A Lectin fromDioclea violaceaInteracts with Midgut Surface ofLutzomyia migonei, Unlike Its Homologues,Cratylia floribundaLectin andCanavalia gladiataLectin

Author:

Monteiro Tínel Juliana Montezuma Barbosa1,Benevides Melina Fechine Costa1,Frutuoso Mércia Sindeaux1,Rocha Camila Farias1,Arruda Francisco Vassiliepe Sousa2,Vasconcelos Mayron Alves2,Pereira-Junior Francisco Nascimento3,Cajazeiras João Batista3,do Nascimento Kyria Santiago3,Martins Jorge Luiz4,Teixeira Edson Holanda2,Cavada Benildo Sousa3,dos Santos Ricardo Pires5,Lima Pompeu Margarida Maria1

Affiliation:

1. Laboratory of Parasitology, Faculty of Medicine, Federal University of Ceará, 60430-160 Fortaleza, CE, Brazil

2. Integrated Laboratory of Biomolecules (LIBS), Department of Pathology and Legal Medicine, Faculty of Medicine, Federal University of Ceará, 60430-160 Fortaleza, CE, Brazil

3. Laboratory of Biologically Actives Molecules, Biochemistry and Molecular Biology Department, Federal University of Ceará, 60440-970 Fortaleza, CE, Brazil

4. Institute of Chemical and Geosciences, Federal University of Pelotas Institute of Chemical and Geosciences, Federal University of Pelotas, 96160-000 Pelotas, RS, Brazil

5. Computer Engineering of Sobral, Federal University of Ceará, 62042-280 Sobral, CE, Brazil

Abstract

Leishmaniasis is a vector-borne disease transmitted by phlebotomine sand fly. Susceptibility and refractoriness toLeishmaniadepend on the outcome of multiple interactions that take place within the sand fly gut. Promastigote attachment to sand fly midgut epithelium is essential to avoid being excreted together with the digested blood meal. Promastigote and gut sand fly surface glycans are important ligands in this attachment. The purpose of the present study was to evaluate the interaction of three lectins isolated from leguminous seeds (Diocleinae subtribe), D-glucose and D-mannose-binding, with glycans onLutzomyia migoneimidgut. To study this interaction the lectins were labeled with FITC and a fluorescence assay was performed. The results showed that onlyDioclea violacealectin (DVL) was able to interact with midgut glycans, unlikeCratylia floribundalectin (CFL) andCanavalia gladiatalectin (CGL). Furthermore, when DVL was blocked with D-mannose the interaction was inhibited. Differences of spatial arrangement of residues and volume of carbohydrate recognition domain (CRD) may be the cause of the fine specificity of DVL for glycans in the surface onLu. migoneimidgut. The findings in this study showed the presence of glycans in the midgut with glucose/mannose residues in its composition and these residues may be important in interaction betweenLu. migoneimidgut andLeishmania.

Funder

Conselho Nacional de Desenvolvimento Científico e Tecnológico

Publisher

Hindawi Limited

Subject

General Environmental Science,General Biochemistry, Genetics and Molecular Biology,General Medicine

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