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      How Influenza Virus Uses Host Cell Pathways during Uncoating

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          Abstract

          Influenza is a zoonotic respiratory disease of major public health interest due to its pandemic potential, and a threat to animals and the human population. The influenza A virus genome consists of eight single-stranded RNA segments sequestered within a protein capsid and a lipid bilayer envelope. During host cell entry, cellular cues contribute to viral conformational changes that promote critical events such as fusion with late endosomes, capsid uncoating and viral genome release into the cytosol. In this focused review, we concisely describe the virus infection cycle and highlight the recent findings of host cell pathways and cytosolic proteins that assist influenza uncoating during host cell entry.

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          Most cited references254

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          Estimates of global seasonal influenza-associated respiratory mortality: a modelling study

          Estimates of influenza-associated mortality are important for national and international decision making on public health priorities. Previous estimates of 250 000-500 000 annual influenza deaths are outdated. We updated the estimated number of global annual influenza-associated respiratory deaths using country-specific influenza-associated excess respiratory mortality estimates from 1999-2015.
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            The ubiquitin code.

            The posttranslational modification with ubiquitin, a process referred to as ubiquitylation, controls almost every process in cells. Ubiquitin can be attached to substrate proteins as a single moiety or in the form of polymeric chains in which successive ubiquitin molecules are connected through specific isopeptide bonds. Reminiscent of a code, the various ubiquitin modifications adopt distinct conformations and lead to different outcomes in cells. Here, we discuss the structure, assembly, and function of this ubiquitin code.
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              Erasers of histone acetylation: the histone deacetylase enzymes.

              Histone deacetylases (HDACs) are enzymes that catalyze the removal of acetyl functional groups from the lysine residues of both histone and nonhistone proteins. In humans, there are 18 HDAC enzymes that use either zinc- or NAD(+)-dependent mechanisms to deacetylate acetyl lysine substrates. Although removal of histone acetyl epigenetic modification by HDACs regulates chromatin structure and transcription, deacetylation of nonhistones controls diverse cellular processes. HDAC inhibitors are already known potential anticancer agents and show promise for the treatment of many diseases.
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                Author and article information

                Contributors
                Role: Academic Editor
                Role: Academic Editor
                Journal
                Cells
                Cells
                cells
                Cells
                MDPI
                2073-4409
                08 July 2021
                July 2021
                : 10
                : 7
                : 1722
                Affiliations
                [1 ]Friedrich Miescher Institute for Biomedical Research, 4058 Basel, Switzerland; etori.moreira@ 123456fmi.ch
                [2 ]Faculty of Life Sciences, School of Cellular and Molecular Medicine, University of Bristol, Bristol BS8 1TD, UK; yohei.yamauchi@ 123456bristol.ac.uk
                [3 ]Faculty of Sciences, University of Basel, 4031 Basel, Switzerland
                Author notes
                Author information
                https://orcid.org/0000-0003-2976-5325
                https://orcid.org/0000-0002-8233-9133
                https://orcid.org/0000-0002-3927-1452
                Article
                cells-10-01722
                10.3390/cells10071722
                8305448
                34359892
                17071b6e-025e-4eb0-b5e7-8b8a537add03
                © 2021 by the authors.

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( https://creativecommons.org/licenses/by/4.0/).

                History
                : 07 May 2021
                : 02 July 2021
                Categories
                Review

                influenza,capsid uncoating,hdac6,ubiquitin,eps8,tnpo1,pandemic,m1,virus–host interaction

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