Bacteroides fragilis causes the majority of anaerobic infections in humans. The presence of a pathogenicity island in the genome discriminates pathogenic and commensal B. fragilis strains. The island encodes metalloproteinase II (MPII), a potential virulence protein, and one of three homologous fragilysin isozymes (FRA; also termed B. fragilis toxin or BFT). Here, we report biochemical data on the structural-functional characteristics of the B. fragilis pathogenicity island proteases by reporting the crystal structure of MPII at 2.13 Å resolution, combined with detailed characterization of the cleavage preferences of MPII and FRA3 (as a representative of the FRA isoforms), identified using a high-throughput peptide cleavage assay with 18 583 substrate peptides. We suggest that the evolution of the MPII catalytic domain can be traced to human and archaebacterial proteinases, whereas the prodomain fold is a feature specific to MPII and FRA. We conclude that the catalytic domain of both MPII and FRA3 evolved differently relative to the prodomain, and that the prodomain evolved specifically to fit the B. fragilis pathogenicity. Overall, our data provide insights into the evolution of cleavage specificity and activation mechanisms in the virulent metalloproteinases.
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http://dx.doi.org/10.1111/febs.12804 | DOI Listing |
Int J Mol Sci
December 2024
Department of Health Sciences, Università Del Piemonte Orientale, 28100 Novara, Italy.
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View Article and Find Full Text PDFGenes (Basel)
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Division of Anaerobe Research, Life Science Research Center, Gifu University, Gifu City 501-1194, Gifu, Japan.
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Service de Parasitologie-Mycologie, CHU Clermont-Ferrand, Clermont-Ferrand, France.
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Division of Epidemiology & Biostatistics, University of Illinois Chicago School of Public Health, Chicago, USA.
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View Article and Find Full Text PDFMar Pollut Bull
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Biomedical Research Center, Qatar University, P.O. Box 2713, Doha, Qatar. Electronic address:
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