Cross-reactivity between the major Parietaria allergen and rotavirus VP4 protein.
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.
di Somma
C
C
Institute of Genetics and Biophysics Adriano Buzzati Traverso, CNR, Naples, Italy.
Fiore
L
L
Di Lonardo
A
A
Ridolfi
B
B
Garzillo
C
C
Chersi
A
A
Buono
C
C
Menna
T
T
Ruffilli
A
A
D000485:Allergens / Q000276:immunology*; D000906:Antibodies / Q000276:immunology; D036022:Capsid Proteins / Q000276:immunology*; D003429:Cross Reactions / Q000187:drug effects; D004797:Enzyme-Linked Immunosorbent Assay; D006801:Humans; D007073:Immunoglobulin E / Q000276:immunology; D007074:Immunoglobulin G / Q000276:immunology; D010455:Peptides / Q000494:pharmacology; D010940:Plant Proteins / Q000276:immunology*; D011863:Radioimmunoassay / Q000379:methods
D000485:Allergens; D000906:Antibodies; D036022:Capsid Proteins; D007074:Immunoglobulin G; C072038:Par o I protein, Parietaria officinalis; D010455:Peptides; D010940:Plant Proteins; C060339:VP4 protein, Rotavirus; D007073:Immunoglobulin E