Lectins of the Araceae family: Insights, distinctions, and future avenues-A three-decade investigation.
Araceae
Characterization
GNA-related lectins
Lectins
Monocot
Structure
Journal
Biochimica et biophysica acta. General subjects
ISSN: 1872-8006
Titre abrégé: Biochim Biophys Acta Gen Subj
Pays: Netherlands
ID NLM: 101731726
Informations de publication
Date de publication:
04 Jul 2024
04 Jul 2024
Historique:
received:
10
05
2024
revised:
09
06
2024
accepted:
03
07
2024
medline:
7
7
2024
pubmed:
7
7
2024
entrez:
6
7
2024
Statut:
aheadofprint
Résumé
The Araceae family boasts >3000 species of flowering plants that thrive across the tropics. Among the focal points of study within this family are lectins, proteins with affinity for binding carbohydrates. This review endeavors to gather data gleaned from numerous studies conducted over the past three decades on lectins extracted from Araceae plants. Our examination spans their extraction and purification methods, their specific interactions with carbohydrates, their molecular structures, and various physicochemical characteristics. Furthermore, we investigated the biological activities of these lectins and investigated the outcomes of cloning their genes. Despite their apparent similarities, these lectins exhibit notable distinctions, particularly regarding their unique preferences in interacting with erythrocytes from animals and humans, their sugar affinities, the critical amino acids for their functionality, the molecular weights of their subunits and their respective topologies, and ultimately, their dimerization and 3D β-prism-II structure, which reportedly diverge from those observed in other GNA-related lectins. These discrepancies not only deepen our understanding of monocot lectins but also render these proteins inherently captivating. This review marks the inaugural attempt at consolidating almost all published reports on lectins from the Araceae family, with the aim of furnishing glycobiology scientists with essential insights into potential laboratory challenges, the characteristics of these lectins, and avenues for future research.
Identifiants
pubmed: 38971261
pii: S0304-4165(24)00110-7
doi: 10.1016/j.bbagen.2024.130667
pii:
doi:
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
130667Informations de copyright
Copyright © 2023. Published by Elsevier B.V.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.