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A series of duplication events led to an expansion of clade B Serine Protease Inhibitors ( SERPIN ), currently displaying a large repertoire of functions in vertebrates. Accordingly, the recent duplicates  SERPINB3  and  B4  located in human 18q21.3  SERPIN  cluster control the activity of different cysteine and serine proteases, respectively. Here, we aim to assess SERPINB3 and B4 coevolution with their target proteases in order to understand the evolutionary forces shaping the accelerated divergence of these duplicates. Phylogenetic analysis of primate sequences placed the duplication event in a Hominoidae ancestor (∼30 Mya) and the emergence of  SERPINB3  in Homininae (∼9 Mya). We detected evidence of strong positive selection throughout  SERPINB4 / B3  primate tree and target proteases, cathepsin L2 ( CTSL2 ) and G ( CTSG ) and chymase ( CMA1 ). Specifically, in the Homininae clade a perfect match was observed between the adaptive evolution of  SERPINB3  and cathepsin S ( CTSS ) and most of sites under positive selection were located at the inhibitor/protease interface. Altogether our results seem to favour a coevolution hypothesis for  SERPINB3 ,  CTSS  and  CTSL2  and for  SERPINB4  and  CTSG  and  CMA1 . A scenario of an accelerated evolution driven by host-pathogen interactions is also possible since SERPINB3/B4 are potent inhibitors of exogenous proteases, released by infectious agents. Finally, similar patterns of expression and the sharing of many regulatory motifs suggest neofunctionalization as the best fitted model of the functional divergence of  SERPINB3  and  B4  duplicates.

Adaptive Evolution and Divergence of SERPINB3: A Young Duplicate in Great Apes