Structural analysis and anthelmintic of Canavalia brasiliensis lectin reveal molecular correlation between the carbohydrate recongnition domain and glycans of Haemonchus contortus

被引：14

作者：

Batista, Karla L. R. ^{[1
]}

Silva, Carolina R. ^{[2
]}

Santos, Valdenice F. ^{[1
]}

Silva, Rafael C. ^{[1
]}

Roma, Renato R. ^{[1
]}

Santos, Ana L. E. ^{[1
]}

Pereira, Raquel O. ^{[1
]}

Delatorre, Plinio ^{[3
]}

Rocha, Bruno A. M. ^{[4
]}

Soares, Alexandra M. S. ^{[5
]}

Costa-Junior, Livio M. ^{[2
]}

Teixeira, Claudener S. ^{[1
]}

机构：

[1] Univ Fed Maranhao, Ctr Ciencias Agr & Ambientais, Chapadinha, Maranhao, Brazil

[2] Univ Fed Maranhao, Dept Patol, Sao Luis, Maranhao, Brazil

[3] Univ Fed Paraiba, Dept Biol Mol, Joao Pessoa, Paraiba, Brazil

[4] Univ Fed Ceara, Dept Bioquim & Biol Mol, Fortaleza, Ceara, Brazil

[5] Univ Fed Maranhao, Curso Engn Quim, Sao Luis, Maranhao, Brazil

来源：

MOLECULAR AND BIOCHEMICAL PARASITOLOGY | 2018年 / 225卷

关键词：

ConBr; Molecular docking; Core trimannoside; Parasite; Anthelmintic activity; CRYSTAL-STRUCTURE; PLANT-EXTRACTS; BINDING LECTIN; RESISTANCE; NEMATODES; PROTEINS; LESSONS;

D O I：

10.1016/j.molbiopara.2018.09.002

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Haemonchus contortus is one of the most economically important parasites infecting small ruminants worldwide. This nematode has shown a great ability to develop resistance to anthelmintic drugs, calling for the development of alternative control approaches. Because lectins recognize and bind to specific carbohydrates and glycan structures present in parasites, they can be considered as an alternative to develop new antiparasitic drugs. Accordingly, this work aimed to investigate the anthelmintic effect of Canavalia brasiliensis (ConBr) lectin against H. contortus and to evaluate a possible interaction of ConBr with glycans of this parasite by molecular docking. ConBr showed significant inhibition of H. contortus larval development with an IC50 of 0.26 mg mL(-1). Molecular docking assays revealed that glycans containing the core trimannoside [Man(alpha 1-3)Man(alpha 1-6)Man] of H. contortus interact in the carbohydrate recognition domain of ConBr with an interaction value of MDS = -248.77. Our findings suggest that the inhibition of H. contortus larval development is directly related to the recognition of the core trimannoside present in the glycans of these parasites. This work is the first to report on the structure-function relationships of the anthelmintic activity of plant lectins.

引用

页码：67 / 72

页数：6

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