Staphylococcus aureus extracellular adherence protein serves as anti-inflammatory factor by inhibiting the recruitment of host leukocytes
Staphylococcus aureus extracellular adherence protein serves as anti-inflammatory factor by inhibiting the recruitment of host leukocytes
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DOI：
10.1038/nm728
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发表时间：
2002-07-01
期刊：
影响因子：
82.9
通讯作者：
Preissner, KT
中科院分区：
文献类型：
--
作者：
Chavakis, T;Hussain, M;Preissner, KT
金黄色葡萄球菌是一种人类病原体，它分泌有助于细菌定植的蛋白质。在这里，我们描述了细胞外黏附蛋白(EAP)作为一种新的抗炎因子，抑制宿主白细胞募集。由于其与宿主黏附蛋白细胞间黏附分子-1(ICAM-1)、纤维蛋白原或玻璃体连结蛋白的直接相互作用，EAP在体外阻断了β(2)整合素和尿激酶受体介导的白细胞黏附。尽管表达EAP的金黄色葡萄球菌在小鼠细菌性腹膜炎中诱导的中性粒细胞募集比EAP阴性株低2-3倍，但分离的EAP在急性硫代乙酸酯诱导的腹膜炎小鼠模型中阻止了β(2)整合素依赖的中性粒细胞募集。因此，与ICAM-1和细胞外基质蛋白的特异性相互作用使EAP成为一种有效的抗炎因子，可能成为一种新的治疗物质来阻止高炎性病理患者的白细胞外渗。
Staphylococcus aureus is a human pathogen that secretes proteins that contribute to bacterial colonization. Here we describe the extracellular adherence protein (Eap) as a novel anti-inflammatory factor that inhibits host leukocyte recruitment. Due to its direct interactions with the host adhesive proteins intercellular adhesion molecule 1 (ICAM-1), fibrinogen or vitronectin, Eap disrupted beta(2)-integrin and urokinase receptor-mediated leukocyte adhesion in vitro. Whereas Eap-expressing S. aureus induced a 2-3-fold lower neutrophil recruitment in bacterial peritonitis in mice as compared with an Eap-negative strain, isolated Eap prevented beta(2)-integrin-dependent neutrophil recruitment in a mouse model of acute thioglycollate-induced peritonitis. Thus, the specific interactions with ICAM-1 and extracellular matrix proteins render Eap a potent anti-inflammatory factor, which may serve as a new therapeutic substance to block leukocyte extravasation in patients with hyperinflammatory pathologies.