Activity Dependence of a Novel Lectin Family on Structure and Carbohydrate-Binding Properties

A GalNAc/Gal-specific lectins named CGL and MTL were isolated and characterized from the edible mussels Crenomytilus grayanus and Mytilus trossulus. Amino acid sequence analysis of these lectins showed that they, together with another lectin MytiLec-1, formed a novel lectin family, adopting β-trefoi...

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Published inMolecules (Basel, Switzerland) Vol. 25; no. 1; p. 150
Main Authors Chikalovets, Irina, Filshtein, Alina, Molchanova, Valentina, Mizgina, Tatyana, Lukyanov, Pavel, Nedashkovskaya, Olga, Hua, Kuo-Feng, Chernikov, Oleg
Format Journal Article
LanguageEnglish
Published Switzerland MDPI AG 30.12.2019
MDPI
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ISSN1420-3049
1420-3049
DOI10.3390/molecules25010150

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Abstract A GalNAc/Gal-specific lectins named CGL and MTL were isolated and characterized from the edible mussels Crenomytilus grayanus and Mytilus trossulus. Amino acid sequence analysis of these lectins showed that they, together with another lectin MytiLec-1, formed a novel lectin family, adopting β-trefoil fold. In this mini review we discuss the structure, oligomerization, and carbohydrate-binding properties of a novel lectin family. We describe also the antibacterial, antifungal, and antiproliferative activities of these lectins and report about dependence of activities on molecular properties. Summarizing, CGL, MTL, and MytiLec-1 could be involved in the immunity in mollusks and may become a basis for the elaboration of new diagnostic tools or treatments for a variety of cancers.
AbstractList A GalNAc/Gal-specific lectins named CGL and MTL were isolated and characterized from the edible mussels Crenomytilus grayanus and Mytilus trossulus. Amino acid sequence analysis of these lectins showed that they, together with another lectin MytiLec-1, formed a novel lectin family, adopting β-trefoil fold. In this mini review we discuss the structure, oligomerization, and carbohydrate-binding properties of a novel lectin family. We describe also the antibacterial, antifungal, and antiproliferative activities of these lectins and report about dependence of activities on molecular properties. Summarizing, CGL, MTL, and MytiLec-1 could be involved in the immunity in mollusks and may become a basis for the elaboration of new diagnostic tools or treatments for a variety of cancers.
A GalNAc/Gal-specific lectins named CGL and MTL were isolated and characterized from the edible mussels Crenomytilus grayanus and Mytilus trossulus. Amino acid sequence analysis of these lectins showed that they, together with another lectin MytiLec-1, formed a novel lectin family, adopting β-trefoil fold. In this mini review we discuss the structure, oligomerization, and carbohydrate-binding properties of a novel lectin family. We describe also the antibacterial, antifungal, and antiproliferative activities of these lectins and report about dependence of activities on molecular properties. Summarizing, CGL, MTL, and MytiLec-1 could be involved in the immunity in mollusks and may become a basis for the elaboration of new diagnostic tools or treatments for a variety of cancers.A GalNAc/Gal-specific lectins named CGL and MTL were isolated and characterized from the edible mussels Crenomytilus grayanus and Mytilus trossulus. Amino acid sequence analysis of these lectins showed that they, together with another lectin MytiLec-1, formed a novel lectin family, adopting β-trefoil fold. In this mini review we discuss the structure, oligomerization, and carbohydrate-binding properties of a novel lectin family. We describe also the antibacterial, antifungal, and antiproliferative activities of these lectins and report about dependence of activities on molecular properties. Summarizing, CGL, MTL, and MytiLec-1 could be involved in the immunity in mollusks and may become a basis for the elaboration of new diagnostic tools or treatments for a variety of cancers.
A GalNAc/Gal-specific lectins named CGL and MTL were isolated and characterized from the edible mussels and . Amino acid sequence analysis of these lectins showed that they, together with another lectin MytiLec-1, formed a novel lectin family, adopting β-trefoil fold. In this mini review we discuss the structure, oligomerization, and carbohydrate-binding properties of a novel lectin family. We describe also the antibacterial, antifungal, and antiproliferative activities of these lectins and report about dependence of activities on molecular properties. Summarizing, CGL, MTL, and MytiLec-1 could be involved in the immunity in mollusks and may become a basis for the elaboration of new diagnostic tools or treatments for a variety of cancers.
A GalNAc/Gal-specific lectins named CGL and MTL were isolated and characterized from the edible mussels Crenomytilus grayanus and Mytilus trossulus . Amino acid sequence analysis of these lectins showed that they, together with another lectin MytiLec-1, formed a novel lectin family, adopting β-trefoil fold. In this mini review we discuss the structure, oligomerization, and carbohydrate-binding properties of a novel lectin family. We describe also the antibacterial, antifungal, and antiproliferative activities of these lectins and report about dependence of activities on molecular properties. Summarizing, CGL, MTL, and MytiLec-1 could be involved in the immunity in mollusks and may become a basis for the elaboration of new diagnostic tools or treatments for a variety of cancers.
Author Chikalovets, Irina
Molchanova, Valentina
Filshtein, Alina
Lukyanov, Pavel
Nedashkovskaya, Olga
Mizgina, Tatyana
Chernikov, Oleg
Hua, Kuo-Feng
AuthorAffiliation 3 Department of Biotechnology and Animal Science, National Ilan University, Ilan 260, Taiwan
4 Department of Pathology, Tri-Service General Hospital, National Defense Medical Center, Taipei 114, Taiwan
1 G.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far Eastern Branch of the Russian Academy of Sciences, Vladivostok 690022, Russia
2 School of Natural Sciences, Far Eastern Federal University, Vladivostok 690950, Russia
AuthorAffiliation_xml – name: 1 G.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far Eastern Branch of the Russian Academy of Sciences, Vladivostok 690022, Russia
– name: 4 Department of Pathology, Tri-Service General Hospital, National Defense Medical Center, Taipei 114, Taiwan
– name: 3 Department of Biotechnology and Animal Science, National Ilan University, Ilan 260, Taiwan
– name: 2 School of Natural Sciences, Far Eastern Federal University, Vladivostok 690950, Russia
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/31905927$$D View this record in MEDLINE/PubMed
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Issue 1
Keywords Gal-specific
mytilectin family
lectin
Crenomytilus grayanus
mussel
carbohydrate specificity
Mytilus trossulus
Language English
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Snippet A GalNAc/Gal-specific lectins named CGL and MTL were isolated and characterized from the edible mussels Crenomytilus grayanus and Mytilus trossulus. Amino acid...
A GalNAc/Gal-specific lectins named CGL and MTL were isolated and characterized from the edible mussels and . Amino acid sequence analysis of these lectins...
A GalNAc/Gal-specific lectins named CGL and MTL were isolated and characterized from the edible mussels Crenomytilus grayanus and Mytilus trossulus . Amino...
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SubjectTerms Antifungal agents
Binding sites
carbohydrate specificity
Carbohydrates
crenomytilus grayanus
Crystal structure
Enzymes
gal-specific
Invertebrates
lectin
Lectins
Ligands
Mammals
mussel
mytilectin family
mytilus trossulus
Proteins
Review
Signal transduction
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Title Activity Dependence of a Novel Lectin Family on Structure and Carbohydrate-Binding Properties
URI https://www.ncbi.nlm.nih.gov/pubmed/31905927
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