Copyright (c) 2016 AJC
This work is licensed under a Creative Commons Attribution 4.0 International License.
Effects of Varroa destructor Anderson & Trueman Infestation on Antioxidant Enzymes of Adult Worker Honey Bee (Apis mellifera L.)
Corresponding Author(s) : Yasar Gülmez
Asian Journal of Chemistry,
Vol. 28 No. 3 (2016): Vol 28 Issue 3
Abstract
One of the most important honeybee pathogens is the mite Varroa destructor, which threats honeybee health and incomes from bee keeping. Varroa mite, among other effects, can cause oxidative stress which is indicated by alterations in antioxidant enzyme activity and total protein levels. In this study, activities of catalase, glutathione S-transferase, superoxide dismutase enzymes and quantity of total protein levels were compared in mite infested and mite-free adult worker bees. Superoxide dismutase enzyme activity remarkably increased in mite infested bees as compared to uninfested ones. Catalase enzyme activity was found low in mite infested bees although no significant difference was observed in glutathione S-transferase enzyme activity. Total protein level in mite infested bees was detected lower than uninfested ones. Changes in enzyme activities and total protein levels are resulted from oxidative stress caused by mite infestation.
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- T.C. Webster and K.S. Delaplane, Dadant and Sons, Inc., 280 pp, Hamilton, Illinois (2001).
- M.L. Reshi, Y.C. Su and J.-R. Hong, Int. J. Cell Biol., Article ID 467452 (2014); doi:10.1155/2014/467452.
- K. Żóltowska, P. Grochla and E. Łopieńska-Biernat, Ann. Parasitol., 52, 283 (2006).
- K. Rahman, Clin. Interv. Aging, 2, 219 (2007).
- G.F. Weirich, A.M. Collins and V.P. Williams, Apidologie (Celle), 33, 3 (2002); doi:10.1051/apido:2001001.
- A.M. Korayem, M.M. Khodairy, A. Abdel-Aal and A.A.M. El-Sonbaty, J. Biol. Earth Sci., 2, B93 (2012).
- A.M. Collins, V. Williams and J.D. Evans, Insect Mol. Biol., 13, 141 (2004); doi:10.1111/j.0962-1075.2004.00469.x.
- T. Kayis, I. Emre and M. Coskun, Turkish J. Entomol., 36, 463 (2012).
- P. Badotra, N.R. Kumar and K. Harjai, J. Global Biosci., 2, 199 (2013).
- Z. Lipinski and K. Zoltowska, J. Apic. Res., 44, 126 (2005).
- W.F. Beyer Jr. and I. Fridovich, Anal. Biochem., 161, 559 (1987); doi:10.1016/0003-2697(87)90489-1.
- H. Aebi, Methods Enzymol., 105, 121 (1984); doi:10.1016/S0076-6879(84)05016-3.
- W. Habig, H. Pabst and M.K. Jakoby, J. Biochem., 249, 7130 (1974).
- J. Bradford, Anal. Biochem., 72, 248 (1976); doi:10.1016/0003-2697(76)90527-3.
- A.J. Nappi, E. Vass, F. Frey and Y. Carton, Eur. J. Cell Biol., 68, 450 (1995).
- M.M.A. Whitten, C.B. Mello, S.A.O. Gomes, Y. Nigam, P. Azambuja, E.S. Garcia and N.A. Ratcliffe, Exp. Parasitol., 98, 44 (2001); doi:10.1006/expr.2001.4615.
- N. Krishnan and D. Kodrík, J. Insect Physiol., 52, 11 (2006); doi:10.1016/j.jinsphys.2005.08.009.
- Y. Kono and I. Fridovich, J. Biol. Chem., 257, 5751 (1982).
- S. Ahmad, D.L. Duval, L.C. Weinhold and R.S. Pardini, Insect Biochem., 21, 563 (1991); doi:10.1016/0020-1790(91)90111-Q.
- C.M. Mathews, C.B. Summers and G.W. Felton, Arch. Insect Biochem. Physiol., 34, 57 (1997); doi:10.1002/(SICI)1520-6327(1997)34:1<57::AID-ARCH5>3.0.CO;2-T.
- C.B. Summers and G.W. Felton, Biochim. Biophys. Acta, 1156, 235 (1993); doi:10.1016/0304-4165(93)90142-U.
- J. Hemingway, N.J. Hawkes, L. McCarroll and H. Ranson, Insect Biochem. Mol. Biol., 34, 653 (2004); doi:10.1016/j.ibmb.2004.03.018.
- P.T. Bowen-Walker and A. Gunn, Entomol. Exp. Appl., 101, 207 (2001); doi:10.1046/j.1570-7458.2001.00905.x.
- C. van Dooremalen, E. Stam, L. Gerritsen, B. Cornelissen, J. van der Steen, F. van Langevelde and T. Blacquiere, J. Insect Physiol., 59, 487 (2013); doi:10.1016/j.jinsphys.2013.02.006.
References
T.C. Webster and K.S. Delaplane, Dadant and Sons, Inc., 280 pp, Hamilton, Illinois (2001).
M.L. Reshi, Y.C. Su and J.-R. Hong, Int. J. Cell Biol., Article ID 467452 (2014); doi:10.1155/2014/467452.
K. Żóltowska, P. Grochla and E. Łopieńska-Biernat, Ann. Parasitol., 52, 283 (2006).
K. Rahman, Clin. Interv. Aging, 2, 219 (2007).
G.F. Weirich, A.M. Collins and V.P. Williams, Apidologie (Celle), 33, 3 (2002); doi:10.1051/apido:2001001.
A.M. Korayem, M.M. Khodairy, A. Abdel-Aal and A.A.M. El-Sonbaty, J. Biol. Earth Sci., 2, B93 (2012).
A.M. Collins, V. Williams and J.D. Evans, Insect Mol. Biol., 13, 141 (2004); doi:10.1111/j.0962-1075.2004.00469.x.
T. Kayis, I. Emre and M. Coskun, Turkish J. Entomol., 36, 463 (2012).
P. Badotra, N.R. Kumar and K. Harjai, J. Global Biosci., 2, 199 (2013).
Z. Lipinski and K. Zoltowska, J. Apic. Res., 44, 126 (2005).
W.F. Beyer Jr. and I. Fridovich, Anal. Biochem., 161, 559 (1987); doi:10.1016/0003-2697(87)90489-1.
H. Aebi, Methods Enzymol., 105, 121 (1984); doi:10.1016/S0076-6879(84)05016-3.
W. Habig, H. Pabst and M.K. Jakoby, J. Biochem., 249, 7130 (1974).
J. Bradford, Anal. Biochem., 72, 248 (1976); doi:10.1016/0003-2697(76)90527-3.
A.J. Nappi, E. Vass, F. Frey and Y. Carton, Eur. J. Cell Biol., 68, 450 (1995).
M.M.A. Whitten, C.B. Mello, S.A.O. Gomes, Y. Nigam, P. Azambuja, E.S. Garcia and N.A. Ratcliffe, Exp. Parasitol., 98, 44 (2001); doi:10.1006/expr.2001.4615.
N. Krishnan and D. Kodrík, J. Insect Physiol., 52, 11 (2006); doi:10.1016/j.jinsphys.2005.08.009.
Y. Kono and I. Fridovich, J. Biol. Chem., 257, 5751 (1982).
S. Ahmad, D.L. Duval, L.C. Weinhold and R.S. Pardini, Insect Biochem., 21, 563 (1991); doi:10.1016/0020-1790(91)90111-Q.
C.M. Mathews, C.B. Summers and G.W. Felton, Arch. Insect Biochem. Physiol., 34, 57 (1997); doi:10.1002/(SICI)1520-6327(1997)34:1<57::AID-ARCH5>3.0.CO;2-T.
C.B. Summers and G.W. Felton, Biochim. Biophys. Acta, 1156, 235 (1993); doi:10.1016/0304-4165(93)90142-U.
J. Hemingway, N.J. Hawkes, L. McCarroll and H. Ranson, Insect Biochem. Mol. Biol., 34, 653 (2004); doi:10.1016/j.ibmb.2004.03.018.
P.T. Bowen-Walker and A. Gunn, Entomol. Exp. Appl., 101, 207 (2001); doi:10.1046/j.1570-7458.2001.00905.x.
C. van Dooremalen, E. Stam, L. Gerritsen, B. Cornelissen, J. van der Steen, F. van Langevelde and T. Blacquiere, J. Insect Physiol., 59, 487 (2013); doi:10.1016/j.jinsphys.2013.02.006.