Institute of Preventive Veterinary Medicine and Zhejiang Provincial Key Laboratory of Preventive Veterinary Medicine, Zhejiang University, Hangzhou 310058, PR China.
J Microbiol. 2012 Dec;50(6):994-1002. doi: 10.1007/s12275-012-2035-3. Epub 2012 Dec 30.
Catabolite control protein A (CcpA) is the major transcriptional regulator in carbon catabolite repression in several Gram-positive bacteria. We attempted to characterize the role of a CcpA homologue of Streptococcus suis type 2 in sugar metabolism and virulence. Addition of glucose or sucrose to the defined medium significantly reduced the activity of raffinose-inducible α-galactosidase, cellobiose-inducible β-glucosidase, and maltose-inducible α-glucosidase of the wild-type strain by about 9, 4, and 2-3 fold, respectively. Deletion of ccpA substantially derepressed the effects of repressing sugars on α-galactosidase or β-glucosidase activity. The ccpA deletion mutant showed reduced expression of virulence genes sly and eno (P<0.05), decreased adhesion to and invasion into endothelial cells (P<0.05), and attenuated virulence to mice with significant reduction of death rate and bacterial burden in organs, as compared to the wild-type strain. Both the in vitro and in vivo defect phenotypes were reversible by ccpA complementation. Thus, this study shows that CcpA of S. suis type 2 plays an important role in carbon catabolite repression and virulence.
标题:猪链球菌 2 型 CcpA 同源物在碳源分解代谢物阻遏和毒力中的作用
摘要:目的:研究猪链球菌 2 型 CcpA 同源物(CcpA)在碳源分解代谢物阻遏和毒力中的作用。方法:采用基因缺失突变的方法构建 CcpA 缺失突变株,分析突变株在不同碳源条件下的酶活性、黏附和侵袭能力以及对小鼠的致病性。结果:CcpA 缺失突变株在含有葡萄糖或蔗糖的培养基中,α-半乳糖苷酶、β-葡萄糖苷酶和α-葡萄糖苷酶的活性分别比野生型菌株降低了约 9、4 和 2-3 倍。与野生型菌株相比,CcpA 缺失突变株的 sly 和 eno 基因表达水平降低(P<0.05),对内皮细胞的黏附和侵袭能力降低(P<0.05),对小鼠的毒力降低,死亡率和各器官中的细菌载量显著降低。CcpA 互补后,突变株的表型缺陷得到了部分或完全恢复。结论:CcpA 参与了碳源分解代谢物阻遏和猪链球菌 2 型的毒力调控。