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Originally published as Genetics Published Articles Ahead of Print on September 12, 2005.
Genetics, Vol. 171, 1847-1859, December 2005, Copyright © 2005
doi:10.1534/genetics.105.045435
The Evolution of Antifungal Peptides in Drosophila
Francis M. Jiggins1 and Kang-Wook Kim
Institute of Evolutionary Biology, University of Edinburgh, Edinburgh EH9 3JT, Scotland
1 Corresponding author: Institute of Evolutionary Biology, School of Biological Sciences, University of Edinburgh, Ashworth Lab, King's Bldgs., West Mains Rd., Edinburgh EH9 3JT, Scotland.
E-mail: francis.jiggins{at}ed.ac.uk
An essential component of the immune system of animals is the production of antimicrobial peptides (AMPs). In vertebrates and termites the protein sequence of some AMPs evolves rapidly under positive selection, suggesting that they may be coevolving with pathogens. However, antibacterial peptides in Drosophila tend to be highly conserved. We have inferred the selection pressures acting on Drosophila antifungal peptides (drosomycins) from both the divergence of drosomycin genes within and between five species of Drosophila and polymorphism data from Drosophila simulans and D. melanogaster. In common with Drosophila antibacterial peptides, there is no evidence of adaptive protein evolution in any of the drosomycin genes, suggesting that they do not coevolve with pathogens. It is possible that this reflects a lack of specific fungal and bacterial parasites in Drosophila populations. The polymorphism data from both species differed from neutrality at one locus, but this was not associated with changes in the protein sequence. The synonymous site diversity was greater in D. simulans than in D. melanogaster, but the diversity both upstream of the genes and at nonsynonymous sites was similar. This can be explained if both upstream and nonsynonymous mutations are slightly deleterious and are removed more effectively from D. simulans due to its larger effective population size.
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