Functional analysis of a putative holin-like peptide-coding gene in the genome of Bacillus licheniformis AnBa9.
作者： P Gunasekaran T Anthony , GS Chellappa , T Rajesh , None
DOI: 10.1007/S00203-009-0530-7
关键词: Transmembrane domain 、 Yeast 、 Holin 、 Biochemistry 、 Microbiology 、 Bacteria 、 Antibacterial agent 、 Bacillus licheniformis 、 Escherichia coli 、 Saccharomyces cerevisiae 、 Biology
摘要: BhlA, a putative holin-like protein of Bacillus licheniformis AnBa9 expressed in Escherichia coli BL21(DE3) showed antibacterial activity against several gram-positive bacteria including methicillin-resistant Staphylococcus aureus (MRSA) and Micrococcusluteus. Deletion analysis bhlA suggests that hydrophobic transmembrane domain, BhlATM is essential for activity. Though the minimum inhibitory concentration (MIC) BhlA was sevenfold lower than BhlATM, domain deleted construct (BhlA∆TM) had no The expression E. found to be toxic cells. Therefore, cloned yeast surface display vector pYD1 Saccharomyces cerevisiae. displayed inhibition bacteria. This recombinant expressing may used as biodrug efficient control multiple drug-resistant bacterial infections.
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