Comparative Study of Lectin Domains in Model Species: New Insights into Evolutionary Dynamics

• Published in: International journal of molecular sciences 2017-05, Vol.18 (6), p.1136
• Main Authors: Van Holle, Sofie, De Schutter, Kristof, Eggermont, Lore, Tsaneva, Mariya, Dang, Liuyi, Van Damme, Els J M
• Format: Article
• Language: English
• Subjects: Binding sites; Biological activity; Biological evolution; carbohydrate; Carbohydrates; Comparative analysis; Comparative studies; Computational Biology - methods; Databases, Genetic; Divergence; Evolution; Evolution, Molecular; Flowers & plants; Genes; Genetic screening; Genomes; lectin; Lectins; Lectins - chemistry; Lectins - genetics; Legumes; Markov chains; Oryza sativa; Phylogenetics; Phylogeny; Plant Lectins - chemistry; Plant Lectins - genetics; Plants - classification; Plants - genetics; Polyploidy; protein domain; Protein Domains - genetics; Proteins; Seeds; Soybeans; Species Specificity
• ISSN: 1422-0067; 1661-6596; 1422-0067
• DOI: 10.3390/ijms18061136

Lectins are present throughout the plant kingdom and are reported to be involved in diverse biological processes. In this study, we provide a comparative analysis of the lectin families from model species in a phylogenetic framework. The analysis focuses on the different plant lectin domains identified in five representative core angiosperm genomes ( , , , ssp. and ssp. ). The genomes were screened for genes encoding lectin domains using a combination of Basic Local Alignment Search Tool (BLAST), hidden Markov models, and InterProScan analysis. Additionally, phylogenetic relationships were investigated by constructing maximum likelihood phylogenetic trees. The results demonstrate that the majority of the lectin families are present in each of the species under study. Domain organization analysis showed that most identified proteins are multi-domain proteins, owing to the modular rearrangement of protein domains during evolution. Most of these multi-domain proteins are widespread, while others display a lineage-specific distribution. Furthermore, the phylogenetic analyses reveal that some lectin families evolved to be similar to the phylogeny of the plant species, while others share a closer evolutionary history based on the corresponding protein domain architecture. Our results yield insights into the evolutionary relationships and functional divergence of plant lectins.