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 in | Molecules (Basel, Switzerland) Vol. 25; no. 1; p. 150 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Switzerland
MDPI AG
30.12.2019
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Online Access | Get full text |
ISSN | 1420-3049 1420-3049 |
DOI | 10.3390/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. |
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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 |
Author_xml | – sequence: 1 givenname: Irina surname: Chikalovets fullname: Chikalovets, Irina – sequence: 2 givenname: Alina surname: Filshtein fullname: Filshtein, Alina – sequence: 3 givenname: Valentina surname: Molchanova fullname: Molchanova, Valentina – sequence: 4 givenname: Tatyana surname: Mizgina fullname: Mizgina, Tatyana – sequence: 5 givenname: Pavel orcidid: 0000-0002-7694-8098 surname: Lukyanov fullname: Lukyanov, Pavel – sequence: 6 givenname: Olga surname: Nedashkovskaya fullname: Nedashkovskaya, Olga – sequence: 7 givenname: Kuo-Feng surname: Hua fullname: Hua, Kuo-Feng – sequence: 8 givenname: Oleg orcidid: 0000-0002-3076-3637 surname: Chernikov fullname: Chernikov, Oleg |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/31905927$$D View this record in MEDLINE/PubMed |
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CitedBy_id | crossref_primary_10_3390_md21010010 crossref_primary_10_1002_iub_2909 crossref_primary_10_1186_s11658_022_00338_4 crossref_primary_10_1016_j_dci_2020_103823 crossref_primary_10_1016_j_ijbiomac_2023_127628 crossref_primary_10_3390_md21120614 |
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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 |
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