Adaptive evolution in subterranean termite antifungal peptides.
We identified and analysed mRNA sequences of two immune proteins from the subterranean termites Reticulitermes flavipes and Reticulitermes virginicus. These proteins correspond to two immune proteins described in the distantly related termite genus Nasutitermes; termicin, which is a small antifungal peptide, and GNBP2, which functions both as a broad pattern recognition receptor and a direct antifungal effector. A population genetic analysis of nucleotide intraspecific polymorphism and interspecific divergence indicates that a selective sweep has reduced polymorphism in the termicins. Moreover, this selective sweep appears to have been driven by the positive selection of beneficial amino acid changes in the antifungal peptide. In contrast, the pattern of polymorphism and divergence in GNBP2 corresponds to the standard neutral model of evolution.
Bulmer
M S
MS
Department of Biological Sciences, Towson University, Towson, MD21252, USA. mbulmer@towson.edu
Lay
F
F
Hamilton
C
C
D019943:Amino Acid Substitution; D000818:Animals; D023181:Antimicrobial Cationic Peptides; D019143:Evolution, Molecular; D043326:Glucan 1,3-beta-Glucosidase / Q000276:immunology*; D054884:Host-Pathogen Interactions; D020049:Isoptera / Q000235:genetics* / Q000276:immunology* / Q000502:physiology; D008969:Molecular Sequence Data; D010455:Peptides / Q000276:immunology*; D011110:Polymorphism, Genetic; D012333:RNA, Messenger / Q000276:immunology; D017423:Sequence Analysis, RNA
D023181:Antimicrobial Cationic Peptides; D010455:Peptides; D012333:RNA, Messenger; C428304:termicin; D043326:Glucan 1,3-beta-Glucosidase