Streptolysin O:  Inhibition of the Conformational Change during Membrane Binding of the Monomer Prevents Oligomerization and Pore Formation†

Biochemistry ◽  
1999 ◽  
Vol 38 (46) ◽  
pp. 15204-15211 ◽  
Author(s):  
El Moeiz Abdel Ghani ◽  
Silvia Weis ◽  
Ivan Walev ◽  
Michael Kehoe ◽  
Sucharit Bhakdi ◽  
...  
Keyword(s):  
Conformational Change ◽  
Pore Formation ◽  
Membrane Binding ◽  
Streptolysin O

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.

scholarly journals Use of a monoclonal antibody to determine the mode of transmembrane pore formation by streptolysin O.

1986 ◽  
Vol 54 (3) ◽  
pp. 641-645 ◽  
Author(s):  
F Hugo ◽  
J Reichwein ◽  
M Arvand ◽  
S Krämer ◽  
S Bhakdi
Keyword(s):  
Monoclonal Antibody ◽  
Pore Formation ◽  
Streptolysin O

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

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 How Could SNARE Proteins Open a Fusion Pore?

Physiology ◽  
2014 ◽  
Vol 29 (4) ◽  
pp. 278-285 ◽  
Author(s):  
Qinghua Fang ◽  
Manfred Lindau
Keyword(s):  
Conformational Change ◽  
Pore Formation ◽  
Vesicle Fusion ◽  
Neurosecretory Cells ◽  
Snare Complex ◽  
Snare Proteins ◽  
Fusion Pore ◽  
Receptor Complex ◽  
Attachment Protein ◽  
Protein Receptor

The SNARE (Soluble NSF Attachment protein REceptor) complex, which in mammalian neurosecretory cells is composed of the proteins synaptobrevin 2 (also called VAMP2), syntaxin, and SNAP-25, plays a key role in vesicle fusion. In this review, we discuss the hypothesis that, in neurosecretory cells, fusion pore formation is directly accomplished by a conformational change in the SNARE complex via movement of the transmembrane domains.

Mechanism of protein-induced membrane fusion: fusion of phospholipid vesicles by clathrin associated with its membrane binding and conformational change

Biochemistry ◽  
1989 ◽  
Vol 28 (3) ◽  
pp. 1422-1428 ◽  
Author(s):  
Shigenori Maezawa ◽  
Tetsuro Yoshimura ◽  
Keelung Hong ◽  
Nejat Duzgunes ◽  
Demetrios Papahadjopoulos
Keyword(s):  
Membrane Fusion ◽  
Conformational Change ◽  
Membrane Binding ◽  
Phospholipid Vesicles ◽  
Induced Membrane

scholarly journals Mechanism of Pore Formation on Erythrocyte Membrane by Streptolysin-O

1993 ◽  
Vol 67 (8) ◽  
pp. 736-740 ◽  
Author(s):  
Kachiko SEKIYA ◽  
Hirofumi DANBARA ◽  
Yutaka FUTAESAKU
Keyword(s):  
Erythrocyte Membrane ◽  
Pore Formation ◽  
Streptolysin O
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