Lectins of the Araceae family: Insights, distinctions, and future avenues—A three-decade investigation

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...

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Published inBiochimica et biophysica acta. General subjects Vol. 1868; no. 9; p. 130667
Main Authors Konozy, Emadeldin Hassan E., Dirar, Amina I., Osman, Makarim Elfadil M.
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.09.2024
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Abstract 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. [Display omitted] •Reviews three decades of Araceae lectin research.•Covers extraction, purification, structures, and properties.•Investigates biological activities and gene cloning.•Examines unique interactions and 3D structures.•First comprehensive review for glycobiology.•Provides insights into challenges and future research.
AbstractList 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.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.
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.
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. [Display omitted] •Reviews three decades of Araceae lectin research.•Covers extraction, purification, structures, and properties.•Investigates biological activities and gene cloning.•Examines unique interactions and 3D structures.•First comprehensive review for glycobiology.•Provides insights into challenges and future research.
ArticleNumber 130667
Author Osman, Makarim Elfadil M.
Konozy, Emadeldin Hassan E.
Dirar, Amina I.
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  givenname: Amina I.
  surname: Dirar
  fullname: Dirar, Amina I.
  organization: Medicinal, Aromatic Plants and Traditional Medicine Research Institute (MAPTRI), National Center for Research, P.O. Box 2404, Mek Nimr Street, Khartoum, Sudan
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  givenname: Makarim Elfadil M.
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  fullname: Osman, Makarim Elfadil M.
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Keywords Characterization
Lectins
GNA-related lectins
Araceae
Structure
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Snippet 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,...
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SubjectTerms Animals
Araceae
Characterization
dimerization
erythrocytes
family
glycomics
GNA-related lectins
Humans
Lectins
Monocot
Plant Lectins - chemistry
Plant Lectins - metabolism
species
Structure
sugars
Title Lectins of the Araceae family: Insights, distinctions, and future avenues—A three-decade investigation
URI https://dx.doi.org/10.1016/j.bbagen.2024.130667
https://www.ncbi.nlm.nih.gov/pubmed/38971261
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https://www.proquest.com/docview/3200280323
Volume 1868
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