Dual functions of discoidinolysin, a cholesterol-dependent cytolysin with N-terminal discoidin domain produced from Streptococcus mitis strain Nm-76.
Dual functions of discoidinolysin, a cholesterol-dependent cytolysin with N-terminal discoidin domain produced from Streptococcus mitis strain Nm-76.
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DOI：
10.1080/20002297.2022.2105013
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发表时间：
2022
影响因子：
4.5
通讯作者：
中科院分区：
文献类型：
--
作者：
一些缓症链球菌菌株由于胆固醇依赖性溶细胞素（CDC）的β-溶血活性而表现出β-溶血。最近，在S.缓症菌菌株Nm-76。然而，该基因的产物仍然未被表征。我们的目的是描述这种非典型CDC及其分子功能和对S.缓症菌菌株Nm-76。基于网络存储的信息进行CDC基因的系统发育分析。利用基因缺失突变株和重组蛋白在大肠杆菌中表达，研究CDC的分子特征。在Nm-76中发现的编码CDC的基因及其同源物分布在许多S.缓症菌株。这种CDC在遗传学上不同于其他先前表征的CDC，如S。螨衍生的人血小板聚集因子（Sm-hPAF）/凝集素和螨溶血素。由于该CDC具有额外的N-末端结构域，包括盘状蛋白基序，因此被称为盘状蛋白溶素（DLY）。除了人细胞的优先裂解，DLY显示N-末端结构域依赖性促进人红细胞聚集和人细胞之间的细胞间缔合。DLY作为溶血素/溶细胞素和红细胞聚集/细胞间缔合分子起作用。这种双功能DLY可能是S.缓解。
Some strains of Streptococcus mitis exhibit β-hemolysis due to the β-hemolytic activity of cholesterol-dependent cytolysin (CDC). Recently, a gene encoding an atypical lectinolysin-related CDC was found in S. mitis strain Nm-76. However, the product of this gene remains uncharacterized. We aimed to characterize this atypical CDC and its molecular functions and contribution to the pathogenicity of S. mitis strain Nm-76. Phylogenetic analysis of the CDC gene was conducted based on the web-deposited information. The molecular characteristics of CDC were investigated using a gene-deletion mutant strain and recombinant proteins expressed in Escherichia coli. The gene encoding CDC found in Nm-76 and its homolog are distributed among many S. mitis strains. This CDC is phylogenetically different from other previously characterized CDCs, such as S. mitis-derived human platelet aggregation factor (Sm-hPAF)/lectinolysin and mitilysin. Because this CDC possesses an additional N-terminal domain, including a discoidin motif, it was termed discoidinolysin (DLY). In addition to the preferential lysis of human cells, DLY displayed N-terminal domain-dependent facilitation of human erythrocyte aggregation and intercellular associations between human cells. DLY functions as a hemolysin/cytolysin and erythrocyte aggregation/intercellular association molecule. This dual-function DLY could be an additional virulence factor in S. mitis.
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