Du Yufeng, Liu Li, Zhang Chunping, Zhang Yani
College of Life Sciences, Northwest University, Xi'an 710069, China,
Ultrasonic Diagnosis Department, Shaanxi Provincial People's Hospital, Xi'an 710068, China.
Infect Drug Resist. 2018 Aug 21;11:1271-1274. doi: 10.2147/IDR.S167779. eCollection 2018.
is becoming increasingly intractable because of its ability to acquire antimicrobial resistance and secrete numerous virulence factors that can exacerbate inflammation. Alpha-hemolysin (Hla) is a pore-forming virulence factor produced by that can self-assemble into heptameric mushroom-structured pores in target cell membranes, leading to cell lysis and death. In the present study, we sought to better understand the mechanism underlying hemolysis and the oligomerization of Hla by creating nine mutants with single amino acid changes in different positions of the Hla protein: N17C, T18C, P103C, N105C, M113C, T117C, N121C, D128C, and T129C. The results showed that the P103C and N105C mutations, which are located in the triangle region, significantly diminished hemolysis and heptamer formation when compared with the wild-type Hla protein. This suggests that the P103 and N105 residues play key roles in the assembly of the Hla pore. These results improve our understanding of the mechanism underlying the pore-forming ability of Hla.
由于其获得抗微生物耐药性的能力以及分泌众多可加剧炎症的毒力因子，它正变得越来越难以对付。α-溶血素（Hla）是由[具体产生源未提及]产生的一种成孔毒力因子，它可以在靶细胞膜中自组装成七聚体蘑菇状孔道，导致细胞裂解和死亡。在本研究中，我们试图通过在Hla蛋白的不同位置创建九个单氨基酸变化的突变体：N17C、T18C、P103C、N105C、M113C、T117C、N121C、D128C和T129C，来更好地理解溶血和Hla寡聚化的潜在机制。结果表明，位于三角形区域的P103C和N105C突变与野生型Hla蛋白相比，显著降低了溶血和七聚体形成。这表明P103和N105残基在Hla孔道的组装中起关键作用。这些结果增进了我们对Hla成孔能力潜在机制的理解。
