Comprehensive review on Caelsalpinioideae lectins: From purification to biological activities

Int J Biol Macromol. 2020 Nov 1:162:333-348. doi: 10.1016/j.ijbiomac.2020.06.161. Epub 2020 Jun 20.

Abstract

Lectins are a class of proteins with specific and reversible carbohydrate binding properties. Plant lectins constitute the group of these proteins most studied, placing emphasis on the legume family. The Caesalpinioideae subfamily is part of Leguminosae and second only to Papilionoideae with more published works on lectins. Classically, Caesalpinioideae is formed by 171 genera and 2250 species. It presents 13 genera with reports of lectins, featuring the Bauhinia genus with the greatest number of species having purified and characterized lectins. Comparing genera, the lectins in this subfamily do not have similar physicochemical or structural properties. Collectively, however, antibacterial, antiviral, and anticancer activities have been reported, as well as applications as biosensors and biomarkers. This review aims to summarize the available data on purified lectins from species of the Caesalpinioideae subfamily, demonstrating the characteristics of these molecules and the potential for their application in future studies of new lectins, as well as of application in several areas.

Keywords: Caesalpinioideae; Lectins; Leguminosae.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Anti-Bacterial Agents / pharmacology*
  • Anti-Inflammatory Agents / pharmacology
  • Antifungal Agents / pharmacology*
  • Antineoplastic Agents / pharmacology*
  • Antiviral Agents / pharmacology*
  • Bauhinia / chemistry*
  • Fabaceae / chemistry
  • Metals / chemistry
  • Molecular Conformation
  • Phylogeny
  • Plant Lectins / chemistry*
  • Plant Lectins / isolation & purification
  • Plant Lectins / metabolism
  • Plant Lectins / pharmacology*
  • Protein Domains

Substances

  • Anti-Bacterial Agents
  • Anti-Inflammatory Agents
  • Antifungal Agents
  • Antineoplastic Agents
  • Antiviral Agents
  • Metals
  • Plant Lectins