The Bfp60 surface adhesin is an extracellular matrix and plasminogen protein interacting in Bacteroides fragilis.
The Bfp60 surface adhesin is an extracellular matrix and plasminogen protein interacting in Bacteroides fragilis.
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DOI：
10.1016/j.ijmm.2013.06.007
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发表时间：
2013-12
期刊：
影响因子：
--
通讯作者：
Domingues RM
中科院分区：
文献类型：
--
作者：
Ferreira Ede O;Teixeira FL;Cordeiro F;Araujo Lobo L;Rocha ER;Smith JC;Domingues RM
纤溶酶原（Plg）是在血液的血浆组分中发现的高度丰富的蛋白质，并且是纤维蛋白、胶原蛋白和组织的其它结构组分的降解所必需的。这种纤维蛋白溶解系统被几种病原性细菌利用，以操纵宿主纤溶酶原系统，并通过在感染期间通过在其表面结合Plg来改变该过程的活化而促进组织的侵入。脆弱拟杆菌是临床上最常见的革兰氏阴性专性厌氧菌，如腹腔积液和厌氧菌血症。B的能力。fragilis将纤溶酶原（Plg）转化为纤溶酶的作用与一种名为Bfp 60的外膜蛋白有关。在本研究中，我们研究了Bfp 60蛋白在B细胞中的功能。通过构建bfp 60缺陷型菌株，并将其与野生型的关于与层粘连蛋白-1（LMN-1）的结合和Plg活化为纤溶酶的比较，来鉴定脆弱型638 R。虽然本研究的结果表明Bfp 60表面蛋白在B. fragilis对于LMN-1的识别和Plg的激活是重要的，在突变株中观察到Plg向纤溶酶的显著缓慢激活。因此，在B中也存在另一种未鉴定的机制激活Plg的可能性。fragilis不能被丢弃。结果表明，Bfp 60蛋白是负责识别层粘连蛋白和Plg-纤溶酶激活。尽管这种蛋白在该物种致病性中的重要性尚不清楚，但人们接受的是，由于其他病原菌在感染期间使用这种机制通过细胞外基质传播，因此它也应该有助于B的毒力。脆弱的。
Plasminogen (Plg) is a highly abundant protein found in the plasma component of blood and is necessary for the degradation of fibrin, collagen, and other structural components of tissues. This fibrinolytic system is utilized by several pathogenic species of bacteria to manipulate the host plasminogen system and facilitate invasion of tissues during infection by modifying the activation of this process through the binding of Plg at their surface. Bacteroides fragilis is the most commonly isolated Gram-negative obligate anaerobe from human clinical infections, such as intra-abdominal abscesses and anaerobic bacteraemia. The ability of B. fragilis to convert plasminogen (Plg) into plasmin has been associated with an outer membrane protein named Bfp60. In this study, we characterized the function of Bfp60 protein in B. fragilis 638R by constructing the bfp60 defective strain and comparing its with that of the wild type regarding binding to laminin-1 (LMN-1) and activation of Plg into plasmin. Although the results showed in this study indicate that Bfp60 surface protein of B. fragilis is important for the recognition of LMN-1 and Plg activation, a significant slow activation of Plg into plasmin was observed in the mutant strain. For that reason, the possibility of another unidentified mechanism activating Plg is also present in B. fragilis can not be discarded. The results demonstrate that Bfp60 protein is responsible for the recognition of laminin and Plg-plasmin activation. Although the importance of this protein is still unclear in the pathogenicity of the species, it is accepted that since other pathogenic bacteria use this mechanism to disseminate through the extracellular matrix during the infection, it should also contribute to the virulence of B. fragilis.
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影响因子：
3.1
作者：
Grab, DJ;Perides, G;Kim, KS
通讯作者：
Kim, KS
影响因子：
3.1
作者：
HU, LT;PERIDES, G;KLEMPNER, MS
通讯作者：
KLEMPNER, MS
DOI：
10.1073/pnas.0307329101
发表时间：
2004-02-17
影响因子：
11.1
作者：
Jönsson, K;Guo, BP;Kronvall, G
通讯作者：
Kronvall, G
影响因子：
64.5
作者：
Coleman, JL;Gebbia, JA;Benach, JL
通讯作者：
Benach, JL
影响因子：
11.8
作者：
Finegold, SM;Wexler, HM
通讯作者：
Wexler, HM