Publications by authors named "Agnieszka Bogucka"

2 Publications

  • Page 1 of 1

Survival on railway tracks of Geranium robertianum-a glyphosate-tolerant plant.

Ecotoxicology 2021 Aug 10;30(6):1186-1202. Epub 2021 Jun 10.

Institute of Environmental Biology, Faculty of Biology, University of Warsaw, I. Miecznikowa 1, 02-096, Warsaw, Poland.

Geranium robertianum is a herbaceous plant that prefers shady and fertile forest habitats. However, it also occurs on railway tracks, where there are difficult conditions for plant growth and regular herbicide spraying (in high concentrations, twice a year). One of the most commonly used herbicides in railway areas is glyphosate. The effect of the glyphosate on the G. robertianum plants found on railway tracks and in nearby forests in north-eastern Poland was checked. The aim of the study was to explain how G. robertianum can survive on railway tracks despite spraying with the glyphosate. Increased tolerance to the glyphosate of the G. robertianum plants from track populations was demonstrated compared to the plants from forest populations that had not previously been in contact with the herbicide. After 35 days after treatment with the herbicide, 75% of the plants from the observed forest populations withered, while only 38% did from the track populations. Ultrastructure of plant leaf cells from forest populations was strongly disturbed, which was not observed in plants from track populations. It was also shown that plants from track populations accumulated more glyphosate and AMPA in their tissues than plants from forest populations. The obtained results indicate that long-term use of herbicides may cause formation of biotypes of plants resistant to a given herbicide. This fact explains the possibility of G. robertianum occurring on railway tracks, despite spraying with the glyphosate. It is also a manifestation of microevolutionary processes.
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http://dx.doi.org/10.1007/s10646-021-02430-5DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8295122PMC
August 2021

Crystal Structure of the Carbohydrate Recognition Domain of the Human Macrophage Galactose C-Type Lectin Bound to GalNAc and the Tumor-Associated Tn Antigen.

Biochemistry 2021 May 16;60(17):1327-1336. Epub 2021 Mar 16.

Division of Experimental Medicine, Department of Medicine, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, Massachusetts 02215, United States.

The human macrophage galactose lectin (MGL) is an endocytic type II transmembrane receptor expressed on immature monocyte-derived dendritic cells and activated macrophages and plays a role in modulating the immune system in response to infections and cancer. MGL contains an extracellular calcium-dependent (C-type) carbohydrate recognition domain (CRD) that specifically binds terminal acetylgalactosamine glycan residues such as the Tn and sialyl-Tn antigens found on tumor cells, as well as other and glycans displayed on certain viruses and parasites. Even though the glycan specificity of MGL is known and several binding glycoproteins have been identified, the molecular basis for substrate recognition has remained elusive due to the lack of high-resolution structures. Here we present crystal structures of the MGL CRD at near endosomal pH and in several complexes, which reveal details of the interactions with the natural ligand, GalNAc, the cancer-associated Tn-Ser antigen, and a synthetic GalNAc mimetic ligand. Like the asialoglycoprotein receptor, additional calcium atoms are present and contribute to stabilization of the MGL CRD fold. The structure provides the molecular basis for preferential binding of acetylgalactosamine over galactose and prompted the re-evaluation of the binding modes previously proposed in solution. Saturation transfer difference nuclear magnetic resonance data acquired using the MGL CRD and interpreted using the crystal structure indicate a single binding mode for GalNAc in solution. Models of MGL1 and MGL2, the mouse homologues of MGL, explain how these proteins might recognize Lewis and GalNAc, respectively.
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http://dx.doi.org/10.1021/acs.biochem.1c00009DOI Listing
May 2021