Haemophilus influenzae surface fibrils contribute to serum resistance by interacting with vitronectin
Haemophilus influenzae surface fibrils contribute to serum resistance by interacting with vitronectin
复制标题
DOI：
10.4049/jimmunol.177.1.430
复制
发表时间：
2006-07-01
影响因子：
4.4
通讯作者：
Riesbeck, Kristian
中科院分区：
文献类型：
--
作者：
Hallstrom, Teresia;Trajkovska, Elena;Riesbeck, Kristian
玻连蛋白抑制补体系统的膜攻击复合物，并在血浆和细胞外基质中发现。在这项研究中，我们已经确定了外膜蛋白嗜血杆菌表面纤维（Hsf）的主要玻连蛋白结合蛋白在封装的H。流感病毒B型。A H.与野生型对应物相比，缺乏Hsf的流感病毒突变体显示出与可溶性和固定化玻连蛋白的结合显著降低。此外，大肠杆菌表达HSF在表面强烈粘附固定玻连蛋白。重要的是，H.当与正常人血清孵育时，与野生型细菌相比，流感Hsf突变体的存活率显著降低。在E.杆菌玻连蛋白结合区位于两个独立的结合结构域内。总之，Hsf与玻连蛋白相互作用，从而抑制补体介导的杀菌活性，因此是主要的H。流感病毒毒力因子
Vitronectin inhibits the membrane attack complex of the complement system and is found both in plasma and the extracellular matrix. In this study, we have identified the outer membrane protein Haemophilus surface fibrils (Hsf) as the major vitronectin-binding protein in encapsulated H. influenzae type b. A H. influenzae mutant devoid of Hsf showed a significantly decreased binding to both soluble and immobilized vitronectin as compared with the wild-type counterpart. Moreover, Escherichia coli-expressing Hsf at the surface strongly adhered to immobilized vitronectin. Importantly, the H. influenzae Hsf mutant had a markedly reduced survival as compared with the wild-type bacterium when incubated with normal human serum. A series of truncated Hsf fragments were recombinantly manufactured in E. coli. The vitronectin binding regions were located within two separate binding domains. In conclusion, Hsf interacts with vitronectin and thereby inhibits the complement-mediated bactericidal activity, and thus is a major H. influenzae virulence factor.