| Literature DB >> 850023 |
B R Paull, J W Yunginger, G J Gleich.
Abstract
The presence of serum IgE antibodies to melittin was tested by the radioallergosorbent test (RAST). Melittin, the principal protein of honeybee venom, was isolated by gel filtration on Sephadex G-75 and covalently bound to cyanogen bromide-activated microcrystalline cellulose. The melittin preparation was homogenous by immunoelectrophoresis with the use of rabbit antiserum to whole honeybee venom and by polyacrylamide electrophoresis in gels containing 1% sodium dodecyl sulfate. Elevated serum IgE antibodies to melittin (three times greater than binding by normal sera) were found in 7 of 24 honeybee venom-sensitive persons and in 5 of 20 nonsensitive beekeepers. In one venom-sensitive patient a particularly high titer of IgE antibody was found. The reaction between solid-phase melittin and IgE antibody could be inhibited by fluid-phase melittin but not by phospholipase A (PLA). Similarly, the reaction of IgE antibody with solid-phase PLA was inhibited by PLA but not by melittin. In passive transfer skin tests with the sensitive patient's serum, positive wheal-and-flare reactions were obtained in 3 nonallergic recipients following melittin challenge; appropriate controls were negative. These results indicate that melittin is an allergen in some honeybee venom-sensitive patients and in an occasional patient melittin may be a major allergen.Entities:
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Year: 1977 PMID: 850023 DOI: 10.1016/0091-6749(77)90056-2
Source DB: PubMed Journal: J Allergy Clin Immunol ISSN: 0091-6749 Impact factor: 10.793