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Coauthors
Peter Mergaert Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, University Paris‐Sud, Université Paris‐Saclay, France
1 protocol

Mick Bourge Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, University Paris‐Sud, Université Paris‐Saclay, France
1 protocol

Olivier Pierre Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, University Paris‐Sud, Université Paris‐Saclay, France
1 protocol

Giulia Runti Department of Life Sciences, University of Trieste, Italy
1 protocol

Marco Scocchi
  • Department of Life Sciences, University of Trieste, Italy
  • 1 Author merit

Education

Ph.D in Biochemistry, Departement  of Medical Sciences, University of Udine, 2000

Current Position

Professor  in Biochemistry, Department of Life Sciences, University of Trieste, Italy

Publications (since 2007)

  1. Xhindoli, D., Pacor, S., Benincasa, M., Scocchi, M., Gennaro, R. and Tossi, A. (2016). The human cathelicidin LL-37--A pore-forming antibacterial peptide and host-cell modulator. Biochim Biophys Acta 1858(3): 546-566.
  2. Seefeldt, A. C., Graf, M., Perebaskine, N., Nguyen, F., Arenz, S., Mardirossian, M., Scocchi, M., Wilson, D. N. and Innis, C. A. (2016). Structure of the mammalian antimicrobial peptide Bac7(1-16) bound within the exit tunnel of a bacterial ribosome. Nucleic Acids Res 44: 2429-2438.
  3. Scocchi, M., Mardirossian, M., Runti, G. and Benincasa, M. (2016). Non-Membrane Permeabilizing Modes of Action of Antimicrobial Peptides on Bacteria. Curr Top Med Chem 16(1): 76-88.
  4. Paulsen, V. S., Mardirossian, M., Blencke, H. M., Benincasa, M., Runti, G., Nepa, M., Haug, T., Stensvag, K. and Scocchi, M. (2016). Inner membrane proteins YgdD and SbmA are required for the complete susceptibility of E. coli to the proline-rich antimicrobial peptide arasin 1(1-25). Microbiology.
  5. Mardirossian, M., Pompilio, A., Crocetta, V., De Nicola, S., Guida, F., Degasperi, M., Gennaro, R., Di Bonaventura, G. and Scocchi, M. (2016). In vitro and in vivo evaluation of BMAP-derived peptides for the treatment of cystic fibrosis-related pulmonary infections. Amino Acids 48(9): 2253-2260.
  6. Guida, F., Benincasa, M., Zahariev, S., Scocchi, M., Berti, F., Gennaro, R. and Tossi, A. (2015). Effect of size and N-terminal residue characteristics on bacterial cell penetration and antibacterial activity of the proline-rich peptide Bac7. J Med Chem 58(3): 1195-1204.
  7. Bociek, K., Ferluga, S., Mardirossian, M., Benincasa, M., Tossi, A., Gennaro, R. and Scocchi, M. (2015). Lipopolysaccharide Phosphorylation by the WaaY Kinase Affects the Susceptibility of Escherichia coli to the Human Antimicrobial Peptide LL-37. J Biol Chem 290(32): 19933-19941.
  8. Benincasa, M., Zahariev, S., Pelillo, C., Milan, A., Gennaro, R. and Scocchi, M. (2015). PEGylation of the peptide Bac7(1-35) reduces renal clearance while retaining antibacterial activity and bacterial cell penetration capacity. Eur J Med Chem 95: 210-219.
  9. Pelillo, C., Benincasa, M., Scocchi, M., Gennaro, R., Tossi, A. and Pacor, S. (2014). Cellular internalization and cytotoxicity of the antimicrobial proline-rich peptide Bac7(1-35) in monocytes/macrophages, and its activity against phagocytosed Salmonella typhimurium. Protein Pept Lett 21(4): 382-390.
  10. Mattiuzzo, M., De Gobba, C., Runti, G., Mardirossian, M., Bandiera, A., Gennaro, R. and Scocchi, M. (2014). Proteolytic activity of Escherichia coli oligopeptidase B against proline-rich antimicrobial peptides. J Microbiol Biotechnol 24(2): 160-167.
  11. Mardirossian, M., Grzela, R., Giglione, C., Meinnel, T., Gennaro, R., Mergaert, P. and Scocchi, M. (2014). The host antimicrobial peptide Bac71-35 binds to bacterial ribosomal proteins and inhibits protein synthesis. Chem Biol 21(12): 1639-1647.
  12. Arnold, M. F., Caro-Hernandez, P., Tan, K., Runti, G., Wehmeier, S., Scocchi, M., Doerrler, W. T., Walker, G. C. and Ferguson, G. P. (2014). Enteric YaiW is a surface-exposed outer membrane lipoprotein that affects sensitivity to an antimicrobial peptide. J Bacteriol 196(2): 436-444.
  13. Runti, G., Lopez Ruiz Mdel, C., Stoilova, T., Hussain, R., Jennions, M., Choudhury, H. G., Benincasa, M., Gennaro, R., Beis, K. and Scocchi, M. (2013). Functional characterization of SbmA, a bacterial inner membrane transporter required for importing the antimicrobial peptide Bac7(1-35). J Bacteriol 195(23): 5343-5351.
  14. Paulsen, V. S., Blencke, H. M., Benincasa, M., Haug, T., Eksteen, J. J., Styrvold, O. B., Scocchi, M. and Stensvag, K. (2013). Structure-activity relationships of the antimicrobial peptide arasin 1 - and mode of action studies of the N-terminal, proline-rich region. PLoS One 8(1): e53326.
  15. Corbalan, N., Runti, G., Adler, C., Covaceuszach, S., Ford, R. C., Lamba, D., Beis, K., Scocchi, M. and Vincent, P. A. (2013). Functional and structural study of the dimeric inner membrane protein SbmA. J Bacteriol 195(23): 5352-5361.
  16. Arnold, M. F., Haag, A. F., Capewell, S., Boshoff, H. I., James, E. K., McDonald, R., Mair, I., Mitchell, A. M., Kerscher, B., Mitchell, T. J., Mergaert, P., Barry, C. E., 3rd, Scocchi, M., Zanda, M., Campopiano, D. J. and Ferguson, G. P. (2013). Partial complementation of Sinorhizobium meliloti bacA mutant phenotypes by the Mycobacterium tuberculosis BacA protein. J Bacteriol 195(2): 389-398.
  17. Tossi, A., Scocchi, M., Zahariev, S. and Gennaro, R. (2012). Use of unnatural amino acids to probe structure-activity relationships and mode-of-action of antimicrobial peptides. Methods Mol Biol 794: 169-183.
  18. Pompilio, A., Crocetta, V., Scocchi, M., Pomponio, S., Di Vincenzo, V., Mardirossian, M., Gherardi, G., Fiscarelli, E., Dicuonzo, G., Gennaro, R. and Di Bonaventura, G. (2012). Potential novel therapeutic strategies in cystic fibrosis: antimicrobial and anti-biofilm activity of natural and designed alpha-helical peptides against Staphylococcus aureus, Pseudomonas aeruginosa, and Stenotrophomonas maltophilia. BMC Microbiol 12: 145.
  19. Scocchi, M., Tossi, A. and Gennaro, R. (2011). Proline-rich antimicrobial peptides: converging to a non-lytic mechanism of action. Cell Mol Life Sci 68(13): 2317-2330.
  20. Pompilio, A., Scocchi, M., Pomponio, S., Guida, F., Di Primio, A., Fiscarelli, E., Gennaro, R. and Di Bonaventura, G. (2011). Antibacterial and anti-biofilm effects of cathelicidin peptides against pathogens isolated from cystic fibrosis patients. Peptides 32(9): 1807-1814.
  21. Wehmeier, S., Arnold, M. F., Marlow, V. L., Aouida, M., Myka, K. K., Fletcher, V., Benincasa, M., Scocchi, M., Ramotar, D. and Ferguson, G. P. (2010). Internalization of a thiazole-modified peptide in Sinorhizobium meliloti occurs by BacA-dependent and -independent mechanisms. Microbiology 156(Pt 9): 2702-2713.
  22. Tomasinsig, L., Benincasa, M., Scocchi, M., Skerlavaj, B., Tossi, A., Zanetti, M. and Gennaro, R. (2010). Role of Cathelicidin Peptides in Bovine Host Defense and Healing. Probiotics Antimicrob Proteins 2(1): 12-20.
  23. Padovan, L., Scocchi, M. and Tossi, A. (2010). Structural aspects of plant antimicrobial peptides. Curr Protein Pept Sci 11(3): 210-219.
  24. Karunakaran, R., Haag, A. F., East, A. K., Ramachandran, V. K., Prell, J., James, E. K., Scocchi, M., Ferguson, G. P. and Poole, P. S. (2010). BacA is essential for bacteroid development in nodules of galegoid, but not phaseoloid, legumes. J Bacteriol 192(11): 2920-2928.
  25. Benincasa, M., Pelillo, C., Zorzet, S., Garrovo, C., Biffi, S., Gennaro, R. and Scocchi, M. (2010). The proline-rich peptide Bac7(1-35) reduces mortality from Salmonella typhimurium in a mouse model of infection. BMC Microbiol 10: 178.
  26. Scocchi, M., Pallavicini, A., Salgaro, R., Bociek, K. and Gennaro, R. (2009). The salmonid cathelicidins: a gene family with highly varied C-terminal antimicrobial domains. Comp Biochem Physiol B Biochem Mol Biol 152(4): 376-381.
  27. Marlow, V. L., Haag, A. F., Kobayashi, H., Fletcher, V., Scocchi, M., Walker, G. C. and Ferguson, G. P. (2009). Essential role for the BacA protein in the uptake of a truncated eukaryotic peptide in Sinorhizobium meliloti. J Bacteriol 191(5): 1519-1527.
  28. Benincasa, M., Pacor, S., Gennaro, R. and Scocchi, M. (2009). Rapid and reliable detection of antimicrobial peptide penetration into gram-negative bacteria based on fluorescence quenching. Antimicrob Agents Chemother 53(8): 3501-3504.
  29. Scocchi, M., Mattiuzzo, M., Benincasa, M., Antcheva, N., Tossi, A. and Gennaro, R. (2008). Investigating the mode of action of proline-rich antimicrobial peptides using a genetic approach: a tool to identify new bacterial targets amenable to the design of novel antibiotics. Methods Mol Biol 494: 161-176.
  30. Mattiuzzo, M., Bandiera, A., Gennaro, R., Benincasa, M., Pacor, S., Antcheva, N. and Scocchi, M. (2007). Role of the Escherichia coli SbmA in the antimicrobial activity of proline-rich peptides. Mol Microbiol 66(1): 151-163.
1 Protocol published
Single Cell Flow Cytometry Assay for Peptide Uptake by Bacteria
Antimicrobial peptides (AMPs) can target the bacterial envelope or alternatively have intracellular targets. The latter requires uptake of the peptide by the bacterial cells. The bacterial internalization of an AMP can be evaluated by a ...