Please use this identifier to cite or link to this item:https://hdl.handle.net/20.500.12259/103212
Type of publication: research article
Type of publication (PDB): Straipsnis Clarivate Analytics Web of Science / Article in Clarivate Analytics Web of Science (S1)
Field of Science: Biologija / Biology (N010);Farmacija / Pharmacy (M003)
Author(s): Balčiūnaitė, Gabrielė;Haimi, Perttu Juhani;Miknienė, Zoja;Savickas, Girius;Ragažinskienė, Ona;Juodžiukynienė, Nomeda;Baniulis, Danas;Pangonytė, Dalia
Title: Identification of Echinacea purpurea (L.) Moench root LysM lectin with nephrotoxic properties
Is part of: Toxins. Basel: MDPI AG, 2020, Vol. 12, iss. 2
Extent: p. 1-18
Date: 2020
Keywords: Lectin;Echinacea purpurea L;Moench;Hemagglutinin;LysM;Lectin purification;Hemagglutinating activity;Affinity chromatography
Abstract: Echinacea purpurea (L.) Moench (EP) is a well-studied plant used for health benefits. Even though there are a lot of data on EP secondary metabolites, its active proteins are not studied well enough. The aim of our experiment was to purify lectin fraction from EP roots and evaluate its biological activity in vitro as well as its effect on kidney morphology in vivo. An EP root glycoprotein fraction was purified by affinity chromatography, identified by LC-MS/MS, and used for biological activity tests in vitro and in vivo. Identified glycoproteins were homologous with the LysM domain containing lectins from the Asteraceae plants Helianthus annuus L., Lactuca sativa L., Cynara cardunculus L. A purified fraction was tested by hemagglutination and hemagglutination inhibition (by carbohydrate reactions) in vitro. We purified the hemagglutinating active ~40 kDa size lactose, D-mannose, and D-galactose specific glycoproteins with two peptidoglycan binding LysM (lysine motif) domains. Purified LysM lectin was tested in vivo. Eight-week old Balb/C male mice (n = 15) were treated with 5 μg of the purified lectin. Injections were repeated four times per week. At the fifth experimental week, animals were sedated with carbon dioxide, then euthanized by cervical dislocation and their kidney samples were collected. Morphological changes were evaluated in hematoxylin and eosin stained kidney samples. The purified LysM lectin induced a statistically significant (p < 0.05) kidney glomerular vacuolization and kidney tubular necrosis (p < 0.001)
Internet: https://www.vdu.lt/cris/bitstream/20.500.12259/103212/2/ISSN2072-6651_2020_V_12_2.PG_1-18.pdf
https://hdl.handle.net/20.500.12259/103212
https://doi.org/10.3390/toxins12020088
Affiliation(s): Lietuvos agrarinių ir miškų mokslų centras
Lietuvos agrarinių ir miškų mokslų centro Sodininkystės ir daržininkystės institutas
Lietuvos sveikatos mokslų universitetas. Medicinos akademija
Lietuvos sveikatos mokslų universitetas. Medicinos akademija. Farmacinių technologijų institutas
Lietuvos sveikatos mokslų universitetas. Veterinarijos akademija
Vaistinių ir prieskon. augalų moks. sek.
Vytauto Didžiojo universitetas
Appears in Collections:1. Straipsniai / Articles
Universiteto mokslo publikacijos / University Research Publications

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