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首页> 外文期刊>Infection and immunity >Identification and Characterization of Cryptosporidium parvum Clec, a Novel C-Type Lectin Domain-Containing Mucin-Like Glycoprotein
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Identification and Characterization of Cryptosporidium parvum Clec, a Novel C-Type Lectin Domain-Containing Mucin-Like Glycoprotein

机译：小隐隐孢子虫Clec，一种新型的C型凝集素域含粘蛋白样糖蛋白的鉴定与表征。

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Cryptosporidium species are waterborne apicomplexan parasites that cause diarrheal disease worldwide. Although the mechanisms underlying Cryptosporidium-host cell interactions are not well understood, mucin-like glycoproteins of the parasite are known to mediate attachment and invasion in vitro. We identified C. parvum Clec (CpClec), a novel mucin-like glycoprotein that contains a C-type lectin domain (CTLD) and has orthologs in C. hominis and C. muris. CTLD-containing proteins are ligand-binding proteins that function in adhesion and signaling and are present in a wide range of organisms, from humans to viruses. However, this is the first report of a CTLD-containing protein in protozoa and in Apicomplexa. CpClec is predicted to be a type 1 membrane protein, with a CTLD, an O-glycosylated mucin-like domain, a transmembrane domain, and a cytoplasmic tail containing a YXX? sorting motif. The predicted structure of CpClec displays several characteristics of canonical CTLD-containing proteins, including a long loop region hydrophobic core associated with calcium-dependent glycan binding as well as predicted calcium- and glycan-binding sites. CpClec expression during C. parvum infection in vitro is maximal at 48 h postinfection, suggesting that it is developmentally regulated. The 120-kDa mass of native CpClec is greater than predicted, most likely due to O-glycosylation. CpClec is localized to the surface of the apical region and to dense granules of sporozoites and merozoites. Taken together, these findings, along with the known functions of C. parvum mucin-like glycoproteins and of CTLD-containing proteins, strongly implicate a significant role for CpClec in Cryptosporidium-host cell interactions.
机译：隐孢子虫种类是水传播的apicomplexan寄生虫，可导致全世界的腹泻病。尽管对隐孢子虫-宿主细胞相互作用的潜在机制尚不清楚，但已知该寄生虫的粘蛋白样糖蛋白可介导体外的附着和侵袭。我们确定了小球藻Clec（ Cp Clec），一种新型的粘蛋白样糖蛋白，包含一个C型凝集素结构域（CTLD），并在人形衣原体和鼠毛衣原体中具有直系同源物。含有CTLD的蛋白质是配体结合蛋白质，在黏附和信号传导中起作用，存在于从人类到病毒的各种生物中。但是，这是原生动物和蜂复合体中含有CTLD的蛋白质的首次报道。预计CpClec是一种1型膜蛋白，具有CTLD，O-糖基化粘蛋白样结构域，跨膜结构域和含有YXX？的胞质尾巴。排序主题。 Cp Clec的预测结构显示出包含CTLD的蛋白质的几个特征，包括与钙依赖性聚糖结合相关的长环区域疏水核以及预测的钙和聚糖结合位点。感染小球藻后 的 Cp Clec表达在感染后48 h达到最大值，表明它在发育上受到调节。天然 Cp Clec的120 kDa质量大于预期，最可能是由于O-糖基化。 Cp Clec定位于根尖区域的表面以及子孢子和裂殖子的致密颗粒。综上所述，这些发现以及小球藻粘蛋白样糖蛋白和含有CTLD的蛋白的已知功能，强烈暗示了 Cp Clec在隐孢子虫-宿主细胞相互作用中的重要作用。

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