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BFRF1 protein is involved in EBV-mediated autophagy manipulation
Affiliation:1. Dep. Experimental Medicine University of Rome “La Sapienza”, Laboratory Affiliated to Istituto Pasteur Italia fondazione Cenci-Bolognetti, Italy;2. Dep. Molecular Medicine University of Rome “La Sapienza”, Italy;3. Boston University School of Medicine, Boston, MA, USA;1. Pharmacy College, Fujian University of Traditional Chinese Medicine, Fuzhou, China;2. Institute of Human Virology, University of Maryland School of Medicine, Baltimore, MD 21201, USA;3. Marlene and Stewart Greenebaum Cancer Center, University of Maryland School of Medicine, Baltimore, MD 21201, USA;4. Departments of Medicine, University of Maryland School of Medicine, Baltimore, MD 21201, USA;5. Departments of Microbiology and Immunology, University of Maryland School of Medicine, Baltimore, MD 21201, USA;1. Department of Respiratory Care, Chang-Gung University of Science and Technology, Chiayi 61363, Taiwan;2. Department of Pediatric Surgery, Chang-Gung Memorial Hospital, Chiayi 61363, Taiwan;3. Graduate Institute of Clinical Medical Sciences, Chang-Gung University, Taoyuan 33302, Taiwan;4. School of Traditional Chinese Medicine, College of Medicine, Chang-Gung University, Taoyuan 33302, Taiwan;5. Department of Pediatrics, Chang-Gung Memorial Hospital, Chiayi 61363, Taiwan;6. Department of Nephrology, Chang-Gung Memorial Hospital, Chiayi 61363, Taiwan;1. Guangdong Provincial Key Laboratory of New Drug Screening, School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, 510515, PR China;2. State Key Laboratory of Organ Failure Research, Guangdong Provincial Institute of Nephrology, Southern Medical University, Guangzhou, 510515, PR China;1. Division of Infectious Disease, Department of Medicine, Brigham & Women’s Hospital, Harvard Medical School, 181 Longwood Avenue, Boston, MA 02115, USA;2. Institut für Klinische und Molekulare Virologie, Friedrich-Alexander-Universität Erlangen-Nürnberg, 91054 Erlangen, Germany;3. Cambridge Institute for Medical Research, University of Cambridge, Hills Road, Cambridge CB2 0XY, UK;4. Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA;5. Wellcome Trust Sanger Institute, Hinxton, Cambridge, CB10 1HH, UK;6. Department of Immunobiology and Microbiology, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115, USA;7. Harvard Virology Program, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115, USA
Abstract:Viral egress and autophagy are two mechanisms that seem to be strictly connected in Herpesviruses’s biology. Several data suggest that the autophagic machinery facilitates the egress of viral capsids and thus the production of new infectious particles. In the Herpesvirus family, viral nuclear egress is controlled and organized by a well conserved group of proteins named Nuclear Egress Complex (NEC). In the case of EBV, NEC is composed by BFRF1 and BFLF2 proteins, although the alterations of the nuclear host cell architecture are mainly driven by BFRF1, a multifunctional viral protein anchored to the inner nuclear membrane of the host cell. BFRF1 shares a peculiar distribution with several nuclear components and with them it strictly interacts. In this study, we investigated the possible role of BFRF1 in manipulating autophagy, pathway that possibly originates from nucleus, regulating the interplay between autophagy and viral egress.
Keywords:EBV lytic cycle  Nuclear egress  Autophagy  BFRF1  LC3  Lamin B1
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