Cross-reactivity within the profilin panallergen family investigated by comparison of recombinant profilins from pear (Pyr c 4), cherry (Pru av 4) and celery (Api g 4) with birch pollen profilin Bet v 2
S. Scheurer et al., Cross-reactivity within the profilin panallergen family investigated by comparison of recombinant profilins from pear (Pyr c 4), cherry (Pru av 4) and celery (Api g 4) with birch pollen profilin Bet v 2, J CHROMAT B, 756(1-2), 2001, pp. 315-325
Profilin is a panallergen which is recognised by IgE From about 20% of birc
h pollen- and plant food-allergic patients. Little is known about epitope d
iversity among these homologous proteins, and about the correlation between
IeE-cross-reactivity and allergenic reactivity. Plant food profilins from
pear (Pyr c 4) and cherry (Pru av 4) were cloned by polymerase chain reacti
on and produced in Escherichia coli BL21. The profilins were purified as no
n-fusion proteins by affinity chromatography on poly-(L-proline)-Sepharose
and characterized by immunoblotting, IgE-inhibition experiments and histami
ne release assays. The coding regions of the cDNA of pear and cherry profil
in were identified as a 393 bp open reading frame. The deduced amino acid s
equences showed high identities with birch pollen profilin Bet v 2 (76-83%)
and other allergenic plant profilins. Pyr c 4 and Pru av 4 were investigat
ed for their immunological properties in comparison with profilins from cel
ery (Api g 4) and birch pollen (Bet v 2). Forty-three of 49 patients (88%),
preselected for an IgE-reactivity with Bet v 2 showed specific IgE-antibod
ies to the recombinant pear protein, 92% of the sera were positive with the
recombinant cherry allergen and 80% of the sera were reactive with the cel
ery protein. Inhibition experiments showed a strong cross-reactivity of IgE
with profilins from plant food and birch pollen. However, IgE binding prof
iles also indicated the presence of epitope differences among related profi
lins. All investigated profilins, Pyr c 4, Pru av 4, Api g 4 and Bet v 2, p
resented almost identical allergenic properties in cellular mediator releas
e tests. Therefore, cross-reactivities between related profilins may explai
n pollen-related allergy to food in a minority of patients. The nucleotide
sequences reported have been submitted to the Genbank database under access
ion numbers AF129424 (Pyr c 4) and AF129425 (Pru av 4). (C) 2001 Elsevier S
cience B.V. All rights reserved.