Role of novel choline binding proteins in virulence of Streptococcus pneumoniae
Role of novel choline binding proteins in virulence of Streptococcus pneumoniae
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DOI：
10.1128/iai.68.10.5690-5695.2000
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发表时间：
2000-10-01
影响因子：
3.1
通讯作者：
Masure, HR
中科院分区：
文献类型：
--
作者：
Gosink, KK;Mann, ER;Masure, HR
胆碱结合蛋白 (CBP) 是一类表面蛋白，通过保守的胆碱结合域非共价结合到肺炎链球菌细胞壁的磷酸胆碱部分。该家族的六个新成员被鉴定出来，并且这六个成员加上最近描述的两个细胞壁水解酶 LytB 和 LytC，对其毒力中的作用进行了表征。构建了 CBP 缺陷突变体，并测试其对真核细胞的粘附、大鼠鼻咽部的定植以及引起脓毒症的能力。五个 CBP 突变体（CbpD、CbpE、CbpG、LytB 和 LytC）显示出鼻咽定植显着减少。对于 CbpE 和 -G，这是由于粘附人类细胞的能力下降。 CbpG，一种推定的丝氨酸蛋白酶，也在脓毒症中发挥作用，这是首次观察到肺炎球菌毒力决定因子对粘膜表面和血流均具有强烈作用。
The choline binding proteins (CBPs) are a family of surface proteins noncovalently bound to the phosphorylcholine moiety of the cell wall of Streptococcus pneumoniae by a conserved choline binding domain. Six new members of this family were identified, and these six plus two recently described cell wall hydrolases, LytB and LytC, were characterized for their roles in virulence. CBP-deficient mutants were constructed and tested for adherence to eukaryotic cells, colonization of the rat nasopharynx, and ability to cause sepsis, Five CBP mutants, CbpD, CbpE, CbpG, LytB, and LytC, showed significantly reduced colonization of the nasopharynx. For CbpE and -G this was attributable to a decreased ability to adhere to human cells. CbpG, a putative serine protease, also played a role in sepsis, the first observation of a pneumococcal virulence determinant strongly operative both on the mucosal surface and in the bloodstream.