The cell surface proteome of Entamoeba histolytica.

The cell surface proteome of Entamoeba histolytica.
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DOI:
10.1074/mcp.m113.031393
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发表时间:
2014-01
期刊:
Molecular & cellular proteomics : MCP
影响因子:
--
通讯作者:
Bruchhaus I
Bruchhaus I
中科院分区:
其他
文献类型:
--
作者:
Biller L;Matthiesen J;Kühne V;Lotter H;Handal G;Nozaki T;Saito-Nakano Y;Schümann M;Roeder T;Tannich E;Krause E;Bruchhaus I

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表面分子对于宿主-寄生虫相互作用是非常重要的。在溶组织内阿米巴感染期间,这些相互作用被预测为对于组织侵入、诱导结肠炎和肝脓肿形成至关重要。然而,到目前为止,人们对参与这些过程的分子知之甚少,只有大约20种蛋白质或蛋白质家族在E.溶组织表面。因此,我们分析了E.溶组织剂使用细胞表面生物素化和质谱,693推定的表面相关蛋白被确定。计算机模拟分析预测,这些蛋白质中约有26%是膜相关的,因为它们含有跨膜结构域和/或信号序列,以及棕榈酰化、肉豆蔻酰化或异戊二烯化位点。另外25%的鉴定蛋白可能代表非经典分泌蛋白。令人惊讶的是,没有膜结合位点可以预测其余49%的蛋白质。为了验证表面定位,随机选择23种蛋白质并通过免疫荧光显微镜进行分析。在这23种蛋白质中,20种(87%)表现出明确的表面定位。这些发现表明,更多的E。溶组织蛋白比以前认为的是表面相关的,这种现象可能是基于E.溶组织剂
Surface molecules are of major importance for host-parasite interactions. During Entamoeba histolytica infections, these interactions are predicted to be of prime importance for tissue invasion, induction of colitis and liver abscess formation. To date, however, little is known about the molecules involved in these processes, with only about 20 proteins or protein families found exposed on the E. histolytica surface. We have therefore analyzed the complete surface proteome of E. histolytica. Using cell surface biotinylation and mass spectrometry, 693 putative surface-associated proteins were identified. In silico analysis predicted that ∼26% of these proteins are membrane-associated, as they contain transmembrane domains and/or signal sequences, as well as sites of palmitoylation, myristoylation, or prenylation. An additional 25% of the identified proteins likely represent nonclassical secreted proteins. Surprisingly, no membrane-association sites could be predicted for the remaining 49% of the identified proteins. To verify surface localization, 23 proteins were randomly selected and analyzed by immunofluorescence microscopy. Of these 23 proteins, 20 (87%) showed definite surface localization. These findings indicate that a far greater number of E. histolytica proteins than previously supposed are surface-associated, a phenomenon that may be based on the high membrane turnover of E. histolytica.