Tp. King et al., MURINE T-CELL AND B-CELL RESPONSES TO NATURAL AND RECOMBINANT HORNET VENOM ALLERGEN DOL-M-5.02 AND ITS RECOMBINANT FRAGMENTS, The Journal of immunology, 154(2), 1995, pp. 577-584
White-face hornet venom allergen, Dol m 5.02, is a protein of 204 amin
o acid residues. This protein and its overlapping fragments, of 53-114
residues in size, containing the N-terminal, middle, and C-terminal r
egions of the molecule, can be expressed in high yield in bacteria by
using the plasmid vector pQE12. Natural (n) and recombinant (r) Dol m
5.02s and the r-fragments are about equally immunogenic for IgG Ab res
ponse in BALB/c mice. n-Dol m 5.02 induces mainly murine IgG Abs speci
fic for its discontinuous B cell epitopes and, to a lesser extent, Abs
specific for its continuous epitopes. r-Dol m 5.02 and the r-fragment
s induce only Abs specific for continuous B cell epitopes that are com
mon with those of the n-protein. Abs specific for the discontinuous ep
itopes show higher affinity than those specific for the continuous epi
topes. r-Dol m 5.02 and the fragments are as efficient as n-Dol m 5.02
in inducing murine T cell responses specific for the n-protein. The d
ifferences in the immunogenicity of n- and r-proteins or r-peptide fra
gments for B and T cell responses are related to their conformations,
inasmuch as only the n-protein is cross-linked by four disulfide bonds
. These findings are relevant to the potential use of r-fragments as i
mmunotherapeutic reagents in humans.