Crystal structure of a hypoallergenic isoform of the major birch pollen allergen Bet v 1 and its likely biological function as a plant steroid carrier. (Articolo in rivista)

Type
Label
  • Crystal structure of a hypoallergenic isoform of the major birch pollen allergen Bet v 1 and its likely biological function as a plant steroid carrier. (Articolo in rivista) (literal)
Anno
  • 2003-01-01T00:00:00+01:00 (literal)
Alternative label
  • Markovic-Housley Z. 1, Degano M. 2, Lamba D. 3, von Roepenack-Lahaye E. 4, Clemens S. 4, Susani M. 5, Ferreira . 6, Scheiner O. 7, Breiteneder H. 7 (2003)
    Crystal structure of a hypoallergenic isoform of the major birch pollen allergen Bet v 1 and its likely biological function as a plant steroid carrier.
    in Journal of Molecular Biology
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Markovic-Housley Z. 1, Degano M. 2, Lamba D. 3, von Roepenack-Lahaye E. 4, Clemens S. 4, Susani M. 5, Ferreira . 6, Scheiner O. 7, Breiteneder H. 7 (literal)
Pagina inizio
  • 123 (literal)
Pagina fine
  • 133 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#altreInformazioni
  • A recent report showed a previously unexpected structural homology between Bet v 1 and the steroidogenic acute regulatory protein lipid transfer domains that are involved in sterol binding and translocation. The observed binding of DCA to PR-10 proteins demonstrates that the Bet v 1-like fold has evolved for a steroid-binding function. DCA promotes lipid metabolism in mammals and is not found, as a metabolite in plants; thus cannot be the natural ligand for the PR-10 proteins. However, bile salts share a striking structural similarity with brassinosteroids (BR), a family of ubiquitous plant steroid hormones that are implicated in plant development and growth processes. Mutant plants deficient in BRs biosynthesis show phenotypes of dwarfism, reduced fertility and light independent development. Therefore, DCA can be considered acting as a molecular mimic of BRs, which we propose as the natural ligands of Bet v1l and homologous PR-10 proteins. Impact factor (2002): 5.359 Citations: 12 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 325 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#descrizioneSinteticaDelProdotto
  • The impact of allergic diseases such as food allergy, rhinitis, eczema, and asthma has been surging in recent years to reach epidemic proportions. The major allergen from the pollen of Betulla verrucosa, termed Bet v 1, is a 17 kDa monomeric protein. More than 90% of individuals allergic to birch pollen have in their sera IgE molecules reactive towards the various natural isoforms of this polypeptide. Recombinant low-allergenic variants of Bet v 1 are possible candidates for vaccination therapies for allergic individuals. Bet v 1 is an epitome for the ubiquitous group of pathogenesis-related proteins (PR-10) upregulated upon fungal or bacterial infection. Despite the biochemical, immunological, and medical interest in these proteins, yet no conclusive study has been reported concerning the biological activity of PR-10 proteins. Diverse functions have been hypothesized, such as a pollen specific, weak ribonuclease activity, enzymatic activity in phenylpropanoid biosynthesis, or in secondary metabolism such as shikonin production. We determined the 3D structure of the low-allergenic isoform Bet v 1l. The structure showed no similarity to known enzymes with ribonuclease activity but two deoxycholate (DCA) molecules, probably bound to the protein during the purification process, could unambiguously be identified in a Y-shaped hydrophobic pocket inside the protein. The 3D structure of Bet v 1l in complex with DCA defines a role for PR-10 proteins as steroid carriers. (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • 1 Uni Basel, 2 DIBIT-HSR, 3 IC-CNR, 4 Leibniz Institute of Plant Biochemistry, 5 BIOMAY Comp, 6 Uni Salzburg, 7 Uni Wien (literal)
Titolo
  • Crystal structure of a hypoallergenic isoform of the major birch pollen allergen Bet v 1 and its likely biological function as a plant steroid carrier. (literal)
Abstract
  • Bet v 1l is a naturally occurring hypoallergenic isoform of the major birch pollen allergen Bet v 1. The Bet v 1 protein belongs to the ubiquitous family of pathogenesis-related plant proteins (PR-10), which are produced in defense-response to various pathogens. Although the allergenic properties of PR-10 proteins have been extensively studied, their biological function in plants is not known. The crystal structure of Bet v 1l in complex with deoxycholate has been determined to a resolution of 1.9A using the method of molecular replacement. The structure reveals a large hydrophobic Y-shaped cavity that spans the protein and is partly occupied by two deoxycholate molecules which are bound in tandem and only partially exposed to solvent. This finding indicates that the hydrophobic cavity may have a role in facilitating the transfer of apolar ligands. The structural similarity of deoxycholate and brassinosteroids (BRs) ubiquitous plant steroid hormones, prompted the mass spectrometry (MS) study in order to examine whether BRs can bind to Bet v 1l. The MS analysis of a mixture of Bet v 1l and BRs revealed a specific non-covalent interaction of Bet v 1l with brassinolide and 24-epicastasterone. Together, our findings are consistent with a general plant-steroid carrier function for Bet v 1 and related PR-10 proteins. The role of BRs transport in PR-10 proteins may be of crucial importance in the plant defense response to pathological situations as well as in growth and development. (literal)
Prodotto di
Autore CNR
Insieme di parole chiave

Incoming links:


Prodotto
Autore CNR di
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi
Insieme di parole chiave di
data.CNR.it