Sequence identity and antigenic cross-reactivity of white face hornet venom allergen, also a hyaluronidase, with other proteins.

White face hornet (Dolichovespula maculata) venom has three known protein allergens which induce IgE response in susceptible people. They are antigen 5, phospholipase A1, and hyaluronidase, also known as Dol m 5, 1, and 2, respectively. We have cloned Dol m 2, a protein of 331 residues.

Murine T and B cell responses to natural and recombinant hornet venom allergen Dol m 5.02 and its recombinant fragments.

White-face hornet venom allergen, Dol m 5.02, is a protein of 204 amino acid residues. This protein and its overlapping fragments, of 53-114 residues in size, containing the N-terminal, middle, and C-terminal regions of the molecule, can be expressed in high yield in bacteria by using the plasmid vector pQE12.

Structure-immunogenicity relationship of melittin, its transposed analogues, and D-melittin.

Melittin, a 26-residue bee venom peptide, is known to induce murine Abs specific for its hydrophilic C-terminus of residues 20-26 and T cell responses specific for its hydrophobic mid-region of residue 11-19. Synthetic melittin analogues with transposed sequences of Ac(21-26) (1-20) and Ac(26-21) (1-20) are found to induce murine Abs specific for the transposed peptide segment and to induce T cell responses that are cross-reactive with melittin. Compared with melittin, the transposed melittin analogues are weaker immunogens and have lower hemolytic activities, lower helical contents, and a lower degree of association in micelles.

Structure-immunogenicity relationship of melittin and its N-terminal truncated analogs.

Melittin is an amphipathic 26-residue peptide from bee venom. We showed previously that, in the murine system, melittin has one major B-cell epitope in the hydrophilic region of residues 21-26 and one T-cell epitope in the hydrophobic midregion of 11-19. In this paper we compared the immunogenicity and the biophysical properties of a series of melittin analogs which differ by stepwise two-residue truncation in the N-terminus of residues 2-10.

Sequence similarity of a hornet (D. maculata) venom allergen phospholipase A1 with mammalian lipases.

We have determined the sequence of a venom allergen phospholipase A1 from white-faced hornet (Dolichovespula maculata) by cDNA and protein sequencings. This protein of 300 amino acid residues (Dol m I) has no sequence similarity with other known phospholipases. But it has sequence similarity with mammalian lipases; about 40% identity in overlaps of 123 residues.