MURINE T-CELL AND B-CELL RESPONSES TO NATURAL AND RECOMBINANT HORNET VENOM ALLERGEN DOL-M-5.02 AND ITS RECOMBINANT FRAGMENTS

Citation
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
Citations number
40
Categorie Soggetti
Immunology
Journal title
The Journal of immunology
ISSN journal
00221767 → ACNP
Volume
154
Issue
2
Year of publication
1995
Pages
577 - 584
Database
ISI
SICI code
0022-1767(1995)154:2<577:MTABRT>2.0.ZU;2-F
Abstract
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.