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Cross‐reactivity between the major Parietaria allergen and rotavirus VP4 protein
Author(s) -
Di Somma C.,
Fiore L.,
Di Lonardo A.,
Ridolfi B.,
Garzillo C.,
Chersi A.,
Buono C.,
Menna T.,
Ruffilli A.
Publication year - 2003
Publication title -
allergy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.363
H-Index - 173
eISSN - 1398-9995
pISSN - 0105-4538
DOI - 10.1034/j.1398-9995.2003.00176.x
Subject(s) - cross reactivity , rotavirus , allergen , virology , antibody , immunology , immunoglobulin e , antigen , biology , recombinant dna , microbiology and biotechnology , virus , allergy , cross reactions , biochemistry , gene
Background: The present study investigates immunological cross‐reactivity between Par o 1, the major pollen allergen of Parietaria , and the VP4 protein of rotavirus, a microorganism that is world‐wide the main etiological agent of gastroenteritis in children. Methods: IgG and IgE cross‐reactivity was assessed by direct binding and competitive inhibition assays (ELISA and DARIA), using recombinant VP4 from rhesus infectious rotavirus (RR), synthetic peptides and Par o 1‐specific antibodies affinity purified from pooled and individual human sera. Results: Antibodies specifically binding Par o 1, affinity purified from the sera of 35 individuals with skin test positivity to Parietaria and from 14 pools, were extensively cross‐reactive with RRVP4. Cross‐reactive binding was specifically inhibited by synthetic peptides derived from the C‐terminal sequences of the VP4 proteins from human and rhesus infectious rotavirus. Conclusions: This study reports the first evidence of cross‐reactivity between an allergen and a viral antigen.