|
|
||||||||
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Molecular & Cellular Proteomics 5:2252-2262, 2006.
© 2006 by The American Society for Biochemistry and Molecular Biology, Inc.


From the UBC Centre for Proteomics, Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia V6T 1Z4, Canada
The honeybee, Apis mellifera, is an invaluable partner in agriculture around the world both for its production of honey and, more importantly, for its role in pollination. Honeybees are largely unexplored at the molecular level despite a long and distinguished career as a model organism for understanding social behavior. Like other eusocial insects, honeybees can be divided into several castes: the queen (fertile female), workers (sterile females), and drones (males). Each caste has different energetic and metabolic requirements, and each differs in its susceptibility to pathogens, many of which have evolved to take advantage of the close social network inside a colony. Hemolymph, arthropods equivalent to blood, distributes nutrients throughout the bee, and the immune components contained within it form one of the primary lines of defense against invading microorganisms. In this study we have applied qualitative and quantitative proteomics to gain a better understanding of honeybee hemolymph and how it varies among the castes and during development. We found large differences in hemolymph protein composition, especially between larval and adult stage bees and between male and female castes but even between adult workers and queens. We also provide experimental evidence for the expression of several unannotated honeybee genes and for the detection of biomarkers of a viral infection. Our data provide an initial molecular picture of honeybee hemolymph, to a greater depth than previous studies in other insects, and will pave the way for future biochemical studies of innate immunity in this animal.
A Michael Smith Foundation Scholar and the Canada Research Chair in Organelle Proteomics. To whom correspondence should be addressed. Tel.: 604-822-8311; Fax: 604-822-2114; E-mail: ljfoster{at}interchange.ubc.ca
![]()
CiteULike
Complore
Connotea
Del.icio.us
Digg
Reddit
Technorati What's this?
This article has been cited by other articles:
![]() |
M. C. M. Kwok, J. M. Holopainen, L. L. Molday, L. J. Foster, and R. S. Molday Proteomics of Photoreceptor Outer Segments Identifies a Subset of SNARE and Rab Proteins Implicated in Membrane Vesicle Trafficking and Fusion Mol. Cell. Proteomics, June 1, 2008; 7(6): 1053 - 1066. [Abstract] [Full Text] [PDF] |
||||
![]() |
P. C. McDonald, A. Oloumi, J. Mills, I. Dobreva, M. Maidan, V. Gray, E. D. Wederell, M. B. Bally, L. J. Foster, and S. Dedhar Rictor and Integrin-Linked Kinase Interact and Regulate Akt Phosphorylation and Cancer Cell Survival Cancer Res., March 15, 2008; 68(6): 1618 - 1624. [Abstract] [Full Text] [PDF] |
||||
![]() |
A. B. Fielding, I. Dobreva, P. C. McDonald, L. J. Foster, and S. Dedhar Integrin-linked kinase localizes to the centrosome and regulates mitotic spindle organization J. Cell Biol., February 25, 2008; 180(4): 681 - 689. [Abstract] [Full Text] [PDF] |
||||
![]() |
K. P. Karunakaran, J. Rey-Ladino, N. Stoynov, K. Berg, C. Shen, X. Jiang, B. R. Gabel, H. Yu, L. J. Foster, and R. C. Brunham Immunoproteomic Discovery of Novel T Cell Antigens from the Obligate Intracellular Pathogen Chlamydia J. Immunol., February 15, 2008; 180(4): 2459 - 2465. [Abstract] [Full Text] [PDF] |
||||
![]() |
L. D. Rogers and L. J. Foster The dynamic phagosomal proteome and the contribution of the endoplasmic reticulum PNAS, November 20, 2007; 104(47): 18520 - 18525. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Journal of Biological Chemistry |
| Journal of Lipid Research | ASBMB Today |