Gebbink Martijn F B G, Claessen Dennis, Bouma Barend, Dijkhuizen Lubbert, Wösten Han A B
Department of Haematology, Thrombosis and Haemostasis Laboratory, Institute of Biomembranes, University Medical Center Utrecht, Heidelberglaan 100, 3584 CX Utrecht, The Netherlands.
Nat Rev Microbiol. 2005 Apr;3(4):333-41. doi: 10.1038/nrmicro1127.
Amyloids are filamentous protein structures approximately 10 nm wide and 0.1-10 mum long that share a structural motif, the cross-beta structure. These fibrils are usually associated with degenerative diseases in mammals. However, recent research has shown that these proteins are also expressed on bacterial and fungal cell surfaces. Microbial amyloids are important in mediating mechanical invasion of abiotic and biotic substrates. In animal hosts, evidence indicates that these protein structures also contribute to colonization by activating host proteases that are involved in haemostasis, inflammation and remodelling of the extracellular matrix. Activation of proteases by amyloids is also implicated in modulating blood coagulation, resulting in potentially life-threatening complications.
淀粉样蛋白是丝状蛋白质结构,宽度约为10纳米,长度为0.1 - 10微米,具有一种共同的结构基序——交叉β结构。这些纤维通常与哺乳动物的退行性疾病有关。然而,最近的研究表明,这些蛋白质也在细菌和真菌细胞表面表达。微生物淀粉样蛋白在介导对非生物和生物底物的机械侵袭中很重要。在动物宿主中,有证据表明这些蛋白质结构还通过激活参与止血、炎症和细胞外基质重塑的宿主蛋白酶来促进定殖。淀粉样蛋白对蛋白酶的激活也与调节血液凝固有关,从而导致潜在的危及生命的并发症。