The Journal of Proteolysis provides an international forum for the electronic publication of the whole spectrum of high-quality articles and reviews in all areas of proteolysis and proteolytic pathways.

The Journal of Proteolysis is committed to rigorous yet rapid reviewing. Final versions are published electronically immediately upon acceptance.

ISSN: 2331-6977

Article In Press: Peptide Sequence Region That is Essential for the Interactions of the Enterotoxigenic Bacteroides fragilis Metalloproteinase II with E-cadherin
Bacteroides fragilis is a valuable anaerobic commensal and an essential component of the gut microbiome in humans. The presence of a short pathogenicity island in the genome is predominantly associated with the enterotoxigenic strains of B. fragilis. Metalloproteinase II (MPII) and fragilysin (FRA) are the structurally related enzymes encoded by the pathogenicity island in the enterotoxigenic strains. Accordingly, there is a significant overlap between the cleavage preferences of MPII and FRA. These proteinases, however, are counter-transcribed in the bacterial genome suggesting their distinct and specialized functions in the course of infection. It is well established that FRA directly cleaves E-cadherin, a key protein of the cell-to-cell adhesion junctions in the intestinal epithelium. Counterintuitively, MPII directly binds to, rather than cleaves, E-cadherin. Structural modeling suggested that a potential E-cadherin binding site involves the C-terminal α-helical region of the MPII catalytic domain. The sequence of this region is different in MPII and FRA. Here, we employed substitution mutagenesis of this C-terminal α-helical region to isolate the MPII mutants with the potentially inactivated E-cadherin binding site. Overall, as a result of our modeling, mutagenesis and binding studies, we determined that the C-terminal ten residue segment is essential for the binding of MPII, but not of FRA3, to E-cadherin, and that the resulting MPII⋅E-cadherin complex does not impair E-cadherin-dependent cell-to-cell contacts. It is possible to envision that the putative cleavage targets of MPII should be explored not only on the host cell surface but also in B. fragilis.
Excellent tool for prediction of the potential cleavage sites for MMPs

Scientists of Sanford Burnham Medical Research Institute (La Jolla, CA, USA) recently announced the opening of a new web server providing excellent tool for prediction of the potential cleavage sites for matrix metalloproteinases (MMPs).

The server is capable to predict cleavage positions for 11 human MMPs: MMP-2, -3, -8, -9, -10, -14, -15, -16, -17, -24, -25, for which statistical profiles have been derived based on high throughput phage display experiments. The server accepts the structure data (in PDB format), the sequence data (in FASTA format) or UNIPROT id of putative protein target as an input and produces information about the position of tentative cleavage sites.

The server additionally provides other available information for your input protein:

  • Co-localization and co-expression of the input protein and its processing MMP
  • Positions of post-translational modifications (PTMs), and Single Nucleotide Polymorphism data (SNPs) that could interfere with the cleavage event (the information about the disease related SNPs is also provided if available)
  • Signal peptide and secondary structure, solvent exposure and transmembrane domain(s)
  • VMS - virtual mass spectroscopy (the server produces ordered mass spectrum of expected mass fragments based on the position of tentative cleavage position, which would be very helpful in interpreting experimental MS data).
  • Server matches the structure to your input protein sequence and displays potential cleavage sites, PTMs and SNPs mapped on this structure.

For more information please visit: But, if you have any specific questions or need more information, you can directly contact Dr. Piotr Cieplak by e-mail:


Call For PapersThe Journal of Proteolysis cordially invites researchers and principal investigators to submit high-quality, innovative and original research papers related to the field of proteolysis and proteolytic pathways. Submissions are accepted in the form of original papers, short communications and reviews.

Why publish in the Journal of Proteolysis?

  • Journal of Proteolysis provides a unique opportunity to publish novel insights and original works in the area of proteolysis and proteolytic pathways in highly specialized academic journal.
  • Open Access publishing option. All articles will be free to download for readers worldwide.
  • Low publication fee. Publication fees for regular research papers and short communications are minimal and one of the lowest in the row of bio-med oriented academic journals.
  • User-friendly electronic submission system. For manuscript submission guidelines please visit the guidelines for authors section on Information for Authors.
  • High-quality yet rapid peer review. The result of peer review for submitted papers will be provided approximately within one month after initial submission.
  • Fast Publication of accepted manuscripts. As soon as the final version of accepted paper is ready, it will immediately appear on the journal website and will be accessible for download.

We look forward to receiving your manuscripts

Journal of Proteolysis Editorial Office
Opening Issue

The Journal of Proteolysis is the open-access online-only journal. It announces the launch of its first issue at the beginning of 2014 and welcomes the original papers and high-quality contributions across the multidisciplinary scientific research of the entire spectrum of proteolysis, proteolytic events and pathways.


The Journal of Proteolysis topics:

  • Proteolytic pathways in cellular regulations
  • Post-translational proteolytic processing and protein degradation
  • Proteolytic events in diseases and proteomics studies
  • Characterization of viral, microbial, plant and mammalian proteinases
  • Proteinases in host-pathogen interactions
  • Natural proteinase inhibitors
  • Drug design studies of proteinases inhibitors
  • Proteinases and their inhibitors in medicine and medical applications
  • Tools, new methods and laboratory applications for scientific research in the area of proteolytic events and proteinases.
Vol 1, No 1 (2014)
Proteolysis and Proteolytic Pathways – Life After the Point of No Return 1-2
Proteolysis is the irreversible post-translational modification affecting a specific peptide bond in a target protein substrate.
Proteolysis Vol 1, No 1 (2014); doi:10.13176/14.609