Native Escherichia coli OmpF porin surfaces probed by atomic force microscopy

Science ◽  
1995 ◽  
Vol 268 (5207) ◽  
pp. 92-94 ◽  
Author(s):  
F. Schabert ◽  
C Henn ◽  
A Engel
Keyword(s):  
Escherichia Coli ◽  
Atomic Force Microscopy ◽  
Ompf Porin ◽  
Force Microscopy ◽  
Atomic Force

Membranolytic Effects of KT2 on Gram-Negative Escherichia coli Evaluated by Atomic Force Microscopy

2019 ◽  
Vol 55 (5) ◽  
pp. 495-505
Author(s):  
T. Theansungnoen ◽  
N. Jangpromma ◽  
P. Anwised ◽  
S. Daduang ◽  
Y. Fukumori ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Atomic Force Microscopy ◽  
Gram Negative ◽  
Force Microscopy ◽  
Atomic Force

Imaging of reconstituted biological channels at molecular resolution by atomic force microscopy

1993 ◽  
Vol 265 (3) ◽  
pp. C851-C856 ◽  
Author(s):  
R. Lal ◽  
H. Kim ◽  
R. M. Garavito ◽  
M. F. Arnsdorf
Keyword(s):  
Atomic Force Microscopy ◽  
High Resolution ◽  
Internal Control ◽  
Imaging Method ◽  
Buffer Solution ◽  
Electron Microscopic ◽  
Ompf Porin ◽  
Force Microscopy ◽  
Atomic Force ◽  
Rectangular Pattern

Using atomic force microscopy (AFM), we obtained high-resolution surface images of the bacterial outer membrane channels Escherichia coli OmpF porin and Bordetella pertussis porin that were reconstituted in artificial bilayer membranes as two-dimensional crystalline arrays. These porins were chosen because they are among the most extensively studied proteins of this type and are known for their well-defined crystalline nature in the native membrane. Such reconstituted membrane proteins are ideal specimens to assess the suitability and resolution of AFM for imaging biomembranes and associated proteins. Although OmpF porin often showed a mixed pattern of rectangular and hexagonal arrays with approximately 8.4 x 9.8- and approximately 7.2-nm-spacings, respectively, B. pertussis porin showed mostly a rectangular pattern with an approximately 7.9 x 13.8-nm spacing. The packing patterns of the E. coli OmpF porin in the membrane are very close to those found in electron-microscopic studies. When B. pertussis porin was imaged in a buffer solution, its trimeric subunits were apparently resolved, and the surface of each monomer revealed beadlike structures. This is the first report of such a high-resolution structural analysis of B. pertussis porin by any imaging method. We also imaged the lipid bilayer itself as an internal control for imaging and to further ascertain the resolution. Individual polar head groups of bilayer lipid molecules were resolved, suggesting the intrinsic resolution of AFM for bioimaging.

Atomic Force Microscopy of Escherichia coli FoF1-ATPase in Reconstituted Membranes

1997 ◽  
Vol 834 (1 Na/K-ATPase a) ◽  
pp. 149-152 ◽  
Author(s):  
KUNIO TAKEYASU ◽  
HIROSHI OMOTE ◽  
SAJU NETTIKADAN ◽  
FUYUKI TOKUMASU ◽  
ATSUKO IWAMOTO-KIHARA ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Atomic Force Microscopy ◽  
Force Microscopy ◽  
Atomic Force ◽  
Reconstituted Membranes ◽  
Fof1 Atpase

scholarly journals Atomic Force Microscopy Study of the Effect of Antimicrobial Peptides on the Cell Envelope of Escherichia coli

2005 ◽  
Vol 49 (10) ◽  
pp. 4085-4092 ◽  
Author(s):  
M. Meincken ◽  
D. L. Holroyd ◽  
M. Rautenbach
Keyword(s):  
Escherichia Coli ◽  
Atomic Force Microscopy ◽  
Morphological Changes ◽  
Cell Envelope ◽  
Microscopy Study ◽  
Target Cells ◽  
Force Microscopy ◽  
E Coli ◽  
Atomic Force ◽  
Before And After

ABSTRACT The influences of the antibacterial magainin 2 and PGLa from the African clawed frog (Xenopus laevis) and the hemolytic bee venom melittin on Escherichia coli as the target cell were studied by atomic force microscopy (AFM). Nanometer-scale images of the effects of the peptides on this gram-negative bacterium's cell envelope were obtained in situ without the use of fixing agents. These high-resolution AFM images of the surviving and intact target cells before and after peptide treatment showed distinct changes in cell envelope morphology as a consequence of peptide action. Although all three peptides are lytic to E. coli, it is clear from this AFM study that each peptide causes distinct morphological changes in the outer membrane and in some cases the inner membrane, probably as a consequence of different mechanisms of action.

A new method of biosensing with 1μl of Escherichia coli suspension using atomic force microscopy

2005 ◽  
Vol 345 (1) ◽  
pp. 116-121 ◽  
Author(s):  
Satoshi Tanaka ◽  
Hiroaki Sugasawa ◽  
Takashi Morii ◽  
Takao Okada ◽  
Masanori Abe ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Atomic Force Microscopy ◽  
New Method ◽  
Force Microscopy ◽  
Atomic Force

Morphological analysis of the antimicrobial action of silver and gold nanoparticles stabilized with ceftriaxone on Escherichia coli using atomic force microscopy

2014 ◽  
Vol 38 (11) ◽  
pp. 5633-5640 ◽  
Author(s):  
Muhammad Raza Shah ◽  
Shujat Ali ◽  
Muhammad Ateeq ◽  
Samina Perveen ◽  
Shakil Ahmed ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Gold Nanoparticles ◽  
Atomic Force Microscopy ◽  
Silver Nanoparticles ◽  
Morphological Analysis ◽  
Antimicrobial Action ◽  
Antibacterial Action ◽  
Gold And Silver Nanoparticles ◽  
Force Microscopy ◽  
Atomic Force

Monitoring the antibacterial action of gold and silver nanoparticlesviaAFM.

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