In Silico Characterization of Meloidogyne Genus Nematode Cellulose Binding Proteins

Abstract

Root-knot nematodes are a group of endoparasites species that induce the formation of giant cells in the hosts, by which they guarantee their feeding and development. Meloidogyne species infect over 2000 plant species, and are highly destructive, causing damage to many crops around the world. M. enterolobii is considered the most aggressive species in tropical regions, such as Africa and South America. Phytonematodes are able to penetrate and migrate within plant tissues, establishing a sophisticated interaction with their hosts through parasitism factors, which include a series of cell wall degradation enzymes and plant cell modification. Among the parasitism factors documented in the M. enterolobii species, cellulose binding protein (CBP), a nematode excretion protein that appears to be associated with the breakdown of cellulose present in the plant cell wall. In silico analysis can be of great importance for the identification, structural and functional characterization of genomic sequences, besides making possible the prediction of structures and functions of proteins. The present work characterized 12 sequences of the CBP protein of nematodes of the genus Meloidogyne present in genomic databases. The results showed that all CBP sequences had signal peptide and that, after their removal, they had an isoelectric point that characterized them as unstable in an acid medium. The values of the average hydrophilicity demonstrated the hydrophilic character of the analyzed sequences. Phylogenetic analyzes were also consistent with the taxonomic classification of the nematode species of this study. Five motifs were identified, which are present in all sequences analyzed. These results may provide theoretical grounds for future studies of plant resistance to nematode infection. HIGHLIGHTS• CBPs are remarkably conserved between Meloidogyne species • CBPs exhibit two to three functional domains related to signal binding and cellulose hydrolase activities Menezes, A.M.F.; et al.

Proteomic insights into the biology of Clinostomum piscidium from a fish, Colisa fasciatus in India using computational tools

“…Two possible transmembrane orientations(Fig. 5) were found for the present peptide sequence with positions in their bracket -Inside to outside helices : 2 found from to score center 2 ( 6) A "+" symbol indicates a preference of this orientation. A "++" symbol indicates a strong preference of this orientation.…”