当前位置： SCI文献检索 > BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS期刊下所有文献 > High-level expression in Escherichia coli and purification of recombinant plant profilins: comparison of IgE-binding capacity and allergenic activity.

High-level expression in Escherichia coli and purification of recombinant plant profilins: comparison of IgE-binding capacity and allergenic activity.

Abstract：

:Because of their structural similarity and ubiquitous distribution as actin binding proteins, plant profilins represent important cross-reactive allergens for almost 20% of patients suffering from Type I allergy to pollen and other plant products. The cDNAs coding for three birch profilin variants (Tyr44, Glu47, and Asn47), timothy grass profilin, and three tobacco profilin isoforms (ntprof1-3) were expressed at high levels in Escherichia coli as non-fusion proteins. The recombinant plant profilins were purified to homogeneity by poly (L-proline) affinity chromatography and showed comparable capacity to bind IgE-antibodies from profilin allergic patients. All recombinant plant profilins elicited dose-dependent histamine release from basophils of a profilin allergic patient and induced immediate type skin reactions. It is concluded that profilins from different plant species share IgE-epitopes and allergenic properties. Plant profilins therefore constitute a family of functional pan-allergens which may substitute each other for diagnosis and specific immunotherapy.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Vrtala S,Wiedemann P,Mittermann I,Eichler HG,Sperr WR,Valent P,Kraft D,Valenta R

doi

10.1006/bbrc.1996.1309

subject

Has Abstract

pub_date

1996-09-04 00:00:00

pages

42-50

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(96)91309-1

journal_volume

226

pub_type

杂志文章

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