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Hemoglobin of the bloody clam Tegillarca granosa (Tg-HbI) is involved in the immune response against bacterial infection

机译:血红蛤Tegillarca granosa(Tg-HbI)的血红蛋白参与针对细菌感染的免疫反应

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Hemoglobins (Hb) are the major protein components of erythrocytes circulating in the red blood, but can serve additional functions besides the transport of oxygen. Here, the cDNA of the bloody clam (Tegillarca granosa) Hb dimer (designated Tg-HbI) was cloned and was found to be 748 bp in length, consisting of an open reading frame of 441 bp encoding a polypeptide of 147 amino acids. The deduced amino acid sequence of Tg-HbI shared 81.6% similarity with HbI from two species of the genus Scapharca and 46-51% similarity with the Hb proteins from other mollusks. The 3D structure of bloody clam TgHbI was predicted by the SWISS-MODEL Protein Modelling Server and compared with that of Scapharca kagoshimensis. The mRNA transcript of Tg-HbI was detected in all of the clam cells/tissues examined, including haemocytes, the adductor muscle, foot, hepatopancreas, gill and mantle. The mRNA expression of Tg-HbI was significantly up-regulated after Vibrio parahaemolyticus, lipopolysaccharide and peptidoglycan challenge, indicating that Tg-HbI was involved in the immune defence responses against bacterial infection and exposure to bacterial pathogenic factors. As the first functional research on the Hb protein in bloody clam, our findings provide new insight into the innate immune defence mechanisms of T granosa and other mollusks
机译:血红蛋白(Hb)是红血球中循环的红细胞的主要蛋白质成分,但除氧的运输外,还可以起到其他功能。在这里,克隆了血蛤(Tegillarca granosa)Hb二聚体(命名为Tg-HbI)的cDNA,发现其长748 bp,由441 bp的开放阅读框组成,编码147个氨基酸。推导的Tg-HbI氨基酸序列与两种Scapharca属的HbI具有81.6%的相似性,与其他软体动物的Hb蛋白具有46-51%的相似性。 SWISS-MODEL蛋白质建模服务器预测了血蛤TgHbI的3D结构,并将其与Scapharca kagoshimensis的3D结构进行了比较。在所有检查的蛤细胞/组织中都检测到了Tg-HbI的mRNA转录本,包括血细胞,内收肌,足,肝胰腺,g和地幔。副溶血性弧菌,脂多糖和肽聚糖攻击后,Tg-HbI的mRNA表达显着上调,表明Tg-HbI参与了针对细菌感染和暴露于细菌致病因素的免疫防御反应。作为对血蛤中Hb蛋白的第一个功能研究,我们的发现为T颗粒和其他软体动物的先天免疫防御机制提供了新的见识。

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