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Detection of seminal fluid proteins in the bed bug, Cimex lectularius, using two-dimensional gel electrophoresis and mass spectrometry

Published online by Cambridge University Press:  18 December 2008

K. REINHARDT*
Affiliation:
University of Sheffield, Department of Animal and Plant Sciences, Western Bank, SheffieldS10 2TN, UK
C. H. WONG
Affiliation:
University of Sheffield, Academic Unit of Reproductive and Developmental Medicine, The Jessop Wing, Tree Root Walk, SheffieldS10 2SF, UK
A. S. GEORGIOU
Affiliation:
University of Sheffield, Academic Unit of Reproductive and Developmental Medicine, The Jessop Wing, Tree Root Walk, SheffieldS10 2SF, UK
*
*Corresponding author: University of Sheffield, Department of Animal and Plant Sciences, Western Bank, Sheffield S10 2TN, UK. Tel: +44 114 222 4778. Fax: +44 114 222 0002. E-mail: k.reinhardt@sheffield.ac.uk

Summary

The global increase of the human parasite, the common bed bug Cimex lectularius, calls for specific pest control target sites. The bed bug is also a model species for sexual conflict theory which suggests that seminal fluids may be highly diverse. The species has a highly unusual sperm biology and seminal proteins may have unique functions. One-dimensional PAGE gels showed 40–50% band sharing between C. lectularius and another cimicid species, Afrocimex constrictus. However, adult, sexually rested C. lectularius males were found to store 5–7 μg of seminal protein and with only 60 μg of protein we obtained informative 2-D PAGE gels. These showed 79% shared protein spots between 2 laboratory populations, and more than half of the shared protein spots were detected in the mated female. Further analysis using liquid chromatography electrospray ionization tandem mass spectrometry revealed that 26·5% of the proteins had matches among arthropods in databases and 14·5% matched Drosophila proteins. These included ubiquitous proteins but also those more closely associated with reproduction such as moj 29, ubiquitin, the stress-related elongation factor EF-1alpha, a protein disulfide isomerase and an antioxidant, Peroxiredoxin 6.

Type
Research Article
Copyright
Copyright © 2008 Cambridge University Press

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