ArticleThe Journal of membrane biology2015
Decreasing Transmembrane Segment Length Greatly Decreases Perfringolysin O Pore Size.
Article in The Journal of membrane biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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Who cites it
5 citing papers in PubMed.
- Beyond pore formation: reorganization of the plasma membrane induced by pore-forming proteins.Cellular and molecular life sciences : CMLS · 2021Review
- Islet Amyloid Polypeptide Membrane Interactions: Effects of Membrane Composition.Biochemistry · 2017Article
- Using ApoE Nanolipoprotein Particles To Analyze SNARE-Induced Fusion Pores.Langmuir : the ACS journal of surfaces and colloids · 2016Article
- Membrane Protein Folding & Lipid Interactions: Theory & Experiment.The Journal of membrane biology · 2015Article
- Review
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Perfringolysin O (PFO) is a transmembrane (TM) β-barrel protein that inserts into mammalian cell membranes. Once inserted into membranes, PFO assembles into pore-forming oligomers containing 30-50 PFO monomers. These form a pore of up to 300 Å, far exceeding the size of most other proteinaceous pores. In this study, we found that altering PFO TM segment length can alter the size of PFO pores. A PFO mutant with lengthened TM segments oligomerized to a similar extent as wild-type PFO, and exhibited pore-forming activity and a pore size very similar to wild-type PFO as measured by electron microscopy and a leakage assay. In contrast, PFO with shortened TM segments exhibited a large reduction in pore-forming activity and pore size. This suggests that the interaction between TM segments can greatly affect the size of pores formed by TM β-barrel proteins. PFO may be a promising candidate for engineering pore size for various applications.
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Registered trials
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