Acinetobacter baumannii (A. baumannii) is an amorphous gram-negative pathogenic bacterium which is highly resistant to antibiotics. As part of its pathogenesis, it secretes proteases to establish infection. One of these proteases is the prolyl oligopeptidase family protein 2 (POP2), which is part of the abhydrolase superfamily. The POP2 protease has features of a typical serine protease and a conserved Asp-His-Ser catalytic triad, although not in the traditional order. In addition to its protease activity, POP2 also exhibits lipase activity and has the possibility of multiple active sites. We have cloned the POP2 gene by PCR amplification out of A. baumannii genomic DNA and have expressed and purified the protein from E. coli. We are testing its activity and specificity for certain protein sequences that are found in antibodies. By further characterizing this protease, we hope to learn its recognition sequence and mechanism of action to further explore this protein’s biochemical properties. This information could be used to potentially alter its resistant effects, making A. baumannii infections easier to control.

Prolyl oligopeptidase family protein 2 (POP2): A protease with a taste for antibodies

255th National Meeting (2018)

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