Induction of antibacterial activity in the haemolymph of the silkworm, Bombyx mori, by injection of formalin-treated Escherichia coli K-12 in the anterior and posterior body part of the ligated larvae

1992 ◽  
Vol 101 (1-2) ◽  
pp. 173-178 ◽  
Author(s):  
Motoyuki Sumida ◽  
Hiromasa Ichimori ◽  
Tamon Yuhki ◽  
Hajime Mori ◽  
Fujiyoshi Matsubara
Keyword(s):  
Escherichia Coli ◽  
Antibacterial Activity ◽  
Bombyx Mori ◽  
Body Part ◽  
K 12 ◽  
Silkworm Bombyx Mori

scholarly journals Ib-M6 Antimicrobial Peptide: Antibacterial Activity against Clinical Isolates of Escherichia coli and Molecular Docking

Antibiotics ◽  
2020 ◽  
Vol 9 (2) ◽  
pp. 79 ◽  
Author(s):  
J. M. Flórez-Castillo ◽  
P. Rondón-Villareal ◽  
J. L. Ropero-Vega ◽  
S. Y. Mendoza-Espinel ◽  
J. A. Moreno-Amézquita ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Antibacterial Activity ◽  
Molecular Docking ◽  
Outer Membrane ◽  
Docking Simulations ◽  
E Coli ◽  
Pathogenic Escherichia Coli ◽  
Membrane Components ◽  
K 12 ◽  
Susceptibility Assay

The Ib-M6 peptide has antibacterial activity against non-pathogenic Escherichia coli K-12 strain. The first part of this study determines the antibacterial activity of Ib-M6 against fourteen pathogenic strains of E. coli O157:H7. Susceptibility assay showed that Ib-M6 had values of Minimum Inhibitory Concentration (MIC) lower than streptomycin, used as a reference antibiotic. Moreover, to predict the possible interaction between Ib-M6 and outer membrane components of E. coli, we used molecular docking simulations where FhuA protein and its complex with Lipopolysaccharide (LPS–FhuA) were used as targets of the peptide. FhuA/Ib-M6 complexes had energy values between −39.5 and −40.5 Rosetta Energy Units (REU) and only one hydrogen bond. In contrast, complexes between LPS–FhuA and Ib-M6 displayed energy values between −25.6 and −40.6 REU, and the presence of five possible hydrogen bonds. Hence, the antimicrobial activity of Ib-M6 peptide shown in the experimental assays could be caused by its interaction with the outer membrane of E. coli.

scholarly journals Eclosion hormone of the silkworm Bombyx mori Expression in Escherichia coli and location of disulfide bonds

FEBS Letters ◽  
1990 ◽  
Vol 263 (2) ◽  
pp. 358-360 ◽  
Author(s):  
Takaharu Kono ◽  
Hiromichi Nagasawa ◽  
Hiroshi Kataoka ◽  
Akira Isogai ◽  
Hajime Fugo ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Bombyx Mori ◽  
Disulfide Bonds ◽  
Eclosion Hormone ◽  
Expression In Escherichia Coli ◽  
Silkworm Bombyx Mori
Sign in / Sign up

Export Citation Format

Share Document