Elucidation of the primary structure and molecular modeling of Parkia pendula lectin and in vitro evaluation of the leishmanicidal activity

• Published in: Process biochemistry (1991) Vol. 101; pp. 1 - 10
• Main Authors: Carneiro, Romulo F., Aguiar, Evelyn S., Santos, Valdenice F., Santos, Ana L.E., Santos, Maria H.C., Roma, Renato R., Silva, Romerio R.S., Leal, Maria L.M.B., Silva, Lívia T., Rocha, Bruno A.M., Silva, Cláudio G.L., Nagano, Celso S., Sampaio, Alexandre H., Souza, Racquel O.S., Teixeira, Claudener S.
• Format: Journal Article
• Language: English
• Published: Barking Elsevier Ltd 01.02.2021; Elsevier BV
• Subjects: Affinity chromatography; Amino acid sequence; Amino acids; Carbohydrates; Cell culture; Domains; Drug development; Lectin; Lectins; Leishmaniasis; Mass spectrometry; Molecular docking; Molecular modelling; Molecular structure; Polysaccharides; Promastigotes; Structure-function relationships; Three dimensional models; Lectin; Leishmaniasis; Mass spectrometry; Molecular docking
• ISSN: 1359-5113; 1873-3298
• DOI: 10.1016/j.procbio.2020.11.004

[Display omitted] •PpeL was purified on a mannose-agarose column.•PpeL structure is composed of three β-prism domains.•PpeL inhibits the development of Leishmania infantum promastigote.•The leishmanicidal effect of PpeL is via carbohydrate recognition domain. Structure-function study of plant lectins has received attention for elucidating possible mechanisms of lectins in cell models. Lectins have the ability to interact with target glycans and trigger responses able to inhibit the development of various pathogens. In this work, we report amino acid sequencing, prediction of the three-dimensional structure of P. pendula lectin (PpeL) and the effect of this lectin on inhibiting the development of Leishmania infantum promastigote. PpeL was purified on affinity chromatography and has haemagglutinating activity after exposure to temperatures up to 50 °C and at a pH corresponding to the range of 5.0 and 7.0. PpeL consists of 447 amino acids; the theoretical average molecular mass was 47,410 Da. The three-dimensional model of PpeL revealed that it consists of three β-prism domains tandemly arranged with each one presenting a different carbohydrate recognition domain (CRD). PpeL inhibited growth of L. infantum promastigotes (45.6 ± 1.92 %) within 48 h, an effect that occurred via the CRD, suggesting an interaction between PpeL and glycans from L. infantum. Our results confirm the leishmanicidal potential of PpeL, suggesting that this lectin may be a new strategy for the development of antileishmanial drugs.