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Structural characterization of a galectin isolated from the marine sponge Chondrilla caribensis with leishmanicidal potential
Biochimica et Biophysica Acta (BBA) - General Subjects ( IF 2.8 ) Pub Date : 2021-09-08 , DOI: 10.1016/j.bbagen.2021.129992
Andressa Rocha de Oliveira Sousa 1 , Francisco Regivânio Nascimento Andrade 1 , Renata Pinheiro Chaves 1 , Bruno Lopes de Sousa 2 , Dimas Batista de Lima 3 , Racquel Oliveira da Silva Souza 3 , Cláudio Gleidiston Lima da Silva 3 , Claudener Souza Teixeira 4 , Alexandre Holanda Sampaio 1 , Celso Shiniti Nagano 1 , Rômulo Farias Carneiro 1
Affiliation  

Background

Solving primary structure of lectins leads to an understanding of the physiological roles within an organism and its biotechnological potential. Only eight sponge lectins have had their primary structure fully determined.

Methods

The primary structure of CCL, Chondrilla caribensis lectin, was determined by tandem mass spectrometry. The three-dimensional structure was predicted and the protein-carbohydrate interaction analysed by molecular docking. Furthermore, the anti-leishmanial activity was observed by assays with Leishmania infantum.

Results

The amino acid sequence consists of 142 amino acids with a calculated molecular mass of 15,443 Da. The lectin has a galectin-like domain architecture. As observed in other sponge galectins, the signature sequence of a highly conserved domain was also identified in CCL with some modifications. CCL exhibits a typical galectin structure consisting of a β-sandwich. Molecular docking showed that the amino acids interacting with CCL ligands at the monosaccharide binding site are mostly the same as those conserved in this family of lectins. Through its interaction with L. infantum glycans, CCL was able to inhibit the development of this parasite. CCL also induced apoptosis after eliciting ROS production and altering the membrane integrity of Leishmania infantum promastigote.

Conclusions

CCL joins the restricted group of sponge lectins with determined primary structure and very high biotechnological potential owing to its promising results against pathogens that cause Leishmaniasis.

General significance

As the determination of primary structure is important for biological studies, now CCL can become a sponge galectin with an exciting future in the field of human health.



中文翻译:


从具有杀利什曼病潜力的海洋海绵Chondrilla caribensis中分离出的半乳糖凝集素的结构表征


 背景


解决凝集素的一级结构有助于了解生物体的生理作用及其生物技术潜力。只有八种海绵凝集素的一级结构被完全确定。

 方法


通过串联质谱法测定了 CCL( Chondrilla caribensis凝集素)的一级结构。通过分子对接预测三维结构并分析蛋白质-碳水化合物相互作用。此外,通过婴儿利什曼原虫测定观察到抗利什曼原虫活性。

 结果


氨基酸序列由 142 个氨基酸组成,计算分子量为 15,443 Da。凝集素具有类似半乳糖凝集素的结构域结构。正如在其他海绵半乳糖凝集素中观察到的那样,在 CCL 中也鉴定出了高度保守结构域的特征序列,并进行了一些修改。 CCL具有典型的半乳糖素结构,由β-三明治组成。分子对接表明,在单糖结合位点与CCL配体相互作用的氨基酸与该凝集素家族中保守的氨基酸大部分相同。通过与婴儿乳杆菌聚糖的相互作用,CCL 能够抑制这种寄生虫的发育。 CCL 还可在引发 ROS 产生并改变婴儿利什曼原虫前鞭毛体膜完整性后诱导细胞凋亡。

 结论


CCL 加入了海绵凝集素这一受限类别,具有确定的一级结构和非常高的生物技术潜力,因为它对引起利什曼病的病原体具有良好的效果。

 一般意义


由于一级结构的测定对于生物学研究非常重要,现在CCL可以成为海绵半乳糖凝集素,在人类健康领域具有令人兴奋的前景。

更新日期:2021-09-12
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