Distinct epitope structures of defensin-like proteins linked to proline-rich regions give rise to differences in their allergenic activity.

ABSTRACT:

Background

Art v 1, Amb a 4, and Par h 1 are allergenic defensin-polyproline-linked proteins present in mugwort, ragweed, and feverfew pollen, respectively. We aimed to investigate the physicochemical and immunological features underlying the different allergenic capacities of those allergens.

Methods

Recombinant defensin-polyproline-linked proteins were expressed in E. coli and physicochemically characterized in detail regarding identity, secondary structure, and aggregation status. Allergenic activity was assessed by mediator releases assay, serum IgE reactivity, and IgE inhibition ELISA using sera of patients from Austria, Canada, and Korea. Endolysosomal protein degradation and T-cell cross-reactivity were studied in vitro.

Results

Despite variations in the prolin

SUBMITTER: Pablos I 

PROVIDER: S-EPMC5771466 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature