Apis mellifera venom

Premier, C., Mach, L., Glossl, J. and Marz, L. (1992) The antigenicity of the carbohydrate moiety of an insect glycoprotein, honey-bee (Apis mellifera) venom phospholipase A2. The role of al,3-fucosylation of the asparagine-bound IV-acetylglucosamine. Bio chemicalJournal 284, 377-380. 

Melittins are peptides of 26 amino acids found in Apis venoms (119, 120). Melittin comprises about 40% to 50% of the dry weight of Apis mellifera venom. At moderate and high concentrations, it exists primarily in the form of tetramers (120, 121), which can be immunogenic and allergenic (123). Tetrameric melittin is a potent lytic agent for cells and can also function as an ion channel (124, 125, 126). Melittin has profound effects on intracellular calcium and interacts with calmodulin (127, 128, 129). It is an amphiphilic and amphipathic molecule that has been found to be very useful in studies of cell lysis, membrane function, calcium regulation and as a model for proteins and peptides. Natural and synthetic melittin have been used in over a 1000 published studies in many areas of science. 

Anionic peptides are almost inactive in the presence of serum because they have the disadvantage of binding to serum proteins. Amphiphilic basic peptides, such as melittin (GIGAVLKVLTTGLPALISWIKRKRQQ-NH2), isolated from the venom of the European honey bee Apis mellifera (Dempsey, 1990) and K5, the... 

Apidae Apis mellifera complex CHCs / venoms McDaniel et al., 1984... 

Bridges, A. R. (1977) Fine structure of the honey bee (Apis mellifera L.) venom gland and reservoir. A system for the secretion and storage of a naturally produced toxin. Micros, Soc, Can., 4, 50-1. 

Apamin was isolated from the venom of honey bee Apis mellifera and chemically modified derivatives of apamin were obtained as described(lO). 

Venoms of both bees and vespid wasps contain the enzyme hyaluronidase with an apparent molecular weight of about 42000 (55, 64, 65, 66, 67). The enzymes from bee and wasp are immunologically cross-reactive (65, 78, 79). The N-terminal regions of the molecules are quite similar among several species (79). The complete sequences of two venom hyaluronidases have been determined from cDNA clones, that of Apis mellifera (80) and Dolichovespula maculata (81). The honeybee venom enzyme has 350 amino acid residues and the hornet enzyme 331 and the sequences are 55.3% identical with many stretches of contiguous identical residues. Searches of the sequence databases showed that the venom hyaluronidases are related to a guinea pig sperm protein, PH-20 (80, 82, 83) involved in sperm-egg adhesion. Further studies have shown that similar proteins are found in all mammalian sperm and that they have hyaluronidase activity (83). 

Franca, F.O.S., Benvenutti, L.A., Fan, H.W., Dossantos, D.R., Hain, S.H., Picchi-martins, F.R., Cardoso, J.L.C., Kamiguti, A.S., Theakston, R.D., and Warrell, D.A., 1994, Severe and fatal mass attacks by killer bees (Africanized honeybees, Apis mellifera scutellata) in Brazil - Clinicopathological studies with measurements of serum venom concentrations. Quart. J. Med. 87 269-282. 

Melittin] (26 aa, 3 kDa, basic, Apis mellifica (mellifera) (bee venom) CaM antagonist [anti-rheumatic]... 

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