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

Zora Marković-Housley, Massimo Degano, Doriano Lamba, Edda Von Roepenack-Lahaye, Stephan Clemens, Markus Susani, Fátima Ferreira, Otto Scheiner, Heimo Breiteneder

Research output: Contribution to journalArticle

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 1.9 Å 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.

Original languageEnglish
Pages (from-to)123-133
Number of pages11
JournalJournal of Molecular Biology
Volume325
Issue number1
DOIs
Publication statusPublished - 2003

Fingerprint

Phytosterols
Betula
Brassinosteroids
Pollen
Allergens
Protein Isoforms
Deoxycholic Acid
Proteins
Mass Spectrometry
Plant Growth Regulators
Growth and Development
Ligands

Keywords

  • Birch pollen allergen
  • Brassinosteroid
  • Crystal structure
  • Plant pathogenesis-related proteins
  • Plant steroid carriers

ASJC Scopus subject areas

  • Virology

Cite this

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. / Marković-Housley, Zora; Degano, Massimo; Lamba, Doriano; Von Roepenack-Lahaye, Edda; Clemens, Stephan; Susani, Markus; Ferreira, Fátima; Scheiner, Otto; Breiteneder, Heimo.

In: Journal of Molecular Biology, Vol. 325, No. 1, 2003, p. 123-133.

Research output: Contribution to journalArticle

Marković-Housley, Z, Degano, M, Lamba, D, Von Roepenack-Lahaye, E, Clemens, S, Susani, M, Ferreira, F, Scheiner, O & Breiteneder, H 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', Journal of Molecular Biology, vol. 325, no. 1, pp. 123-133. https://doi.org/10.1016/S0022-2836(02)01197-X
Marković-Housley, Zora ; Degano, Massimo ; Lamba, Doriano ; Von Roepenack-Lahaye, Edda ; Clemens, Stephan ; Susani, Markus ; Ferreira, Fátima ; Scheiner, Otto ; Breiteneder, Heimo. / 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. 2003 ; Vol. 325, No. 1. pp. 123-133.
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AB - 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 1.9 Å 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.

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