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Trends Microbiol. 2008 Aug;16(8):353-60. doi: 10.1016/j.tim.2008.05.007. Epub 2008 Jul 16.

Did cathelicidins, a family of multifunctional host-defense peptides, arise from a cysteine protease inhibitor?

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  • 1Group of Animal Innate Immunity, State Key Laboratory of Integrated Management of Pest Insects & Rodents, Institute of Zoology, Chinese Academy of Sciences, Beijing 100101, People's Republic of China.


Cystatins, the cysteine protease inhibitors, and the cathelin-like domain (CLD) of the antimicrobial cathelicidins are classified into the same superfamily because of their overall structural similarity. However, their evolutionary relationship has remained obscure owing to low sequence similarity. Structural similarity of two proteins often provides evidence for divergent evolution; however, structural convergence can not be completely ruled out in this case. Conserved gene structure and related function provide new evidence in favor of a common ancestral origin for cystatins and CLDs. On the basis of two observations, the C-terminal location of the cathelicidin antimicrobial domain and evolutionary gain of one 3' intron, I propose a gradual evolution model to explain how the AMD evolved from the ancestral cystatin scaffold.

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