Membrane Binding and Pore Formation of the Antibacterial Peptide PGLa:  Thermodynamic and Mechanistic Aspects†

Biochemistry ◽  
2000 ◽  
Vol 39 (2) ◽  
pp. 442-452 ◽  
Author(s):  
Torsten Wieprecht ◽  
Ognjan Apostolov ◽  
Michael Beyermann ◽  
Joachim Seelig
Keyword(s):  
Pore Formation ◽  
Membrane Binding ◽  
Antibacterial Peptide

scholarly journals Dual modes of membrane binding direct pore formation by Streptolysin O

2015 ◽  
Vol 97 (6) ◽  
pp. 1036-1050 ◽  
Author(s):  
Cara C. Mozola ◽  
Michael G. Caparon
Keyword(s):  
Pore Formation ◽  
Membrane Binding ◽  
Streptolysin O

The structural basis for membrane binding and pore formation by lymphocyte perforin

Nature ◽  
2010 ◽  
Vol 468 (7322) ◽  
pp. 447-451 ◽  
Author(s):  
Ruby H. P. Law ◽  
Natalya Lukoyanova ◽  
Ilia Voskoboinik ◽  
Tom T. Caradoc-Davies ◽  
Katherine Baran ◽  
...  
Keyword(s):  
Pore Formation ◽  
Membrane Binding ◽  
Structural Basis

scholarly journals Bax-type Apoptotic Proteins Porate Pure Lipid Bilayers through a Mechanism Sensitive to Intrinsic Monolayer Curvature

2002 ◽  
Vol 277 (51) ◽  
pp. 49360-49365 ◽  
Author(s):  
Gorka Basañez ◽  
Juanita C. Sharpe ◽  
Jennifer Galanis ◽  
Teresa B. Brandt ◽  
J. Marie Hardwick ◽  
...  
Keyword(s):  
Lipid Bilayers ◽  
Mitochondrial Membrane ◽  
Pore Formation ◽  
Membrane Binding ◽  
Membrane Permeabilization ◽  
Outer Mitochondrial Membrane ◽  
Intrinsic Curvature ◽  
Differential Effects ◽  
Cleavage Fragment ◽  
Induced Changes

During apoptosis, Bax-type proteins permeabilize the outer mitochondrial membrane to release intermembrane apoptogenic factors into the cytosol via a poorly understood mechanism. We have proposed that Bax and ΔN76Bcl-xL(the Bax-like cleavage fragment of Bcl-xL) function by forming pores that are at least partially composed of lipids (lipidic pore formation). Since the membrane monolayer must bend during lipidic pore formation, we here explore the effect of intrinsic membrane monolayer curvature on pore formation. Nonlamellar lipids with positive intrinsic curvature such as lysophospholipids promoted membrane permeabilization, whereas nonlamellar lipids with negative intrinsic curvature such as diacylglycerol and phosphatidylethanolamine inhibited membrane permeabilization. The differential effects of nonlamellar lipids on membrane permeabilization were not correlated with lipid-induced changes in membrane binding or insertion of Bax or ΔN76Bcl-xL. Altogether, these results are consistent with a model whereby Bax-type proteins change the bending propensity of the membrane to form pores comprised at least in part of lipids in a structure of net positive monolayer curvature.

Membrane Binding and Pore Formation by a Cytotoxic Fragment of Amyloid β Peptide

2017 ◽  
Vol 121 (45) ◽  
pp. 10293-10305 ◽  
Author(s):  
Nabin Kandel ◽  
Tianyu Zheng ◽  
Qun Huo ◽  
Suren A. Tatulian
Keyword(s):  
Pore Formation ◽  
Membrane Binding ◽  
Amyloid Β ◽  
Amyloid Β Peptide

Divalent cations modulate membrane binding and pore formation of a potent antibiotic peptide analog of alamethicin

Cell Calcium ◽  
2013 ◽  
Vol 53 (3) ◽  
pp. 180-186 ◽  
Author(s):  
Marco Aquila ◽  
Mascia Benedusi ◽  
Karl-Wilhelm Koch ◽  
Daniele Dell’Orco ◽  
Giorgio Rispoli
Keyword(s):  
Pore Formation ◽  
Divalent Cations ◽  
Membrane Binding ◽  
Peptide Analog ◽  
Antibiotic Peptide

Piercing the lipid raft: the case of Vibrio cholerae cytolysin

2018 ◽  
Vol 475 (24) ◽  
pp. 3917-3919
Author(s):  
Normand Cyr
Keyword(s):  
Vibrio Cholerae ◽  
Lipid Bilayer ◽  
Lipid Raft ◽  
Pore Formation ◽  
Membrane Binding ◽  
Membrane Lipid ◽  
Recent Issue ◽  
Biochemical Journal ◽  
Oligomeric Assembly ◽  
Binding Capability

In a recent issue of Biochemical Journal, Kathuria et al. [Biochem. J. (2018) 475, 3039–3055] report that membrane binding of the pore-forming toxin Vibrio cholerae cytolysin (VCC) is facilitated by the presence of cholesterol, and the presence of this sterol within the lipid bilayer is key for the formation of a functional pore. Yet, in the presence of accessory non-lipid components, VCC retains its membrane-binding capability likely through membrane lipid raft structures. In light of their results, the authors provide new insights into the roles of cholesterol and of membrane microstructures in the binding, the oligomeric assembly and the cytolytic pore formation of VCC which all take place following infection by V. cholerae.

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