Marco Caterino

Post-doctoral Research Fellow

Name Marco
Surname Caterino
Institution Università di Napoli Federico II
E-Mail marco.caterino@unina.it
Address Department of Pharmacy via D. Montesano, 49 80131 Naples, Italy
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Marco Caterino

Member PUBLICATIONS

  • High yield purification and first structural characterization of the full-length bacterial toxin CNF1.

    Publication Date: 01/01/2018 on Biotechnology progress
    by Colarusso A, Caterino M, Fabbri A, Fiorentini C, Vergara A, Sica F, Parrilli E, Tutino ML
    DOI: 10.1002/btpr.2574

    The Cytotoxic Necrotizing Factor 1 (CNF1) is a bacterial toxin secreted by certain Escherichia coli strains causing severe pathologies, making it a protein of pivotal interest in toxicology. In parallel, the CNF1 capability to influence important neuronal processes, like neuronal arborization, astrocytic support, and efficient ATP production, has been efficiently used in the treatment of neurological diseases, making it a promising candidate for therapy. Nonetheless, there are still some unsolved issues about the CNF1 mechanism of action and structuration probably caused by the difficulty to achieve sufficient amounts of the full-length protein for further studies. Here, we propose an efficient strategy for the production and purification of this toxin as a his-tagged recombinant protein from E. coli extracts (CNF1-H8). CNF1-H8 was expressed at the low temperature of 15°C to diminish its characteristic degradation. Then, its purification was achieved using an immobilized metal affinity chromatography (IMAC) and a size exclusion chromatography so as to collect up to 8 mg of protein per liter of culture in a highly pure form. Routine dynamic light scattering (DLS) experiments showed that the recombinant protein preparations were homogeneous and preserved this state for a long time. Furthermore, CNF1-H8 functionality was confirmed by testing its activity on purified RhoA and on HEp-2 cultured cells. Finally, a first structural characterization of the full-length toxin in terms of secondary structure and thermal stability was performed by circular dichroism (CD). These studies demonstrate that our system can be used to produce high quantities of pure recombinant protein for a detailed structural analysis. © 2017 American Institute of Chemical Engineers Biotechnol. Prog., 34:150-159, 2018.

  • Mapping the protein-binding sites for iridium(iii)-based CO-releasing molecules.

    Publication Date: 26/07/2016 on Dalton transactions (Cambridge, England : 2003)
    by Caterino M, Petruk AA, Vergara A, Ferraro G, Marasco D, Doctorovich F, Estrin DA, Merlino A
    DOI: 10.1039/c6dt01685e

    A combination of mass spectrometry, Raman microspectroscopy, circular dichroism and X-ray crystallography has been used to obtain detailed information on the reaction of an iridium-based CO-releasing molecule (Ir-CORM), Cs2IrCl5CO, with a model protein, bovine pancreatic ribonuclease. The results show that Ir-compound fragments bind to the N-terminal amine and close to histidine and methionine side chains, and the CO ligand is retained for a long time. The data provide helpful information for identifying protein targets for Ir-CORMs and for studying the mechanism that allows them to exhibit their interesting biological properties.

  • Missing gold atoms in lysozyme crystals used to grow gold nanoparticles.

    Publication Date: 01/04/2015 on Nature nanotechnology
    by Merlino A, Caterino M, Russo Krauss I, Vergara A
    DOI: 10.1038/nnano.2015.53