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Proteomic analysis of the honey bee worker venom gland focusing on the mechanisms of protection against tissue damage

Nico Peiren, Dirk de Graaf UGent, Frank Vanrobaeys, Ellen Danneels UGent, Bart Devreese UGent, Jozef Van Beeumen UGent and Franciscus Jacobs UGent (2008) Toxicon. 52(1). p.72-83
abstract
Honey bee workers use venom for the defence of the colony and themselves when they are exposed to dangers and predators. It is produced by a long thin, convoluted, and bifurcated gland, and consists of several toxic proteins and peptides. The present study was undertaken in order to identify the mechanisms that protect the venom gland secretory cells against these harmful components. Samples of whole venom glands, including the interconnected reservoirs, were separated by two-dimensional gel electrophoresis and the most abundant protein spots were subjected to mass spectrometric identification using MALDI TOF/TOF-MS and LC MS/MS. This proteomic study revealed four antioxidant enzymes: CuZn superoxide dismutase (SOD1), glutathione-S-transferase sigma 1 isoform A (GSTS1), peroxiredoxin 2540 (PXR2540) and thioredoxin peroxidase I isoform A (TPX1). Although glutathione-S-transferase (GST) has also been associated with xenobiotic detoxification, the protein we found belongs to the GST Sigma class which is known to protect against oxidative stress only. Moreover, we could demonstrate that the GST and SOD activity of the venom gland was low and moderate, respectively, when compared to other tissues from the adult honey bee. Several proteins involved in other forms of stress were likewise found but it remains uncertain what their function is in the venom gland. In addition to major royal jelly protein 9 (MRJP9), already found in a previous proteomic study, we identified MRJP8 as second member of the MRJP protein family to be associated with the venom gland. Transcripts of both MRJPs were amplified and sequenced. Two endocuticular structural proteins were abundantly present in the 2D-gel and most probably represent a structural component of the epicuticular lining that protects the secretory cells from the toxins they produce.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
journal title
Toxicon
volume
52
issue
1
pages
72 - 83
Web of Science type
Article
Web of Science id
000258816500009
JCR category
TOXICOLOGY
JCR impact factor
2.46 (2008)
JCR rank
27/74 (2008)
JCR quartile
2 (2008)
ISSN
0041-0101
DOI
10.1016/j.toxicon.2008.05.003
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
594756
handle
http://hdl.handle.net/1854/LU-594756
date created
2009-04-16 13:37:04
date last changed
2009-04-22 12:11:59
@article{594756,
  abstract     = {Honey bee workers use venom for the defence of the colony and themselves when they are exposed to dangers and predators. It is produced by a long thin, convoluted, and bifurcated gland, and consists of several toxic proteins and peptides. The present study was undertaken in order to identify the mechanisms that protect the venom gland secretory cells against these harmful components. Samples of whole venom glands, including the interconnected reservoirs, were separated by two-dimensional gel electrophoresis and the most abundant protein spots were subjected to mass spectrometric identification using MALDI TOF/TOF-MS and LC MS/MS. This proteomic study revealed four antioxidant enzymes: CuZn superoxide dismutase (SOD1), glutathione-S-transferase sigma 1 isoform A (GSTS1), peroxiredoxin 2540 (PXR2540) and thioredoxin peroxidase I isoform A (TPX1). Although glutathione-S-transferase (GST) has also been associated with xenobiotic detoxification, the protein we found belongs to the GST Sigma class which is known to protect against oxidative stress only. Moreover, we could demonstrate that the GST and SOD activity of the venom gland was low and moderate, respectively, when compared to other tissues from the adult honey bee. Several proteins involved in other forms of stress were likewise found but it remains uncertain what their function is in the venom gland. In addition to major royal jelly protein 9 (MRJP9), already found in a previous proteomic study, we identified MRJP8 as second member of the MRJP protein family to be associated with the venom gland. Transcripts of both MRJPs were amplified and sequenced. Two endocuticular structural proteins were abundantly present in the 2D-gel and most probably represent a structural component of the epicuticular lining that protects the secretory cells from the toxins they produce.},
  author       = {Peiren, Nico and de Graaf, Dirk and Vanrobaeys, Frank and Danneels, Ellen and Devreese, Bart and Van Beeumen, Jozef and Jacobs, Franciscus},
  issn         = {0041-0101},
  journal      = {Toxicon},
  language     = {eng},
  number       = {1},
  pages        = {72--83},
  title        = {Proteomic analysis of the honey bee worker venom gland focusing on the mechanisms of protection against tissue damage},
  url          = {http://dx.doi.org/10.1016/j.toxicon.2008.05.003},
  volume       = {52},
  year         = {2008},
}

Chicago
Peiren, Nico, Dirk de Graaf, Frank Vanrobaeys, Ellen Danneels, Bart Devreese, Jozef Van Beeumen, and Franciscus Jacobs. 2008. “Proteomic Analysis of the Honey Bee Worker Venom Gland Focusing on the Mechanisms of Protection Against Tissue Damage.” Toxicon 52 (1): 72–83.
APA
Peiren, N., de Graaf, D., Vanrobaeys, F., Danneels, E., Devreese, B., Van Beeumen, J., & Jacobs, F. (2008). Proteomic analysis of the honey bee worker venom gland focusing on the mechanisms of protection against tissue damage. Toxicon, 52(1), 72–83.
Vancouver
1.
Peiren N, de Graaf D, Vanrobaeys F, Danneels E, Devreese B, Van Beeumen J, et al. Proteomic analysis of the honey bee worker venom gland focusing on the mechanisms of protection against tissue damage. Toxicon. 2008;52(1):72–83.
MLA
Peiren, Nico, Dirk de Graaf, Frank Vanrobaeys, et al. “Proteomic Analysis of the Honey Bee Worker Venom Gland Focusing on the Mechanisms of Protection Against Tissue Damage.” Toxicon 52.1 (2008): 72–83. Print.