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Title: Decreasing transmembrane segment length greatly decreases perfringolysin O pore size

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.
Authors:
 [1] ;  [2] ;  [3] ;  [1]
  1. Stony Brook Univ., Stony Brook, NY (United States)
  2. Stony Brook Univ., Stony Brook, NY (United States); Brookhaven National Lab. (BNL), Upton, NY (United States)
  3. Brookhaven National Lab. (BNL), Upton, NY (United States)
Publication Date:
OSTI Identifier:
1215609
Report Number(s):
BNL--108347-2015-JA
Journal ID: ISSN 0022-2631; 400412000
Grant/Contract Number:
SC00112704
Type:
Accepted Manuscript
Journal Name:
Journal of Membrane Biology
Additional Journal Information:
Journal Volume: 248; Journal Issue: 3; Journal ID: ISSN 0022-2631
Publisher:
Springer
Research Org:
Brookhaven National Laboratory (BNL), Upton, NY (United States)
Sponsoring Org:
National Institute of Health
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES cholesterol-dependent cytolysin; bacterial toxin proteins; cholesterol; transmembrane protein; hydrophobic mismatch