A new C-type lectin (FcLec5) from the Chinese white shrimp Fenneropenaeus chinensis
A new C-type lectin (FcLec5) from the Chinese white shrimp Fenneropenaeus chinensis
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来自中国明对虾的新型 C 型凝集素 (FcLec5)
DOI：
10.1007/s00726-010-0558-7
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发表时间：
2010-03
期刊：
影响因子：
3.5
通讯作者：
Zhang, Xiao-Wen
中科院分区：
文献类型：
--
作者：
Xu, wen-Teng;Wang, Xian-Wei;Wang, Jin-Xing;Yu, Xiao-Qiang;Zhao, Xiao-Fan;Zhang, Xiao-Wen
C 型凝集素是模式识别受体 (PRR) 家族之一，在先天免疫中发挥重要作用。在这项工作中，从中国明对虾中获得了一种新的 C 型凝集素 (FcLec5) 的 cDNA 和基因组序列。 FcLec5 cDNA包含1,008 bp的开放阅读框，其基因组序列为1,137 bp，具有4个外显子和3个内含子。预测的 FcLec5 蛋白包含一个信号肽和两个碳水化合物识别域 (CRD)。 FcLec5的N端CRD具有预测的碳水化合物识别基序Gln-Pro-Asp (QPD)，而C端CRD包含Glu-Pro-Gln (EPQ)基序。 Northern blot分析显示FcLec5 mRNA在肝胰腺中特异性表达。 FcLec5蛋白在肝胰腺中表达并分泌到血淋巴中。实时PCR显示FcLec5转录本在受到鳗弧菌或白斑综合症病毒(WSSV)免疫攻击后表现出不同的表达谱。重组FcLec5及其两个单独的CRD可以凝集大多数测试的细菌，并且凝集活性是Ca2+依赖性的。此外，对革兰氏阴性菌的凝集活性高于对革兰氏阳性菌的凝集活性。直接结合测定表明，重组 FcLec5 可以以不依赖 Ca2+ 的方式与所有测试的微生物（五种革兰氏阳性细菌和四种革兰氏阴性细菌以及酵母）结合。重组 FcLec5 还直接与细菌肽聚糖、脂多糖和脂磷壁酸结合。这些结果表明，FcLec5 可能通过与中国白虾细菌细胞壁多糖结合而充当细菌的 PRR。
C-type lectins are one family of pattern recognition receptors (PRRs) that play important roles in innate immunity. In this work, cDNA and genomic sequences for a new C-type lectin (FcLec5) were obtained from the Chinese white shrimp Fenneropenaeus chinensis. FcLec5 cDNA contains an open reading frame of 1,008 bp and its genomic sequence is 1,137 bp with 4 exons and 3 introns. The predicted FcLec5 protein contains a signal peptide and two carbohydrate recognition domains (CRDs). The N-terminal CRD of FcLec5 has a predicted carbohydrate recognition motif of Gln-Pro-Asp (QPD), while the C-terminal CRD contains a motif of Glu-Pro-Gln (EPQ). Northern blot analysis showed that FcLec5 mRNA was specifically expressed in hepatopancreas. FcLec5 protein was expressed in hepatopancreas and secreted into hemolymph. Real-time PCR showed that FcLec5 transcript exhibited different expression profiles after immune-challenged with Vibrio anguillarum or White Spot Syndrome Virus (WSSV). Recombinant FcLec5 and its two individual CRDs could agglutinate most bacteria tested, and the agglutinating activity was Ca2+-dependent. Besides, the agglutinating activity to gram-negative bacteria is higher than that to gram-positive bacteria. Direct binding assay showed that recombinant FcLec5 could bind to all microorganisms tested (five gram-positive and four gram-negative bacteria, as well as yeast) in a Ca2+-independent manner. Recombinant FcLec5 also directly bound to bacterial peptidoglycan, lipopolysaccharide and lipoteichoic acids. These results suggest that FcLec5 may act as a PRR for bacteria via binding to bacterial cell wall polysaccharides in Chinese white shrimp.
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