Apimedica: Bee Venom Collected Directly from Venom Glands has Better Biological Activity, Lower Allergic Reaction than that Collected by Electrical Stimulation

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Apimondia Apimedica-Apiquality International Forum
Oct. 22-25, 2012Zhenjiang, ChinaProteome Comparison of Honeybee (Apis mellifera ligustica) WorkerVenom Between Directly Collected from Venom Glands and Electrical Stimulations
LI Rong-li, HAN Bin, FANG Yu, FENG Mao, LI Jian-ke(Institute of Apicultural Research, Chinese Academy ofAgricultural Sciences, Beijing 100093,China) Italian bee (Apis melliferaligustica) is the most important bees for the beekeeping industry of China. Understandingits venom composition is vital for the reasonable use of bee venom for thehuman health promotion. The proteome between the venom collected directly from thevenom glands and artificially electrical stimulations were compared usinggel-based (one-dimensional gel electrophoresis, 1-DE, two-dimensional gelelectrophoresis, 2-DE) and gel-free proteomics approaches, mass spectrometry,bioinformatics. Overall, 31 nonredundant proteins were identified in the venomcollected from the glands, which are mainly bee venom toxins, antioxidantsystem, protein folding, molecular transporters. In construct, only 15 nonredundantproteins were identified in the venom collected by electrical stimulation,which mainly contains bee venom toxins. Phospholipase A2-like protein was identifiedfirst time in two forms of venom and peptidyl-prolyl cis-trans isomerase wasidentified for the first time only in the venom directly collected from theglands. There were 17 differentially expressed proteins in two forms of venomwith higher abundance in the venom collected from the gland were proteinfolding, molecular transporters, antioxidant systems and part of the venomtoxins, such as melittin, apamin preproprotein, secapin, venom proteases andicarapin-like precursor. However, phospholipase A2, allergen Api m 6 and mast cell degranulatingpeptide had higher abundance in the venom collected by electrical stimulations.Our data suggests that the bee venom directly collected from venom glandspotentially has better biological activity and lower allergic reaction than theelectrical stimulations. The identified new proteins significantly increase theproteome coverage of the bee venom. This may provide theoretical basis for therational use of the honeybee venom.Key words: honeybee; venom; proteome; gel-electrophoresis;gel-freeæ„�大利工蜂毒腺内蜂毒与电å�–蜂毒蛋白质组比较æ�Žè�£ä¸½，韩 宾，房宇，冯 毛，æ�Žå»ºç§‘（中国农业科学院蜜蜂研究所，北京 100093，中国）【目的】æ„�大利蜜蜂（æ„�蜂）是我国饲养主è¦�蜂ç§�，探究其蜂毒组æˆ�æˆ�分将对å�ˆç�†åˆ©ç”¨å…·æœ‰é‡�è¦�æ„�义。【方法】采用å‡�胶电泳和é�žå‡�胶技术对直接从毒腺内å�–蜂毒和电å�–蜂毒的蛋白质组进行比较，对差异蛋白进行质谱分æž�、功能鉴定和生物信æ�¯å­¦åˆ†æž�。【结果】在毒腺蜂毒中，一维å‡�胶电泳（1-DE）鉴定20ç§�蛋白，å�Œå�‘å‡�胶电泳（2-DE）鉴定11 ç§�蛋白，é�žå‡�胶法鉴定15 ç§�蛋白，三ç§�方法在毒腺蜂毒中共鉴定31 ç§�é�žå†—余蛋白质，它们是蜂毒毒素æˆ�分、抗氧化、蛋白折å� 、分å­�转è¿�类等。在电å�–蜂毒中，1-DE鉴定13 ç§�蛋白，2-DE鉴定4 ç§�蛋白，é�žå‡�胶方法鉴定8 ç§�蛋白，三ç§�方法共鉴定15 ç§�é�žå†—余蛋白质，主è¦�是蜂毒毒素æˆ�分。其中类磷脂酶A2 是在2 ç§�蜂毒中首次鉴定，肽基辅氨酰顺å��异构酶是首次在毒腺蜂毒中å�‘现。毒腺蜂毒与电å�–蜂毒中差异蛋白为17ç§�，其中毒腺蜂毒å�«é‡�显著高于电å�–蜂毒的蛋白为蛋白折å� 、分å­�转è¿�ç±»、抗氧化类以å�Šèœ‚毒毒素æˆ�分中的蜂毒肽、蜂毒明肽、镇é�™è‚½、毒液蛋白酶、毒液ä¸�氨酸蛋白酶和icarapin-likeprecursor。电å�–蜂毒中å�«é‡�高于毒腺蜂毒的蛋白为蜂毒毒素æˆ�分中的磷脂酶A2、allergenApi m6和肥大细胞脱粒肽。【结论】毒腺蜂毒在功能æˆ�分的å�«é‡�上è¦�显著高于电å�–蜂毒，且过æ•�æº�物质低于电å�–蜂毒，说明毒腺内蜂毒比电å�–蜂毒ä¸�但具有更好的生物学活性而且具有更低的过æ•�å��应，æ–°å�‘现的蛋白是对蜂毒功能æˆ�分完善和补充，这将对蜂毒的å�ˆç�†åˆ©ç”¨æ��供一定ç�†è®ºä¾�æ�®。关键è¯�：æ„�大利蜜蜂；毒腺蜂毒；电å�–蜂毒；蛋白质组；é�žå‡�胶电泳；å‡�胶电泳