scholarly journals Mechanisms of Action of Probiotics based on Bacillus subtilis

2016 ◽  
Vol 0 (2.11) ◽  
pp. 35 ◽  
Author(s):  
A.V. Savustyanenko
2005 ◽  
Vol 73 (1) ◽  
pp. 31-36 ◽  
Author(s):  
Y. Douville ◽  
J.G. Boland

The influence and mechanisms of action of Bacillus subtilis on Colletotrichum trifolii, a causal agent of anthracnose of alfalfa (Medicago sativa), were studied in vivo and in vitro. In growth room conditions, a cell-free culture filtrate of B. subtilis significantly reduced disease incidence and severity on alfalfa seedlings from 56% to 16% and from 2.0 to 1.2, respectively. Treatment of seedlings with washed cell suspensions of B. subtilis had no influence on disease. Applications of crude filtrate on alfalfa leaflets inoculated with C. trifolii were associated with reduced germination of conidia, lysis of conidia, and reduced formation of appressoria. Under in vitro conditions, crude filtrate reduced germination of conidia, and induced lysis of conidia and the formation of inflated germ tubes on germinating conidia. An antibiotic of the iturin family, iturin D, was tentatively identified as the active compound responsible for the suppressive effect of B. subtilis on C. trifolii.


PLoS ONE ◽  
2014 ◽  
Vol 9 (1) ◽  
pp. e87454 ◽  
Author(s):  
Renata Damásio de Souza ◽  
Milene Tavares Batista ◽  
Wilson Barros Luiz ◽  
Rafael Ciro Marques Cavalcante ◽  
Jaime Henrique Amorim ◽  
...  

Author(s):  
Dwight Anderson ◽  
Charlene Peterson ◽  
Gursaran Notani ◽  
Bernard Reilly

The protein product of cistron 3 of Bacillus subtilis bacteriophage Ø29 is essential for viral DNA synthesis and is covalently bound to the 5’-termini of the Ø29 DNA. When the DNA-protein complex is cleaved with a restriction endonuclease, the protein is bound to the two terminal fragments. The 28,000 dalton protein can be visualized by electron microscopy as a small dot and often is seen only when two ends are in apposition as in multimers or in glutaraldehyde-fixed aggregates. We sought to improve the visibility of these small proteins by use of antibody labeling.


2003 ◽  
Vol 19 (3) ◽  
pp. 164-174 ◽  
Author(s):  
Stephen N. Haynes ◽  
Andrew E. Williams

Summary: We review the rationale for behavioral clinical case formulations and emphasize the role of the functional analysis in the design of individualized treatments. Standardized treatments may not be optimally effective for clients who have multiple behavior problems. These problems can affect each other in complex ways and each behavior problem can be influenced by multiple, interacting causal variables. The mechanisms of action of standardized treatments may not always address the most important causal variables for a client's behavior problems. The functional analysis integrates judgments about the client's behavior problems, important causal variables, and functional relations among variables. The functional analysis aids treatment decisions by helping the clinician estimate the relative magnitude of effect of each causal variable on the client's behavior problems, so that the most effective treatments can be selected. The parameters of, and issues associated with, a functional analysis and Functional Analytic Clinical Case Models (FACCM) are illustrated with a clinical case. The task of selecting the best treatment for a client is complicated because treatments differ in their level of specificity and have unequally weighted mechanisms of action. Further, a treatment's mechanism of action is often unknown.


Author(s):  
Joe L. Martinez ◽  
Patricia H. Janak ◽  
Susan B. Weinberger ◽  
Gery Schulteis

Planta Medica ◽  
2008 ◽  
Vol 74 (09) ◽  
Author(s):  
N Padilla-Montaño ◽  
IL Bazzocchi ◽  
L Moujir

Planta Medica ◽  
2012 ◽  
Vol 78 (11) ◽  
Author(s):  
CBS Lau ◽  
VKM Lau ◽  
CL Liu ◽  
PKK Lai ◽  
JCW Tam ◽  
...  

Planta Medica ◽  
2016 ◽  
Vol 81 (S 01) ◽  
pp. S1-S381 ◽  
Author(s):  
B Ovalle-Magallanes ◽  
A Madariaga-Mazón ◽  
A Navarrete ◽  
R Mata

1979 ◽  
Author(s):  
L Miles ◽  
J Burnier ◽  
M Verlander ◽  
M Goodman ◽  
A Kleiss ◽  
...  

Flu-HPA is one of a series of flufenamic acid derivations that enhances plasminogen-dependent clot lysis in vitro. Studies of possible mechanisms of action of Flu-HPA were undertaken. The influence of Flu-HPA on the inhibition of purified plasmin by purified PI was studied. PI activity was assessed by its inhibition of the clevage of the tripeptide S-2251 (H-D-Val-Leu-Lys-pNA) by plasmin. Flu-HPA was dissolved in DMF or in methonol and preincubated with PI before addition of plasmin. At Flu-HPA concentrations greater than 1mM and up to 60mM, the inhibitory activity of PI was totally lost. The inhibitory effect of normal human plasma on plasmin was also completely abolished at concentrations of Flu-HPA between 2.5 and 40mM. The effect of Flu-HPA on the inhibition of purified plasma kallikrein by purified CI-Inh was also studied. CI-Inh activity was measured by its inhibition of cleavage of the tripeptide Bz-Pro-Phe-Arg-pNA by kallikrein. When Flu-HPA, dissolved in DMF or in methonol, was preincubated with CI-Inh, a concentration dependent inhibition of CI-Inh activity was observed. CI-Inh activity was abolished by concentrations of Flu-HPA greater than 1mM. Flu-HPA also inhibited the activity of CI-Inh on purified Factor XIIa. These observations suggest that this flufenamic acid derivative may enhance fibrinolysis not only by inhibiting PI activity but also by decreasing the inactivation of plasminogen activators by CI-Inh.


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