In silico characterization and phylogenetic analysis of a mannose-specific lectin in Allium species

H.J. Jimenez, L.S.S. Martins, R. Carvalho, A.V.V. Montarroyos, R.M. Moraes Filho
Published: June 18, 2019
Genet. Mol. Res. 18(2): GMR18187
DOI: https://doi.org/10.4238/gmr18187

Cite this Article:
H.J. Jimenez, L.S.S. Martins, R. Carvalho, A.V.V. Montarroyos, R.M.Moraes Filho (2019). In silico characterization and phylogenetic analysis of a mannose-specific lectin in Allium species. Genet. Mol. Res. 18(2): GMR18187. https://doi.org/10.4238/gmr18187

About the Authors
H.J. Jimenez, L.S.S. Martins, R. Carvalho, A.V.V. Montarroyos, R.M. Moraes Filho

Corresponding Author
R.M. Moraes Filho
Email: romulommfilho@yahoo.com.br

ABSTRACT
The Allium genus stands out for its uses in human food and also for its medicinal properties. Many representatives of the Amaryllidaceae family are known for producing mannose binding lectins (MBL). In plants, lectins act as reserves of proteins that can be used for plant growth and development and also in defense against herbivores and pathogens, being toxic to some aphids and sucking insects. We examined physicochemical characteristics, such as isoelectric points and hydropathicity, of 22 sequences of MBL protein from Allium species and from other representatives of the Amaryllidaceae family present in public databases. Phylogenetic analysis, identification of functional domains and 3D homology modeling were also performed. We found two conserved functional motifs in the MBL sequences. It was observed that for all species the MBL had a hydrophilic character and great variation in isoelectric points. The phylogenetic analysis was not consistent with the taxonomic classification of the species evaluated at the infrageneric level. However, the methods proved efficient for the separation up to the level of tribes within the Amaryllidaceae family. The generated 3D models also provide a better understanding of their tertiary structures and molecular functions.

Key words: Bioinformatics, Conserved domains, Homology modeling.

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