Efficient Production and Purification of Bioactive E50-52-Class IIa Peptidic Bacteriocin Is Achieved through Fusion with the Catalytic Domain of Lysostaphin-Class III Bacteriocin.

E50-52, a class IIa-peptidic bacteriocin produced by a strain of , has broad-spectrum antimicrobial activity against various foodborne pathogens. However, effective utilization of the E50-52 has been limited by low production yields and challenges associated with separation and purification of this 39-amino acid antimicrobial peptide. In this study, we have successfully produced a biologically active recombinant form of E50-52 by fusing it with the 16-kDa catalytic domain of lysostaphin-class III bacteriocin (LssCAT), which resulted in high-yield production.

Effects of anodal tDCS on resting state eeg power and motor function in acute stroke: a randomized controlled trial.

Background: Anodal transcranial direct current stimulation (tDCS) is a beneficial adjunctive tool in stroke rehabilitation. However, only a few studies have investigated its effects on acute stroke and recruited only individuals with mild motor deficits. This study investigated the effect of five consecutive sessions of anodal tDCS and conventional physical therapy on brain activity and motor outcomes in individuals with acute stroke, with low and high motor impairments.

Bacillus thuringiensis Cry4Ba toxin employs two receptor-binding loops for synergistic interactions with Cyt2Aa2.

We previously demonstrated that co-expression in Escherichia coli of Bacillus thuringiensis (Bt) subsp. israelensis Cry4Ba and Bt subsp. darmstadiensis Cyt2Aa2 shows high synergistic toxicity against target mosquito larvae.

Correlative effect on the toxicity of three surface-exposed loops in the receptor-binding domain of the Bacillus thuringiensis Cry4Ba toxin.

Surface-exposed loop residues, Pro(389) (beta(6)-beta(7) loop), Glu(417) (beta(8)-beta(9) loop), Tyr(455) and Asn(456) (beta(10)-beta(11) loop), in the receptor-binding domain of the Bacillus thuringiensis Cry4Ba toxin have been previously demonstrated to be crucial for toxicity. Herein, five combinations of two-loop mutants, P389A/E417A (beta(6)-beta(7)/beta(8)-beta(9) loops), P389A/Y455A, P389A/N456A (beta(6)-beta(7)/beta(10)-beta(11) loops), E417A/Y455A and E417A/N456A (beta(8)-beta(9)/beta(10)-beta(11) loops), were constructed as a means of examining a correlative effect of these three critical loops on Cry4Ba toxicity. All 130-kDa mutant protoxins were overexpressed as inclusion bodies in Escherichia coli with yields comparable to the wild-type toxin.