Identification and characterization of a fibronectin-binding protein from Granulicatella adiacens
Identification and characterization of a fibronectin-binding protein from Granulicatella adiacens
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来自 Granulicatelladiacens 的纤连蛋白结合蛋白的鉴定和表征
DOI：
10.1111/j.2041-1014.2011.00623.x
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发表时间：
2011
影响因子：
3.7
通讯作者：
Takahiko Oho
中科院分区：
文献类型：
--
作者：
Taihei Yamaguchi;Sakiko Soutome;Takahiko Oho
微生物与纤维连接蛋白的相互作用在感染性心内膜炎中起着重要的作用。颗粒状球菌（Granulicatella adiacensis）是口腔微生物群中的一员，以前被称为营养变异链球菌，并且经常从心内膜炎患者中分离。在本研究中，我们确定了一个表面蛋白，命名为Cha，它结合到纤连蛋白，通过噬斑杂交程序使用shA序列作为探针，它编码一个纤连蛋白结合分子的戈登链球菌DL 1。该序列与cshA高度同源，编码2351个氨基酸残基。该蛋白质在N-末端半区中包含独特序列。C末端区域包含9个完整的和1个不完整的115个氨基酸残基重复区。在8株营养变异链球菌中，3株G. adiacens和1株Abiotrophia defectiva携带该基因。异源表达的研究表明，Cha坚持固定化纤连蛋白，这一功能是位于独特的区域。重组Cha蛋白也能粘附到纤维连接蛋白上，并以剂量依赖性方式部分抑制G. adiacens对纤维连接蛋白的粘附。这些结果表明Cha是一种细胞表面蛋白，它介导了黄曲霉与纤连蛋白的粘附。
The interaction of microorganisms with fibronectin plays an important role in infective endocarditis.Granulicatella adiacensis a member of the oral microbiota, formerly known as nutritionally variant streptococci, and is often isolated from endocarditis patients. In the present study we identified a surface protein, designated Cha, which binds to fibronectin, by a plaque hybridization procedure using thecshAsequence as probe, which encodes a fibronectin‐binding molecule ofStreptococcus gordoniiDL1. Thechasequence was highly homologous tocshAand encoded a product of 2351 amino acid residues. The protein comprised a unique sequence in the N‐terminal half region. The C‐terminal region contained nine complete, and one incomplete, 115‐amino acid residue repeat blocks. Among eight strains of nutritionally variant streptococci, threeG. adiacensstrains and oneAbiotrophia defectivastrain carried thechagene. Heterologous expression studies suggested that Cha adhered to immobilized fibronectin, and that this function was located in the unique region. Recombinant Cha protein also adhered to immobilize fibronectin and partially inhibited adherence ofG. adiacensto fibronectin in a dose‐dependent manner. These results suggest that Cha is a cell surface protein that mediates adherence ofG. adiacensto fibronectin.