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Proteomic Analysis Of Honeybee Venom

Posted on:2014-05-29Degree:MasterType:Thesis
Country:ChinaCandidate:R L LiFull Text:PDF
GTID:2250330401478805Subject:Farming
Abstract/Summary:PDF Full Text Request
Honeybee venom is a complicated defensive insect toxin and has a wide range of pharmacologicalapplications for human therapeutics. Apis mellifera ligustica is the most widely distributed honeybeearound the globe and is widely used by human. Apis cerana cerana is the native bees in China.Although there are significant different compositions of the venom between the different bee species,the gland venom (GV) and electrical stimulated venom (ESV), knowledge on which venom forms andbee species is more suitable for uilization are still lacking. The proteome of GV and ESV of A. m.ligustica were compared using gel-based (one-dimensional gel electrophoresis, two-dimensional gelelectrophoresis)and shotgun proteomics approaches. Of the44identified proteins in the GV and ESV ofA. m. ligustica,39showed significant different abundance. In GV, it contained more proteins than inESV, which63%proteins were related to antioxidant systems, protein folding and moleculartransporters and the others. On the other hand in ESV, most of the proteins were the bee venom toxins,in which the abundance of seven toxin proteins such as phospholipase A-2, hyaluronidase, venomdipeptidylpeptidase4, mast cell degranulating peptide, melittin, apamin and secapin were significanthigher or not lower than in GV. This suggests an evolutionary strategy of the honeybees involving in anefficient mechanism to defend and protect themselves and the colony. Given the ESV is convenient tobe harvested and contains the main pharmacological components, it is therefore the ESV is the moreeffective way for utilization as a medical resource. Four novel proteins (phospholipase A2-like, DnaJhomolog subfamily B member11-like, dehydrogenase/reductase SDR family member11-like andhistone H2B.3-like) and10phosphopeptides with8phosphorylated sites of three phosphoproteins wereidentified. The phophorylated venomic protein may strengthen the toxity of the venom in order to bebetter as chemical weapon. Lable-free proteomics analysis of the proteome of ESV of A. m. ligusticaand A. c. cerana showed that the venom of the former one contained more proteins than the later one.Of which the most toxins in A. m. ligustica were higher than in A. c. cerana. This is likely to be A. m.ligustica has developed a more efficient defense mechanisms than A. c. cerana that is shaped by theevolutionary process. To be used as a medical resource, the A. m. ligustica’s venom is more efficientthan the A. c. cerana. Our data provides vital knowledge for deep understanding of the bee venomcomposition and provides the theoretical and practical basis for future rational use of the honeybeevenom.
Keywords/Search Tags:Apis mellifera ligustica, Apis cerana cerana, venom, proteomic
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