Common peptide epitope in mumps virus nucleocapsid protein and MHC class II-associated invariant chain.

The present study describes a 7 amino acid-long sequence (YQQQGRL) which is identical in HLA-associated invariant chain and mumps virus nucleocapsid protein and is additionally followed by one conservative amino acid pair. As such a long amino acid homology is extremely rare in two evolutionarily unrelated proteins the possibility that it could induce immunological cross-reactivity was evaluated. Several antigenicity indices suggested high antigen potential within this region. Synthetic peptides containing this sequence were reactive with 31% of monoclonal antibodies specific for mumps virus nucleocapsid protein in ELISA. High antibody levels against this epitope were found in 7% of mumps-seropositive human sera and antibody levels clearly increased after natural mumps infections and mumps vaccinations. Rabbit antibodies raised against a synthetic invariant chain peptide AYF-LYQQQGRLDKL-C reacted with corresponding nucleocapsid peptide RFAKYQQQGRLEAR-C and antibodies against the nucleocapsid peptide reacted with the invariant chain peptide. Rabbit antibodies against the invariant chain peptide also reacted with nucleocapsid molecules in formaldehyde-fixed mumps virus-infected cells, and antibodies against the nucleocapsid peptide reacted with invariant chains expressed in methanol-fixed cells. One monoclonal antibody specific for the nucleocapsid molecule also reacted with cells expressing invariant chains. In immunoprecipitation rabbit antibodies against the invariant chain peptide bound to invariant chains while antibodies against the nucleocapsid peptide did not. The results suggest that there is antigenic similarity in mumps virus nucleocapsid molecule and HLA-associated invariant chain which may cause immunological cross-reactivity between these molecules.