BFRF1 protein is involved in EBV-mediated autophagy manipulation
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...
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Published in | Microbes and infection Vol. 22; no. 10; pp. 585 - 591 |
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Main Authors | , , , , , , , , |
Format | Journal Article |
Language | English |
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Elsevier Masson SAS
01.11.2020
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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. |
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AbstractList | 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. |
Author | Farina, Antonella Farina, Giuseppina A. Santarelli, Roberta Valia, Sandro Dimarco, Marzia Angeloni, Antonio Faggioni, Alberto Cirone, Mara Gonnella, Roberta |
Author_xml | – sequence: 1 givenname: Roberta surname: Gonnella fullname: Gonnella, Roberta organization: Dep. Experimental Medicine University of Rome “La Sapienza”, Laboratory Affiliated to Istituto Pasteur Italia fondazione Cenci-Bolognetti, Italy – sequence: 2 givenname: Marzia surname: Dimarco fullname: Dimarco, Marzia organization: Dep. Experimental Medicine University of Rome “La Sapienza”, Laboratory Affiliated to Istituto Pasteur Italia fondazione Cenci-Bolognetti, Italy – sequence: 3 givenname: Giuseppina A. surname: Farina fullname: Farina, Giuseppina A. organization: Boston University School of Medicine, Boston, MA, USA – sequence: 4 givenname: Roberta surname: Santarelli fullname: Santarelli, Roberta organization: Dep. Experimental Medicine University of Rome “La Sapienza”, Laboratory Affiliated to Istituto Pasteur Italia fondazione Cenci-Bolognetti, Italy – sequence: 5 givenname: Sandro surname: Valia fullname: Valia, Sandro organization: Dep. Molecular Medicine University of Rome “La Sapienza”, Italy – sequence: 6 givenname: Alberto surname: Faggioni fullname: Faggioni, Alberto organization: Dep. Experimental Medicine University of Rome “La Sapienza”, Laboratory Affiliated to Istituto Pasteur Italia fondazione Cenci-Bolognetti, Italy – sequence: 7 givenname: Antonio surname: Angeloni fullname: Angeloni, Antonio organization: Dep. Experimental Medicine University of Rome “La Sapienza”, Laboratory Affiliated to Istituto Pasteur Italia fondazione Cenci-Bolognetti, Italy – sequence: 8 givenname: Mara surname: Cirone fullname: Cirone, Mara organization: Dep. Experimental Medicine University of Rome “La Sapienza”, Laboratory Affiliated to Istituto Pasteur Italia fondazione Cenci-Bolognetti, Italy – sequence: 9 givenname: Antonella orcidid: 0000-0002-8629-0971 surname: Farina fullname: Farina, Antonella email: antonella.farina@uniroma1.it organization: Dep. Experimental Medicine University of Rome “La Sapienza”, Laboratory Affiliated to Istituto Pasteur Italia fondazione Cenci-Bolognetti, Italy |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/32882412$$D View this record in MEDLINE/PubMed |
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Keywords | EBV lytic cycle Lamin B1 BFRF1 Nuclear egress Autophagy LC3 |
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Snippet | Viral egress and autophagy are two mechanisms that seem to be strictly connected in Herpesviruses’s biology. Several data suggest that the autophagic machinery... Viral egress and autophagy are two mechanisms that seem to be strictly connected in Herpesviruses's biology. Several data suggest that the autophagic machinery... |
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SubjectTerms | Autophagy BFRF1 EBV lytic cycle HEK293 Cells Herpesvirus 4, Human - physiology Humans Lamin B1 Lamin Type B - metabolism LC3 Membrane Proteins - metabolism Microtubule-Associated Proteins - metabolism Nuclear egress Nuclear Envelope - metabolism Protein Binding rab GTP-Binding Proteins - metabolism rab7 GTP-Binding Proteins Viral Proteins - metabolism Virus Release |
Title | BFRF1 protein is involved in EBV-mediated autophagy manipulation |
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