[1] Alim M.A., Tsuji N., Miyoshi T., Islam M.K., Hugang X., Hatta T., Fujisaki K. 2008. H1Lgm2, a member of asparaginyl endopeptidases/legumains in the mitgut of the ixodid tick Haemaphysalis longicornis, is involved in blood-meal digestion. Journal of Insect Physiology, 54, 573–585. DOI: 10.1016/j.jinsphys.2007.12.006. http://dx.doi.org/10.1016/j.jinsphys.2007.12.006CrossrefWeb of ScienceGoogle Scholar
[2] Anderson D.L., Trueman J.W.H. 2000. Varroa jacobsoni (Acari: Varroidae) is more than one species. Experimental and Applied Acarology, 24, 165–189. DOI: 10.1023/A:1006456720416. http://dx.doi.org/10.1023/A:1006456720416CrossrefGoogle Scholar
[3] Bania J., Polanowski A. 1999. Bioinsekticides and insect defense mechanisms. Postępy Biochemii, 45, 143–149 [in Polish]. Google Scholar
[4] Bania J., Stachowik D., Polanowski A. 1999. Primary structure and properties of the cathepsin G/chymotrypsin inhibitor from the larval hemolymph of Apis mellifera. European Journal of Biochemistry, 262, 680–687. DOI: 10.1046/j.1432-1327.1999.00406.x. http://dx.doi.org/10.1046/j.1432-1327.1999.00406.xCrossrefGoogle Scholar
[5] Cerenius L., Kawabata S., Lee B.L., Nonaka M., Söberhäll K. 2010. Proteolytic cascades and their involvement in invertebrate immunity. Trends in Biochemical Sciences, 35, 575–583.DOI: 10.1016/j.tibs.2010.04.006. http://dx.doi.org/10.1016/j.tibs.2010.04.006CrossrefWeb of ScienceGoogle Scholar
[6] Chan Q.W.T., Howes CH.G., Foster L.J. 2006. Quantitative composition of caste differences in honeybee hemolymph. Molecular and Cellular Proteomics, 5, 2252–2262.DOI: 10.1074/mcp.M600197-MCP200. http://dx.doi.org/10.1074/mcp.M600197-MCP200CrossrefGoogle Scholar
[7] Cicero J.M., Sammataro D. 2010. The salivary glands of adult female Varroa destructor (Acari, Varroidae), an ectoparasite of the honey bee, Apis mellifera (Hymenoptera, Apidae). International Journal of Acarology, 36, 377–386. DOI: 10.1080/0164795100475796. http://dx.doi.org/10.1080/01647951003757961CrossrefWeb of ScienceGoogle Scholar
[8] Cierpicki T., Bania J., Otlewski J. 2000. NMR solution structure of Apis mellifera chymotrypsin/cathepsin G inhibitor-1 (AMCI-1), Structural similarity with Ascaris protease inhibitor. Protein Science, 9, 976–984. DOI: 10.1110/ps.9.5.976. http://dx.doi.org/10.1110/ps.9.5.976CrossrefGoogle Scholar
[9] Felicioli A., Donadio E., Balestreri E., Montagnoli G., Felicioli R., Podesta A. 2004. Expression profile of water-soluble proteinases during ontogenesis of Megachile rotundata, an electrophoretic investigation. Apidologie, 35, 595–604. DOI: 10.1051/apido:2004064. http://dx.doi.org/10.1051/apido:2004064CrossrefGoogle Scholar
[10] Frączek R., Żółtowska K., Lipiński Z. 2009. The activity of nineteen hydrolases in extracts from Varroa destructor and hemolymph of Apis mellifera carnica. Journal of Apicultural Science, 53, 42–51. Google Scholar
[11] Frączek R., Żółtowska K., Lipiński Z., Dmitryjuk M. 2012. Proteolytic activity In the extracts and In the excretory/secretory products from Varroa destructor parasitic mite of honeybee. International Journal of Acarology, 38, 101–109. DOI: 10.1080/01647954.2011.610357. http://dx.doi.org/10.1080/01647954.2011.610357Web of ScienceCrossrefGoogle Scholar
[12] Genersch E. 2010. Honey bee pathology, current threats to honey bees and beekeeping. Applied Microbiology and Biotechnology, 87, 87–97. DOI: 10.1007/s00253-010-2573-8. http://dx.doi.org/10.1007/s00253-010-2573-8Web of ScienceCrossrefGoogle Scholar
[13] Grzywnowicz K., Ciołek A., Tabor A., Jaszek M. 2009. Profiles of the body-surface proteolytic system of honey bee queens, workers and drones. Ontogenetic and seasonal changes in proteases and their natural inhibitors. Apidologie, 40, 4–19. DOI: 10.1051/apido:2008057. CrossrefWeb of ScienceGoogle Scholar
[14] Küster F.W., Thiel A. 1993. Rechentafeln für die chemische Analytik. Walter de Gruyter, Berlin — NY. ISBN — 311012131X. Google Scholar
[15] Liao M., Zhou J., Gong H., Boldbaatar D., Shirafuji R., Battur B., Nishikawa Y., Fujisaki K. 2009. Hemlin, a thrombin inhibitor isolated from a midgut cDNA library from the hard tick Haemaphsalis longicormis. Journal of Insect Physiology, 55, 165–174. DOI: 10.1016/j.jinsphys.2008.11.004. http://dx.doi.org/10.1016/j.jinsphys.2008.11.004Web of ScienceCrossrefGoogle Scholar
[16] Lowry O.H., Rosenbrough N.J., Farr A.R., Randall K.J. 1951. Protein measurement with the Folin phenol-reagent. Journal of Biological Chemistry, 193, 265–275. Google Scholar
[17] Maritz-Olivier C., Stutzer C., Jongejan F., Neitz A.W.H., Gaspar A.R.D. 2007. Tick anti-haemostatic’s, targets for future vaccines and therapeutics. Trends Parasitology, 23, 397–407. http://dx.doi.org/10.1016/j.pt.2007.07.005Web of ScienceGoogle Scholar
[18] Mendiola J., Alonso M., Marquetti M.C., Finlay C. 1996. Boophilus microplus, multiple proteolytic activities in the midgut. Experimental Parasitology, 82, 27–33. http://dx.doi.org/10.1006/expr.1996.0004Google Scholar
[19] Muta T., Iwanaga S. 1998. The role of hemolymph coagulation in innate immunity. Current Opinion in Immunology, 8, 41–47. http://dx.doi.org/10.1016/S0952-7915(96)80103-8Google Scholar
[20] Richards E.H., Jones B., Bowman A. 2011. Salivary secretions from the honeybee mite Varroa destructor, effects on insect haemocytes and preliminary biochemical characterization. Parasitology, 138, 602–608. DOI: 10.107/S0031182011000072. http://dx.doi.org/10.1017/S0031182011000072Web of ScienceGoogle Scholar
[21] Rosenkranz P., Aumeier P., Ziegelmann B. 2010. Biology and control of Varroa destructor. Journal of Invertebrate Pathology, 103, S96–S119. DOI: 10.1016/j.jip.2009.07.016. http://dx.doi.org/10.1016/j.jip.2009.07.016Web of ScienceCrossrefGoogle Scholar
[22] Strachecka A., Grzywnowicz K. 2008. Activity of protease inhibitors on the body surface of the honeybee. Medycyna Weterynaryjna, 64, 1256–1259 [in Polish]. Google Scholar
[23] Tewarson N.C., Jany K.D. 1982. Determination of proteolysis activity in Varroa jacobsoni an ectoparasitic hemophagous mite of honey bees (Apis sp.). Apidologie, 13, 383–389. http://dx.doi.org/10.1051/apido:19820405Google Scholar
[24] Uriel J., Berges J. 1968. Characterization of natural inhibitors of trypsin and chymotrypsin by electrophoresis In acrylamideagarose gels. Nature, 218, 578–580. DOI: 10.1038/218578b0. http://dx.doi.org/10.1038/218578b0CrossrefGoogle Scholar
[25] Vilcinskas A. 2010. Coevolution between pathogen-derived proteinases and proteinase inhibitors of host insects. Virulence, 1, 206–214. DOI: 10.4161/viru.1.3.12072. http://dx.doi.org/10.4161/viru.1.3.12072CrossrefWeb of ScienceGoogle Scholar
[26] Willadsen P., Riding G.A. 1980. On the biological role of a proteolytic-enzyme inhibitor from the ectoparasitic tick Boophilus microplus. Biochemical Journal, 189, 295–303. Google Scholar
[27] Zou Z., Lopez D.L., Kanost M.R., Evans J.D., Jiang H. 2006. Comparative analysis of serine protease-related genes in the honey bee genome, possible involvement in embryonic development and innate immunity. Insect Molecular Biology, 15, 603–614. DOI: 10.1111/j.1365-2583.2006.00684.x. http://dx.doi.org/10.1111/j.1365-2583.2006.00684.xCrossrefGoogle Scholar
Comments (0)