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Renato Brandimarti

Ricercatore confermato

Dipartimento di Farmacia e Biotecnologie

Curriculum vitae

Scarica Curriculum Vitae (.pdf 245KB )

Education

University of Bologna, Italy, Science Dr, 1988, Biology

University of Bologna, Italy, PhD, 1993, Cell Biology and Physiology

University of Chicago, IL, USA, Postdoc, 1993-1999, Molecular Virology

Positions, Scientific Appointments and Honors

Positions and Employment

1993-1995 University of Chicago, Chicago, IL. Dept. of Molecular Genetics and Cellular Biology.

Research Associate (AIDS Research Fellow)

1995-1998 University of Chicago, Chicago, IL. Dept. of Molecular Genetics and Cellular Biology.

Research Associate

1998-1999 University of Chicago, Chicago, IL. Dept. of Molecular Genetics and Cellular Biology.

Research Associate-Instructor

1999-present University of Bologna, Italy. Department of Experimental Pathology - Department of Pharmacy and Biotechnology,

Assistant Professor

2001-present Drexel University College of Medicine (formerly MCP-Hahnemann University), Philadelphia PA

Department of Pharmacology and Physiology, Visiting Researcher

2011-2014 University of Bologna, Italy. Member of the Academic Senate.

Teaching

Since 1999, I’ve been teaching in different Programs at the University of Bologna.

URL to teaching activity at the University of Bologna: https://www.unibo.it/sitoweb/renato.brandimarti/didattica

Contribution to science

My interest in understanding the effects and the molecular basis of the several functional changes associated with Alzheimer's Disease (AD) and AD-Related Dementias (ADRD) developed over several years of research. This specific focus did not diverge from previous activities that were more oriented on investigating signaling mechanisms in the Central Nervous System (CNS), and on defining the contribution of individual viral proteins on the infectious process. Indeed, beside providing solid technical and rational basis, these different efforts well integrate into a research strategy that takes advantage of these complimentary perspectives.

  1. Control of AD-related proteins behavior through repurposed US9-based molecular tools.

    HSV is a neurotropic virus able to establish a life-long latency in the nervous system. This specific property requires specialized functionalities that can support an effective transport of the virion inside the long neuronal processes. We contributed to establish the viral protein US9 as the HSV anterograde transport protein in axons. Furthermore, we were able to demonstrate that US9 transport properties were not dependent on other viral functions, and that it could be loaded with functional cargos that would localize in specific subcellular compartments. Finally, we showed that by modifying US9 with APP-related proteins, APP processing and AD-related proteins can be altered. This research establishes US9 as a novel tool to study AD-related molecular changes and possibly identify individual steps leading to the disease.

    1. Brandimarti R, Irollo E, Meucci O. The US9-Derived Protein gPTB9TM Modulates APP Processing Without Targeting Secretase Activities. Mol. Neurobiol. 2023; Apr;60(4):1811-1825. doi: 10.1007/s12035-022-03153-2. PMID: 36576708 PMCID: PMC9984340
    2. Brandimarti R, Hill GS, Geiger JD, Meucci O. The lipid raft-dwelling protein US9 can be manipulated to target APP compartmentalization, APP processing, and neurodegenerative disease pathogenesis. Sci Rep. 2017; 7(1):15103. doi: 10.1038/s41598-017-15128-8.
    3. Pedrazzi M, Nash B, Meucci O, Brandimarti R. Molecular features contributing to virus-independent intracellular localization and dynamic behavior of the herpesvirus transport protein US9. PLoS One. 2014; 9(8):e104634. doi: 10.1371/journal.pone.0104634.
    4. LaVail JH, Tauscher AN, Sucher A, Harrabi O, Brandimarti R. Viral regulation of the long distance axonal transport of herpes simplex virus nucleocapsid. Neuroscience. 2007; 146(3):974-85.
  2. Interplay between chemokine signaling and cell-cycle proteins in the brain

    Neurons are post-mitotic cells, with cell-cycle proteins not expected to play a canonical role. Our interest in defining the effect that chemokines, namely CXCL12, have in neurons brought us to investigate changes induced by the presence of the chemokine. This series of studies contributed to our understanding of the neuroprotective activity of CXCL12 and its importance for neuronal survival and function, also providing some details on the induced molecular changes.

    1. Khan MZ, Brandimarti R, Shimizu S, Nicolai J, Crowe E, Meucci O.The chemokine CXCL12 promotes survival of postmitotic neurons by regulating Rb protein. Cell Death Differ. 2008. 15(10):1663-72.
    2. KHAN MZ, SHIMIZU S, PATEL JP, NELSON A, LE MT, MULLEN-PRZEWORSKI A, BRANDIMARTI R, FATATIS A, MEUCCI O. Regulation of neuronal P53 activity by CXCR 4.
      Mol Cell Neurosci. 2005;30(1):58-66.

    3. Khan, M.Z., Brandimarti, R., Patel, J., HUYNH,N., WANG, J.,HUANG, Z., FATATIS, A., and MEUCCI, O. Apoptotic and Antiapoptotic Effects of CXCR4: Is It a Matter of Intrinsic Efficacy? Implications for HIV Neuropathogenesis. AIDS Research and Human Retroviruses. 2004; 20(10): 1063-71.
    4. BRANDIMARTI, R., KHAN, M.Z., MUSSER, B.J., RESUE, D.M., FATATIS, A., and O.MEUCCI. Regulation of celle cycle proteins by chemokine receptors: a novel pathway in HIV pathogenesis? J Neurovirol. 2004;10 Suppl 1:108-12.
    5. KHAN, M.Z., BRANDIMARTI, R., MUSSER, B.J., RESUE, D.M., FATATIS, A., and O. MEUCCI. The chemokine receptor CXCR4 regulates cell cycle proteins in neurons. J Neurovirol. Jun;9(3):300-14. 2003.
  3. Role of viral proteins in the HSV infectious cycle

HSV is a large DNA virus that impacts cellular functionalities at several stages during its replication cycle. Our studies significantly contributed to the understanding of the initial steps of the infection, providing findings that allowed the identification of the individual role played by viral proteins present on the HSV envelope in the attachment and penetration steps. Furthermore, we studied the fine tuning of cellular protein synthesis during viral infection. These studies were instrumental in defining the role played by specific viral proteins in establishing a productive viral infection, and are essential part of the rational background for the design and generation of oncolytic viruses currently used.

  1. HE, B., CHOU, J., BRANDIMARTI, R., MOHR, J., GLUZMAN, Y., and ROIZMAN, B. Suppression of the phenotype of γ134.5- herpes simplex virus 1: failure of activated RNA-dependent protein kinase to shut off protein synthesis is associated with a deletion in the domain of the a47 gene. J. Virol., 71:6049-54, 1997.
  2. BRANDIMARTI, R., HUANG, T., ROIZMAN, B., and CAMPADELLI FIUME, G., Mapping of Herpes Simplex Virus 1 genes with mutations which overcome host restrictions to infection. Proc. Natl. Acad. Sci. USA, 91:5406-5410, 1994.
  3. VAN GENDEREN, I.L., BRANDIMARTI, R., TORRISI, M.R., CAMPADELLI, G., and VAN MEER, G., The phospholipid composition of extracellular herpes simplex virions differs from that of host cell nuclei. Virology, 200:831-836, 1994.
  4. CAMPADELLI, G., BRANDIMARTI, R., DI LAZZARO, C., WARD, P.L., ROIZMAN, B., and TORRISI, R., Fragmentation and dispersal of Golgi proteins and redistribution of Glycoproteins and glycolipids processed through the Golgi apparatus after infection with herpes simplex virus. Proc. Natl. Acad. Sci. USA, 90:2798-2802, 1993.

 

Peer reviewed publications

Irollo, E., Nash, B., Luchetta, J. Brandimarti, R, Meucci, O. The Endolysosomal Transporter DMT1 is Required for Morphine Regulation of Neuronal Ferritin Heavy Chain. J Neuroimmune Pharmacol. 2023. 18, 495–508. https://doi-org.ezproxy.unibo.it/10.1007/s11481-023-10082-x

Brandimarti R, Irollo E, Meucci O. The US9-Derived Protein gPTB9TM Modulates APP Processing Without Targeting Secretase Activities. Mol. Neurobiol. 2023; Apr;60(4):1811-1825. doi: 10.1007/s12035-022-03153-2. PMID: 36576708 PMCID: PMC9984340

Nash B, Irollo E, Brandimarti R, Meucci O. Opioid Modulation of Neuronal Iron and Potential Contributions to NeuroHIV. Methods Mol Biol. 2021;2201:139-162. doi: 10.1007/978-1-0716-0884-5_13. PMID: 32975796; PMCID: PMC7641316.

Borsetti F, Dal Piaz F, D'Alessio F, Stefan A, Brandimarti R, Sarkar A, Datta A, Montón Silva A, den Blaauwen T, Alberto M, Spisni E, Hochkoeppler A. Manganese is a Deinococcus radiodurans growth limiting factor in rich culture medium. Microbiology. 2018 164(10):1266-1275. doi: 10.1099/mic.0.000698.

Brandimarti R, Hill GS, Geiger JD, Meucci O. The lipid raft-dwelling protein US9 can be manipulated to target APP compartmentalization, APP processing, and neurodegenerative disease pathogenesis. Sci Rep. 2017; 7(1):15103. doi: 10.1038/s41598-017-15128-8.

Lapenta F, Montón Silva A, Brandimarti R, Lanzi M, Gratani FL, Vellosillo Gonzalez P, Perticarari S, Hochkoeppler A. Escherichia coli DnaE Polymerase Couples Pyrophosphatase Activity to DNA Replication. PLoS One. 2016; 11(4):e0152915. doi: 10.1371/journal.pone.0152915

Pedrazzi M, Nash B, Meucci O, Brandimarti R. Molecular features contributing to virus-independent intracellular localization and dynamic behavior of the herpesvirus transport protein US9. PLoS One. 2014; 9(8):e104634. doi: 10.1371/journal.pone.0104634.

Khan MZ, Brandimarti R, Shimizu S, Nicolai J, Crowe E, Meucci O.The chemokine CXCL12 promotes survival of postmitotic neurons by regulating Rb protein. Cell Death Differ. 2008. 15(10):1663-72.

LaVail JH, Tauscher AN, Sucher A, Harrabi O, Brandimarti R. Viral regulation of the long distance axonal transport of herpes simplex virus nucleocapsid. Neuroscience. 2007; 146(3):974-85.

Khan MZ, Shimizu S, Patel JP, Nelson A, Le MT, Mullen-Przeworski A, Brandimarti R, Fatatis A, Meucci O. Regulation of neuronal P53 activity by CXCR 4.
Mol Cell Neurosci. 2005;30(1):58-66.

Khan, M.Z., Brandimarti, R., Patel, J., HUYNH,N., WANG, J.,HUANG, Z., FATATIS, A., and MEUCCI, O. Apoptotic and Antiapoptotic Effects of CXCR4: Is It a Matter of Intrinsic Efficacy? Implications for HIV Neuropathogenesis. AIDS Research and Human Retroviruses. 2004; 20(10): 1063-71.

BRANDIMARTI, R., KHAN, M.Z., MUSSER, B.J., RESUE, D.M., FATATIS, A., and O.MEUCCI. Regulation of celle cycle proteins by chemokine receptors: a novel pathway in HIV pathogenesis? J Neurovirol. 2004;10 Suppl 1:108-12. .

KHAN, M.Z., BRANDIMARTI, R., MUSSER, B.J., RESUE, D.M., FATATIS, A., and O. MEUCCI. The chemokine receptor CXCR4 regulates cell cycle proteins in neurons. J Neurovirol. Jun;9(3):300-14. 2003.

GALVAN, V., BRANDIMARTI, R., MUNGER, J., and B. ROIZMAN. Bcl-2 blocks a caspase-dependent pathway of apoptosis activated by herpes simplex virus 1 infection in HEp-2 cells. J Virol. 74:1931-8, 2000.

ADVANI, S.J., BRANDIMARTI, R., WEICHSELBAUM, R.R., and B. ROIZMAN. The disappearance of cyclins A and B and the increase in activity of the G(2)/M-phase cellular kinase cdc2 in herpes simplex virus 1-infected cells require expression of the alpha22/U(S)1.5 and U(L)13 viral genes. J Virol. 74:8-15, 2000.

GALVAN, V., BRANDIMARTI, R., and B. ROIZMAN. Herpes simplex virus 1 blocks caspase-3-independent and caspase-dependent pathways to cell death. J Virol. 73:3219-26,1999.

BRANDIMARTI, R., and B. ROIZMAN. US9, a stable lysine-less herpes simplex virus 1 protein, is ubiquitinated prior to packaging into virions, and associates with proteasomes. Proc. Natl. Acad. Sci. USA, 94:13973-13978, 1997.

HE, B., CHOU, J., BRANDIMARTI, R., MOHR, J., GLUZMAN, Y., and ROIZMAN, B. Suppression of the phenotype of ã134.5- herpes simplex virus 1: failure of activated RNA-dependent protein kinase to shut off protein synthesis is associated with a deletion in the domain of the a47 gene. J. Virol., 71:6049-54, 1997.

BRANDIMARTI, R., HUANG, T., ROIZMAN, B., and CAMPADELLI FIUME, G., Mapping of Herpes Simplex Virus 1 genes with mutations which overcome host restrictions to infection. Proc. Natl. Acad. Sci. USA, 91:5406-5410, 1994.

VAN GENDEREN, I.L., BRANDIMARTI, R., TORRISI, M.R., CAMPADELLI, G., and VAN MEER, G., The phospholipid composition of extracellular herpes simplex virions differs from that of host cell nuclei. Virology, 200:831-836, 1994.

CAMPADELLI, G., BRANDIMARTI, R., DI LAZZARO, C., WARD, P.L., ROIZMAN, B., and TORRISI, R., Fragmentation and dispersal of Golgi proteins and redistribution of Glycoproteins and glycolipids processed through the Golgi apparatus after infection with herpes simplex virus. Proc. Natl. Acad. Sci. USA, 90:2798-2802, 1993.

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