Computer-Aided Drug Design and Molecular Modeling Lab, Department of Bioinformatics, Alagappa University, Karaikudi, 630004, Tamil Nadu, India.
Appl Biochem Biotechnol. 2014 Feb;172(4):1790-806. doi: 10.1007/s12010-013-0641-0. Epub 2013 Nov 22.
Bacillus anthracis is a well-known bioweapon pathogen, which coordinates the expression of its virulence factors in response to a specific environmental signal by its protein architecture. Absences of sortase signal functioning may fail to assemble the surface linked proteins and so B. anthracis cannot sustain an infection with host cells. Targeting the signaling mechanism of B. anthracis can be achieved by inhibition of SrtA enzyme through λphage-derived plyG. The lysin enzyme plyG is experimentally proven as bacteriolytic agent, specifically kill's B. anthracis by inhibiting the SrtA. Here, we have screened the peptides from λphage lysin, and these peptides are having the ability as LPXTG competitive inhibitors. In comparison to the activator peptide LPXTG binding motif, λphage lysin based inhibitor peptides are having much supremacy towards binding of SrtA. Finally, peptide structures extracted from PlyG are free from toxic, allergic abilities and also have the ability to terminate the signal transduction mechanism in B. anthracis.
炭疽杆菌是一种众所周知的生物武器病原体，它通过其蛋白质结构对特定的环境信号做出响应，协调其毒力因子的表达。如果缺少信号转导酶的功能，表面连接蛋白就无法组装，因此炭疽杆菌无法在宿主细胞中维持感染。通过抑制 SrtA 酶来靶向炭疽杆菌的信号机制，可通过 λ噬菌体衍生的 plyG 来实现。lysG 酶是一种实验证明的溶菌酶，通过抑制 SrtA 特异性杀死炭疽杆菌。在这里，我们从 λ噬菌体溶菌酶中筛选出肽，这些肽具有 LPXTG 竞争性抑制剂的能力。与激活肽 LPXTG 结合基序相比，λ噬菌体溶菌酶抑制剂肽对 SrtA 的结合具有更大的优势。最后，从 PlyG 中提取的肽结构没有毒性、过敏能力，并且能够终止炭疽杆菌中的信号转导机制。
