Highly sensitive quenched fluorescent substrate of Legionella major secretory protein (msp) based on its structural analysis.

ABSTRACT: Legionella pneumophila has been shown to secrete a protease termed major secretory protein (Msp). This protease belongs to the M4 family of metalloproteases and shares 62.9% sequence similarity with pseudolysin (EC 3.4.24.26). With the aim of developing a specific enzymatic assay for the detection and quantification of Msp, the Fluofast substrate library was screened using both enzymes in parallel. Moreover, based on the crystal structure of pseudolysin, a model of the Msp structure was built. Screening of the peptide library identified a lead substrate specifically cleaved by Msp that was subsequently optimized by rational design. The proposed model for Msp is consistent with the enzymatic characteristics of the studied peptide substrates and provides new structural information useful for

SUBMITTER: Poras H 

PROVIDER: S-EPMC3370204 | biostudies-literature | 2012 Jun

REPOSITORIES: biostudies-literature