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Structural glycobiology of the major allergen of Artemisia vulgaris pollen, Art v 1: O-glycosylation influence on the protein dynamics and allergenicity.
Glycobiology. 2012 Jun; 22(6):817-25.G

Abstract

Art v 1 is the major allergen of mugwort (Artemisia vulgaris) pollen. It is formed by an N-terminal globular defensin-like part and a C-terminal proline-rich domain. As the structure and the dynamics of Art v 1 have been mostly described for its recombinant, non-glycosylated form, which does not occur in normal plant physiology, the present work intends to obtain a three-dimensional model for Art v 1 native O-glycosylation structure and to evaluate the influence of such glycans over the protein dynamics and allergenicity through molecular dynamics simulations in triplicates. Structural insights into the mutual recognition of Art v 1 protein and carbohydrate moieties recognition by antibodies were obtained, in which glycan chains remained close to the previously identified epitopes in the defensin-like domain, thus pointing to potential interferences with antibodies recognition. To our knowledge, this is the first structural report of an entire furanose-containing glycoprotein. As well, together with the previously determined NMR structures, the obtained results contribute in the comprehension of the effect of glycosylation over both proline-rich and defensin-like domains, providing an atomic representation of such alterations.

Authors+Show Affiliations

Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul, Av Bento Gonçalves 9500, CP 15005, Porto Alegre 91500-970 RS, Brazil.No affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

22367746

Citation

Pol-Fachin, Laercio, and Hugo Verli. "Structural Glycobiology of the Major Allergen of Artemisia Vulgaris Pollen, Art V 1: O-glycosylation Influence On the Protein Dynamics and Allergenicity." Glycobiology, vol. 22, no. 6, 2012, pp. 817-25.
Pol-Fachin L, Verli H. Structural glycobiology of the major allergen of Artemisia vulgaris pollen, Art v 1: O-glycosylation influence on the protein dynamics and allergenicity. Glycobiology. 2012;22(6):817-25.
Pol-Fachin, L., & Verli, H. (2012). Structural glycobiology of the major allergen of Artemisia vulgaris pollen, Art v 1: O-glycosylation influence on the protein dynamics and allergenicity. Glycobiology, 22(6), 817-25. https://doi.org/10.1093/glycob/cws056
Pol-Fachin L, Verli H. Structural Glycobiology of the Major Allergen of Artemisia Vulgaris Pollen, Art V 1: O-glycosylation Influence On the Protein Dynamics and Allergenicity. Glycobiology. 2012;22(6):817-25. PubMed PMID: 22367746.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Structural glycobiology of the major allergen of Artemisia vulgaris pollen, Art v 1: O-glycosylation influence on the protein dynamics and allergenicity. AU - Pol-Fachin,Laercio, AU - Verli,Hugo, Y1 - 2012/02/23/ PY - 2012/2/28/entrez PY - 2012/3/1/pubmed PY - 2013/1/10/medline SP - 817 EP - 25 JF - Glycobiology JO - Glycobiology VL - 22 IS - 6 N2 - Art v 1 is the major allergen of mugwort (Artemisia vulgaris) pollen. It is formed by an N-terminal globular defensin-like part and a C-terminal proline-rich domain. As the structure and the dynamics of Art v 1 have been mostly described for its recombinant, non-glycosylated form, which does not occur in normal plant physiology, the present work intends to obtain a three-dimensional model for Art v 1 native O-glycosylation structure and to evaluate the influence of such glycans over the protein dynamics and allergenicity through molecular dynamics simulations in triplicates. Structural insights into the mutual recognition of Art v 1 protein and carbohydrate moieties recognition by antibodies were obtained, in which glycan chains remained close to the previously identified epitopes in the defensin-like domain, thus pointing to potential interferences with antibodies recognition. To our knowledge, this is the first structural report of an entire furanose-containing glycoprotein. As well, together with the previously determined NMR structures, the obtained results contribute in the comprehension of the effect of glycosylation over both proline-rich and defensin-like domains, providing an atomic representation of such alterations. SN - 1460-2423 UR - https://www.unboundmedicine.com/medline/citation/22367746/Structural_glycobiology_of_the_major_allergen_of_Artemisia_vulgaris_pollen_Art_v_1:_O_glycosylation_influence_on_the_protein_dynamics_and_allergenicity_ L2 - https://academic.oup.com/glycob/article-lookup/doi/10.1093/glycob/cws056 DB - PRIME DP - Unbound Medicine ER -