Anno2015
AutoriValeria Longo, Maria Assunta Costa, Fabio Cibella, Giuseppina Cuttitta, Stefania La Grutta, Paolo Colombo
AbstractThe interaction between IgE antibodies and allergens is a key event in triggering an allergic reaction. The
characterization of this region provides information of paramount importance for diagnosis and therapy.
Par j 2 Lipid Transfer Protein is one of the most important allergens in southern Europe and a wellestablished marker of sensitization in Parietaria pollen allergy. The main aim of this study was to map the
IgE binding regions of this allergen and to study the pattern of reactivity of individual Parietaria-allergic
patients. By means of gene fragmentation, six overlapping peptides were expressed in Escherichia coli, and
their IgE binding activity was evaluated by immunoblotting in a cohort of 79 Parietaria-allergic patients.
Our results showed that Pj-allergic patients display a heterogeneous pattern of IgE binding to the different
recombinant fragments, and that patients reacted simultaneously against several protein domains spread
all the over the molecule, even in fragments which do not contain structural features resembling the
native allergen. Our results reveal the presence of a large number of linear and conformational epitopes
on the Par j 2 sequence, which probably explains the high allergenic activity of this allergen
RivistaMolecular Immunology
ISSN0161-5890
Impact factor0
Volume63
Pagina inizio412
Pagina fine419
Autori IBFMaria Assunta COSTA
Linee di Ricerca IBFMD.P01.002.001
Sedi IBFIBF.PA