Functional analysis of a putative holin-like peptide-coding gene in the genome of Bacillus licheniformis AnBa9

作者：Anthony Thangamani; Chellappa Gunasekaran Stalin; Rajesh Thangamani; Gunasekaran Paramasamy^*

来源：Archives of Microbiology, 2010, 192(1): 51-56.

DOI：10.1007/s00203-009-0530-7

• Bacillus licheniformis
• BhlA
• Holin-like protein
• Transmembrane domain
• Antibacterial activity
• Yeast surface display

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 Micrococcus luteus. Deletion analysis of bhlA suggests that a hydrophobic transmembrane domain, BhlATM is essential for antibacterial activity. Though the minimum inhibitory concentration (MIC) of BhlA was sevenfold lower than BhlATM, transmembrane domain deleted construct (BhlAa dagger TM) had no antibacterial activity. The expression of BhlA in E. coli was found to be toxic to cells. Therefore, the bhlA was cloned in yeast surface display vector pYD1 and expressed in Saccharomyces cerevisiae. The surface displayed yeast showed inhibition of several gram-positive bacteria. This recombinant yeast expressing BhlA may be used as biodrug for efficient control of multiple drug-resistant bacterial infections.

• 出版日期2010-1