, pore-forming immune effectors combat bacterial infections or trigger cell-cell signalling events by damaging cellular membranes [6,19]. To date, numerous families of PFPs have been identified and reviewed extensively (Figure 1a,c) [12,[20][21][22][23][24][25][26][27][28].…”

Section: Version Of Record Published: 8 November 2021mentioning

confidence: 99%

Challenges and approaches to studying pore-forming proteins

Benton

Bayly-Jones

2021

Biochemical Society Transactions

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Pore-forming proteins (PFPs) are a broad class of molecules that comprise various families, structural folds, and assembly pathways. In nature, PFPs are most often deployed by their host organisms to defend against other organisms. In humans, this is apparent in the immune system, where several immune effectors possess pore-forming activity. Furthermore, applications of PFPs are found in next-generation low-cost DNA sequencing, agricultural crop protection, pest control, and biosensing. The advent of cryoEM has propelled the field forward. Nevertheless, significant challenges and knowledge-gaps remain. Overcoming these challenges is particularly important for the development of custom, purpose-engineered PFPs with novel or desired properties. Emerging single-molecule techniques and methods are helping to address these unanswered questions. Here we review the current challenges, problems, and approaches to studying PFPs.

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Structural insight into Bacillus thuringiensis Sip1Ab reveals its similarity to ETX_MTX2 family beta‐pore‐forming toxin

Chen,

Shi,

Wang

et al. 2023

Pest Management Science

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BACKGROUNDMicrobially derived, protein‐based biopesticides are an important approach for sustainable pest management. The secreted insecticidal proteins (Sips) produced by the bacterium Bacillus thuringiensis exhibit potent insecticidal activity against coleopteran pests and are, therefore, attractive as candidate biopesticides. However, the modes‐of‐action of Sips are unclear as comprehensive structural information for these proteins is lacking.RESULTSUsing X‐ray crystallography, we elucidated the structure of monomeric Sip1Ab at 2.28 Å resolution. Structural analyses revealed that Sip1Ab has the three domains and conserved fold characteristic of other aerolysin‐like beta‐pore‐forming toxins (β‐PFTs). Based on the sequence and structural similarities between Sip1Ab and other ETX_MTX2 subfamily toxins, we suggested the mechanism of these proteins and proposed that it is common to them all.CONCLUSIONThe atomic‐level structural data for Sip1Ab generated by the present study could facilitate future structural and mechanistic research on Sips as well as their application in sustainable insect pest management. © 2023 Society of Chemical Industry.

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Structural Basis of the Pore-Forming Toxin/Membrane Interaction

Cited by 27 publications

References 142 publications

Bacterial pore-forming toxins

Bacterial pore-forming toxins

Challenges and approaches to studying pore-forming proteins

Structural insight into Bacillus thuringiensis Sip1Ab reveals its similarity to ETX_MTX2 family beta‐pore‐forming toxin

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