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Structure and Biological Properties of Ribosome-Inactivating Proteins and Lectins from Elder (Sambucus nigra L.) Leaves
Ribosome-inactivating proteins (RIPs) are a group of proteins with rRNA N-glycosylase activity that catalyze the removal of a specific adenine located in the sarcin–ricin loop of the large ribosomal RNA, which leads to the irreversible inhibition of protein synthesis and, consequently, cell death. T...
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Published in: | Toxins 2022-09, Vol.14 (9), p.611 |
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description | Ribosome-inactivating proteins (RIPs) are a group of proteins with rRNA N-glycosylase activity that catalyze the removal of a specific adenine located in the sarcin–ricin loop of the large ribosomal RNA, which leads to the irreversible inhibition of protein synthesis and, consequently, cell death. The case of elderberry (Sambucus nigra L.) is unique, since more than 20 RIPs and related lectins have been isolated and characterized from the flowers, seeds, fruits, and bark of this plant. However, these kinds of proteins have never been isolated from elderberry leaves. In this work, we have purified RIPs and lectins from the leaves of this shrub, studying their main physicochemical characteristics, sequences, and biological properties. In elderberry leaves, we found one type 2 RIP and two related lectins that are specific for galactose, four type 2 RIPs that fail to agglutinate erythrocytes, and one type 1 RIP. Several of these proteins are homologous to others found elsewhere in the plant. The diversity of RIPs and lectins in the different elderberry tissues, and the different biological activities of these proteins, which have a high degree of homology with each other, constitute an excellent source of proteins that are of great interest in diagnostics, experimental therapy, and agriculture. |
doi_str_mv | 10.3390/toxins14090611 |
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However, these kinds of proteins have never been isolated from elderberry leaves. In this work, we have purified RIPs and lectins from the leaves of this shrub, studying their main physicochemical characteristics, sequences, and biological properties. In elderberry leaves, we found one type 2 RIP and two related lectins that are specific for galactose, four type 2 RIPs that fail to agglutinate erythrocytes, and one type 1 RIP. Several of these proteins are homologous to others found elsewhere in the plant. The diversity of RIPs and lectins in the different elderberry tissues, and the different biological activities of these proteins, which have a high degree of homology with each other, constitute an excellent source of proteins that are of great interest in diagnostics, experimental therapy, and agriculture.</description><identifier>ISSN: 2072-6651</identifier><identifier>EISSN: 2072-6651</identifier><identifier>DOI: 10.3390/toxins14090611</identifier><identifier>PMID: 36136551</identifier><language>eng</language><publisher>Basel: MDPI AG</publisher><subject>Adenine ; anticancer agents ; Bark ; Biological properties ; Cell death ; Chloride ; Chromatography ; Composition ; Deactivation ; Elderberries ; Elders (Plants) ; Erythrocytes ; Evaluation ; Flowers ; Galactose ; Homology ; Identification and classification ; Leaves ; lectin ; Lectins ; N-Glycosylase ; nanoLC–tandem mass spectrometry (nLC-MS/MS) ; Polypeptides ; Properties ; Protein biosynthesis ; Protein synthesis ; protein synthesis (inhibition) ; Proteins ; ribosome-inactivating protein (RIP) ; Ricin ; rRNA ; Sambucus ; Sambucus nigra ; Seeds ; Sodium ; Toxicity</subject><ispartof>Toxins, 2022-09, Vol.14 (9), p.611</ispartof><rights>COPYRIGHT 2022 MDPI AG</rights><rights>2022 by the authors. 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Leaves</title><title>Toxins</title><description>Ribosome-inactivating proteins (RIPs) are a group of proteins with rRNA N-glycosylase activity that catalyze the removal of a specific adenine located in the sarcin–ricin loop of the large ribosomal RNA, which leads to the irreversible inhibition of protein synthesis and, consequently, cell death. The case of elderberry (Sambucus nigra L.) is unique, since more than 20 RIPs and related lectins have been isolated and characterized from the flowers, seeds, fruits, and bark of this plant. However, these kinds of proteins have never been isolated from elderberry leaves. In this work, we have purified RIPs and lectins from the leaves of this shrub, studying their main physicochemical characteristics, sequences, and biological properties. In elderberry leaves, we found one type 2 RIP and two related lectins that are specific for galactose, four type 2 RIPs that fail to agglutinate erythrocytes, and one type 1 RIP. Several of these proteins are homologous to others found elsewhere in the plant. The diversity of RIPs and lectins in the different elderberry tissues, and the different biological activities of these proteins, which have a high degree of homology with each other, constitute an excellent source of proteins that are of great interest in diagnostics, experimental therapy, and agriculture.</description><subject>Adenine</subject><subject>anticancer agents</subject><subject>Bark</subject><subject>Biological properties</subject><subject>Cell death</subject><subject>Chloride</subject><subject>Chromatography</subject><subject>Composition</subject><subject>Deactivation</subject><subject>Elderberries</subject><subject>Elders (Plants)</subject><subject>Erythrocytes</subject><subject>Evaluation</subject><subject>Flowers</subject><subject>Galactose</subject><subject>Homology</subject><subject>Identification and classification</subject><subject>Leaves</subject><subject>lectin</subject><subject>Lectins</subject><subject>N-Glycosylase</subject><subject>nanoLC–tandem mass spectrometry (nLC-MS/MS)</subject><subject>Polypeptides</subject><subject>Properties</subject><subject>Protein biosynthesis</subject><subject>Protein synthesis</subject><subject>protein synthesis (inhibition)</subject><subject>Proteins</subject><subject>ribosome-inactivating protein (RIP)</subject><subject>Ricin</subject><subject>rRNA</subject><subject>Sambucus</subject><subject>Sambucus nigra</subject><subject>Seeds</subject><subject>Sodium</subject><subject>Toxicity</subject><issn>2072-6651</issn><issn>2072-6651</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><sourceid>DOA</sourceid><recordid>eNptks9vFCEUxydGY5vaq-dJvNTDbvkxMMPFpDZVN9lEY_VMgHmMbGZgBWar_73strGuKRx4ee_zvvAlr6peY7SkVKDLHH45n3CDBOIYP6tOCWrJgnOGn_8Tn1TnKW1QWZRigduX1QnlmHLG8Gl1d5vjbPIcoVa-r9-7MIbBGTXWX2LYQswOUh1s_dXpkMIEi5VXJrudys4PeyZDecKhdw2lUGIbw1TfjD3E-uJWTXo2c6q9G6Kq18u3BVM7SK-qF1aNCc4fzrPq-4ebb9efFuvPH1fXV-uFYaTLC046bUBowJ3lwgLpiwNDcK810T1DBlGhNWUcFYhhao2lFjpmG2JEMU_PqtW9bh_URm6jm1T8LYNy8pAIcZCqmDQjyB4jYShljWKkET2ITmlmrcWCU0SoKVrv7rW2s56gN-BzVOOR6HHFux9yCDspGCoKTRG4eBCI4ecMKcvJJQPjqDyEOUnSYi4aSvkeffMfuglz9OWrDhRHLaPtIzWoYsB5G8q9Zi8qr9qGF5B2qFDLJ6iye5icCR6sK_mnGkwMKUWwfz1iJPeTJ48nj_4BlBvKwA</recordid><startdate>20220901</startdate><enddate>20220901</enddate><creator>Iglesias, Rosario</creator><creator>Russo, Rosita</creator><creator>Landi, Nicola</creator><creator>Valletta, Mariangela</creator><creator>Chambery, Angela</creator><creator>Di Maro, Antimo</creator><creator>Bolognesi, Andrea</creator><creator>Ferreras, José M</creator><creator>Citores, Lucía</creator><general>MDPI AG</general><general>MDPI</general><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7T7</scope><scope>7U7</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>P64</scope><scope>PATMY</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PYCSY</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope><orcidid>https://orcid.org/0000-0002-2235-6302</orcidid><orcidid>https://orcid.org/0000-0003-4816-5878</orcidid><orcidid>https://orcid.org/0000-0002-5136-0941</orcidid><orcidid>https://orcid.org/0000-0001-7497-4586</orcidid><orcidid>https://orcid.org/0000-0003-3784-5042</orcidid><orcidid>https://orcid.org/0000-0002-5021-1733</orcidid><orcidid>https://orcid.org/0000-0002-9595-9665</orcidid></search><sort><creationdate>20220901</creationdate><title>Structure and Biological Properties of Ribosome-Inactivating Proteins and Lectins from Elder (Sambucus nigra L.) Leaves</title><author>Iglesias, Rosario ; Russo, Rosita ; Landi, Nicola ; Valletta, Mariangela ; Chambery, Angela ; Di Maro, Antimo ; Bolognesi, Andrea ; Ferreras, José M ; Citores, Lucía</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c528t-628bce9be18f69fe2d191c21dbb2bd50c039bb3560e9b513fcf3fe85f42c96653</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Adenine</topic><topic>anticancer agents</topic><topic>Bark</topic><topic>Biological properties</topic><topic>Cell death</topic><topic>Chloride</topic><topic>Chromatography</topic><topic>Composition</topic><topic>Deactivation</topic><topic>Elderberries</topic><topic>Elders (Plants)</topic><topic>Erythrocytes</topic><topic>Evaluation</topic><topic>Flowers</topic><topic>Galactose</topic><topic>Homology</topic><topic>Identification and classification</topic><topic>Leaves</topic><topic>lectin</topic><topic>Lectins</topic><topic>N-Glycosylase</topic><topic>nanoLC–tandem mass spectrometry (nLC-MS/MS)</topic><topic>Polypeptides</topic><topic>Properties</topic><topic>Protein biosynthesis</topic><topic>Protein synthesis</topic><topic>protein synthesis (inhibition)</topic><topic>Proteins</topic><topic>ribosome-inactivating protein (RIP)</topic><topic>Ricin</topic><topic>rRNA</topic><topic>Sambucus</topic><topic>Sambucus nigra</topic><topic>Seeds</topic><topic>Sodium</topic><topic>Toxicity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Iglesias, Rosario</creatorcontrib><creatorcontrib>Russo, Rosita</creatorcontrib><creatorcontrib>Landi, Nicola</creatorcontrib><creatorcontrib>Valletta, Mariangela</creatorcontrib><creatorcontrib>Chambery, Angela</creatorcontrib><creatorcontrib>Di Maro, Antimo</creatorcontrib><creatorcontrib>Bolognesi, Andrea</creatorcontrib><creatorcontrib>Ferreras, José M</creatorcontrib><creatorcontrib>Citores, Lucía</creatorcontrib><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Toxicology Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>ProQuest - Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Environmental Science Collection</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>Toxins</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Iglesias, Rosario</au><au>Russo, Rosita</au><au>Landi, Nicola</au><au>Valletta, Mariangela</au><au>Chambery, Angela</au><au>Di Maro, Antimo</au><au>Bolognesi, Andrea</au><au>Ferreras, José M</au><au>Citores, Lucía</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure and Biological Properties of Ribosome-Inactivating Proteins and Lectins from Elder (Sambucus nigra L.) Leaves</atitle><jtitle>Toxins</jtitle><date>2022-09-01</date><risdate>2022</risdate><volume>14</volume><issue>9</issue><spage>611</spage><pages>611-</pages><issn>2072-6651</issn><eissn>2072-6651</eissn><abstract>Ribosome-inactivating proteins (RIPs) are a group of proteins with rRNA N-glycosylase activity that catalyze the removal of a specific adenine located in the sarcin–ricin loop of the large ribosomal RNA, which leads to the irreversible inhibition of protein synthesis and, consequently, cell death. The case of elderberry (Sambucus nigra L.) is unique, since more than 20 RIPs and related lectins have been isolated and characterized from the flowers, seeds, fruits, and bark of this plant. However, these kinds of proteins have never been isolated from elderberry leaves. In this work, we have purified RIPs and lectins from the leaves of this shrub, studying their main physicochemical characteristics, sequences, and biological properties. In elderberry leaves, we found one type 2 RIP and two related lectins that are specific for galactose, four type 2 RIPs that fail to agglutinate erythrocytes, and one type 1 RIP. Several of these proteins are homologous to others found elsewhere in the plant. The diversity of RIPs and lectins in the different elderberry tissues, and the different biological activities of these proteins, which have a high degree of homology with each other, constitute an excellent source of proteins that are of great interest in diagnostics, experimental therapy, and agriculture.</abstract><cop>Basel</cop><pub>MDPI AG</pub><pmid>36136551</pmid><doi>10.3390/toxins14090611</doi><orcidid>https://orcid.org/0000-0002-2235-6302</orcidid><orcidid>https://orcid.org/0000-0003-4816-5878</orcidid><orcidid>https://orcid.org/0000-0002-5136-0941</orcidid><orcidid>https://orcid.org/0000-0001-7497-4586</orcidid><orcidid>https://orcid.org/0000-0003-3784-5042</orcidid><orcidid>https://orcid.org/0000-0002-5021-1733</orcidid><orcidid>https://orcid.org/0000-0002-9595-9665</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | Adenine anticancer agents Bark Biological properties Cell death Chloride Chromatography Composition Deactivation Elderberries Elders (Plants) Erythrocytes Evaluation Flowers Galactose Homology Identification and classification Leaves lectin Lectins N-Glycosylase nanoLC–tandem mass spectrometry (nLC-MS/MS) Polypeptides Properties Protein biosynthesis Protein synthesis protein synthesis (inhibition) Proteins ribosome-inactivating protein (RIP) Ricin rRNA Sambucus Sambucus nigra Seeds Sodium Toxicity |
title | Structure and Biological Properties of Ribosome-Inactivating Proteins and Lectins from Elder (Sambucus nigra L.) Leaves |
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