Next Article in Journal
Lobster Supply Chains Are Not at Risk from Paralytic Shellfish Toxin Accumulation during Wet Storage
Next Article in Special Issue
Folding Control in the Path of Type 5 Secretion
Previous Article in Journal
De Novo Venom-Gland Transcriptomics of Spine-Bellied Sea Snake (Hydrophis curtus) from Penang, Malaysia—Next-Generation Sequencing, Functional Annotation and Toxinological Correlation
Previous Article in Special Issue
Pathogenic Pore Forming Proteins of Plasmodium Triggers the Necrosis of Endothelial Cells Attributed to Malaria Severity
Review

Structural Basis of the Pore-Forming Toxin/Membrane Interaction

1
Department of Clinical Laboratory, the First Affiliated Hospital of Anhui Medical University, Hefei 230022, China
2
Hefei National Laboratory for Physical Sciences at Microscale, Laboratory of Structural Immunology, CAS Key Laboratory of Innate Immunity and Chronic Disease, Division of Life Sciences and Medicine, School of Basic Medical Sciences, University of Science and Technology of China, Hefei 230027, China
*
Authors to whom correspondence should be addressed.
Toxins 2021, 13(2), 128; https://doi.org/10.3390/toxins13020128
Received: 26 October 2020 / Revised: 13 January 2021 / Accepted: 2 February 2021 / Published: 9 February 2021
(This article belongs to the Special Issue Bacterial Toxins: Protein Folding and Membrane Interactions)
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. View Full-Text
Keywords: pore-forming toxin; structure; membrane interaction pore-forming toxin; structure; membrane interaction
Show Figures

Figure 1

MDPI and ACS Style

Li, Y.; Li, Y.; Mengist, H.M.; Shi, C.; Zhang, C.; Wang, B.; Li, T.; Huang, Y.; Xu, Y.; Jin, T. Structural Basis of the Pore-Forming Toxin/Membrane Interaction. Toxins 2021, 13, 128. https://doi.org/10.3390/toxins13020128

AMA Style

Li Y, Li Y, Mengist HM, Shi C, Zhang C, Wang B, Li T, Huang Y, Xu Y, Jin T. Structural Basis of the Pore-Forming Toxin/Membrane Interaction. Toxins. 2021; 13(2):128. https://doi.org/10.3390/toxins13020128

Chicago/Turabian Style

Li, Yajuan, Yuelong Li, Hylemariam M. Mengist, Cuixiao Shi, Caiying Zhang, Bo Wang, Tingting Li, Ying Huang, Yuanhong Xu, and Tengchuan Jin. 2021. "Structural Basis of the Pore-Forming Toxin/Membrane Interaction" Toxins 13, no. 2: 128. https://doi.org/10.3390/toxins13020128

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop