Anna Cereseto
e-mail: cereseto AT science.unitn.it
affiliation: University of Trento, CIBIO
research area(s): Molecular Biology, Immunity And Infection
Course:
Biomolecular Sciences
University/Istitution: Università di Trento
University/Istitution: Università di Trento
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HIV-1 is the causative agent of AIDS. An essential step in HIV-1 replication cycle is the integration of the viral DNA into the host cellular genome. Following viral entry only a small percentage of virions enter the nucleus and successfully integrate. Therefore, a critical step in HIV-1 life cycle is the translocation into the nucleus and a proper interaction with the nuclear structure to achieve a productive infection. Unraveling the mechanisms of HIV-nuclear interaction is important not only to better understand the biology of HIV-1 but also as groundwork for new therapeutic strategies.
Similar to other viruses, HIV-1 has a small genome and the virus takes advantage of cellular proteins to complete the different steps in its life cycle. Our group is interested in defining the multiple interactions between the virus and cellular components with particular reference to the nuclear compartment.
To reveal new details of the biology of HIV-1 the lab is integrating tools of molecular biology, virology cellular biology and advanced optical techniques. Our research activities are organized in two main groups:
One line of research exploits the state-of-the-art microscopy tools to analyze HIV-1 trafficking in live cells. The dynamic of HIV-1 is monitored in the nuclei of infected cells to delineate the movements of viral particles and the cellular molecules necessary for the virus to reach the final integration sites. Time -lapse experiments in infected cells allows monitoring interactions of the viral particles with cellular structures (e.g. nuclear pores, nuclear lamin, chromatin structures) along the replication cycle.
A second major interest of the Group is unraveling the molecular determinants of viral integration in the host cell genome. We study the viral enzyme that catalyzes the integration reaction, Integrase, in terms of its post-translational modifications (acetylation and phosphorylation) and protein-protein interactions with cellular factors. In this context newly identified cellular proteins binding to acetylated Integrase are currently evaluated for their role in protecting the cells from viral infectivity (restriction factors).
Similar to other viruses, HIV-1 has a small genome and the virus takes advantage of cellular proteins to complete the different steps in its life cycle. Our group is interested in defining the multiple interactions between the virus and cellular components with particular reference to the nuclear compartment.
To reveal new details of the biology of HIV-1 the lab is integrating tools of molecular biology, virology cellular biology and advanced optical techniques. Our research activities are organized in two main groups:
One line of research exploits the state-of-the-art microscopy tools to analyze HIV-1 trafficking in live cells. The dynamic of HIV-1 is monitored in the nuclei of infected cells to delineate the movements of viral particles and the cellular molecules necessary for the virus to reach the final integration sites. Time -lapse experiments in infected cells allows monitoring interactions of the viral particles with cellular structures (e.g. nuclear pores, nuclear lamin, chromatin structures) along the replication cycle.
A second major interest of the Group is unraveling the molecular determinants of viral integration in the host cell genome. We study the viral enzyme that catalyzes the integration reaction, Integrase, in terms of its post-translational modifications (acetylation and phosphorylation) and protein-protein interactions with cellular factors. In this context newly identified cellular proteins binding to acetylated Integrase are currently evaluated for their role in protecting the cells from viral infectivity (restriction factors).
Allouch A, Di Primio C, Alpi E, Lusic M, Arosio D, Giacca M, Cereseto A. The TRIM Family Protein KAP1 Inhibits HIV-1 Integration. Cell Host Microbe. 2011 Jun 16;9(6):484-95.
Terreni M., Valentini P., Liverani V., Gutierrez M. I., Di Primio C., Di Fenza A.,Tozzini V., Allouch A., Albanese A., Giacca M., Cereseto A. GCN5-dependent acetylation of HIV-1 integrase enhances viral integration. Retrovirology, 2010. 7:18.
Manganaro L., Lusic M., Gutierrez M.I., Cereseto A., Del Sal G., Giacca M., Concerted action of cellular JNK and Pin-1 restrict HIV-1 integration to activated CD4+ T lymphocytes. Nature Medicine, 2010; 16 (3): 329-333.
Allouch A. and Cereseto A., Identification of cellular factors binding to acetylated HIV-1 integrase. Amino Acids. 2011 Nov;41(5):1137-45.
Paolinelli R., Mendoza-Maldonado R., Cereseto A., Giacca M., Acetylation of human CDC6 by GCN5 regulates CDK-mediated protein phosphorylation in the S-phase of the cell cycle. Nature Struct Mol Biol., 2009. 16(4): 412-420.
Christ F., Thys W., De Rijck J., Albanese A., Arosio D., Emiliani S., Rain J.C., Benarous R., Cereseto A., Debyser Z., Transportin-SR2 imports HIV into the nucleus. Current Biology, 2008. 18(16):1192-202.
Albanese A., Arosio D., Terreni M., Cereseto A. HIV pre-integration complexes selectively target decondensed chromatin in the nuclear periphery. Plos One , 2008. Jun 11;3(6):e2413.
Costi R., Di Santo R., Artico M., Miele G., Valentini P., Novellino E., Cereseto A. Cynnamoil Compounds as Simple Molecules that Inhibitf p300 Histone Acetyltransferase. Journal of Medicinal Chemistry , 2007. 50 (8): p. 1973-77.
Cereseto A., Manganaro L., Gutierrez M.I., Terreni M., Fittipaldi A., Lusic M., Marcello A., Giacca M., Acetylation of HIV-1 Integrase by p300 Regulates Viral Integration. Embo J, 2005. 24 (17): p. 3070-81.
Terreni M., Valentini P., Liverani V., Gutierrez M. I., Di Primio C., Di Fenza A.,Tozzini V., Allouch A., Albanese A., Giacca M., Cereseto A. GCN5-dependent acetylation of HIV-1 integrase enhances viral integration. Retrovirology, 2010. 7:18.
Manganaro L., Lusic M., Gutierrez M.I., Cereseto A., Del Sal G., Giacca M., Concerted action of cellular JNK and Pin-1 restrict HIV-1 integration to activated CD4+ T lymphocytes. Nature Medicine, 2010; 16 (3): 329-333.
Allouch A. and Cereseto A., Identification of cellular factors binding to acetylated HIV-1 integrase. Amino Acids. 2011 Nov;41(5):1137-45.
Paolinelli R., Mendoza-Maldonado R., Cereseto A., Giacca M., Acetylation of human CDC6 by GCN5 regulates CDK-mediated protein phosphorylation in the S-phase of the cell cycle. Nature Struct Mol Biol., 2009. 16(4): 412-420.
Christ F., Thys W., De Rijck J., Albanese A., Arosio D., Emiliani S., Rain J.C., Benarous R., Cereseto A., Debyser Z., Transportin-SR2 imports HIV into the nucleus. Current Biology, 2008. 18(16):1192-202.
Albanese A., Arosio D., Terreni M., Cereseto A. HIV pre-integration complexes selectively target decondensed chromatin in the nuclear periphery. Plos One , 2008. Jun 11;3(6):e2413.
Costi R., Di Santo R., Artico M., Miele G., Valentini P., Novellino E., Cereseto A. Cynnamoil Compounds as Simple Molecules that Inhibitf p300 Histone Acetyltransferase. Journal of Medicinal Chemistry , 2007. 50 (8): p. 1973-77.
Cereseto A., Manganaro L., Gutierrez M.I., Terreni M., Fittipaldi A., Lusic M., Marcello A., Giacca M., Acetylation of HIV-1 Integrase by p300 Regulates Viral Integration. Embo J, 2005. 24 (17): p. 3070-81.
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