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      Bat-derived influenza-like viruses H17N10 and H18N11

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          Highlights

          • Bat-derived influenza-like virus hemagglutinin and neuraminidase lack canonical functions and structures.

          • Putative functional modules/domains in other bat-derived influenza-like proteins are conserved.

          • Potential genomic reassortments with canonical influenza virus cannot be ruled out and should be assessed.

          Abstract

          Shorebirds and waterfowls are believed to be the reservoir hosts for influenza viruses, whereas swine putatively act as mixing vessels. The recent identification of two influenza-like virus genomes (designated H17N10 and H18N11) from bats has challenged this notion. A crucial question concerns the role bats might play in influenza virus ecology. Structural and functional studies of the two major surface envelope proteins, hemagglutinin (HA) and neuraminidase (NA), demonstrate that neither has canonical HA or NA functions found in influenza viruses. However, putative functional modules and domains in other encoded proteins are conserved, and the N-terminal domain of the H17N10 polymerase subunit PA has a classical structure and function. Therefore, potential genomic reassortments of such influenza-like viruses with canonical influenza viruses cannot be excluded at this point and should be assessed.

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          Most cited references42

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          Human Infection with a Novel Avian-Origin Influenza A (H7N9) Virus

          New England Journal of Medicine, 368(20), 1888-1897
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            Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin.

            Hemagglutinin (HA) is the receptor-binding and membrane fusion glycoprotein of influenza virus and the target for infectivity-neutralizing antibodies. The structures of three conformations of the ectodomain of the 1968 Hong Kong influenza virus HA have been determined by X-ray crystallography: the single-chain precursor, HA0; the metastable neutral-pH conformation found on virus, and the fusion pH-induced conformation. These structures provide a framework for designing and interpreting the results of experiments on the activity of HA in receptor binding, the generation of emerging and reemerging epidemics, and membrane fusion during viral entry. Structures of HA in complex with sialic acid receptor analogs, together with binding experiments, provide details of these low-affinity interactions in terms of the sialic acid substituents recognized and the HA residues involved in recognition. Neutralizing antibody-binding sites surround the receptor-binding pocket on the membrane-distal surface of HA, and the structures of the complexes between neutralizing monoclonal Fabs and HA indicate possible neutralization mechanisms. Cleavage of the biosynthetic precursor HA0 at a prominent loop in its structure primes HA for subsequent activation of membrane fusion at endosomal pH (Figure 1). Priming involves insertion of the fusion peptide into a charged pocket in the precursor; activation requires its extrusion towards the fusion target membrane, as the N terminus of a newly formed trimeric coiled coil, and repositioning of the C-terminal membrane anchor near the fusion peptide at the same end of a rod-shaped molecule. Comparison of this new HA conformation, which has been formed for membrane fusion, with the structures determined for other virus fusion glycoproteins suggests that these molecules are all in the fusion-activated conformation and that the juxtaposition of the membrane anchor and fusion peptide, a recurring feature, is involved in the fusion mechanism. Extension of these comparisons to the soluble N-ethyl-maleimide-sensitive factor attachment protein receptor (SNARE) protein complex of vesicle fusion allows a similar conclusion.
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              Avian influenza A (H5N1) infection in humans.

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                Author and article information

                Contributors
                Journal
                Trends Microbiol
                Trends Microbiol
                Trends in Microbiology
                Elsevier Ltd.
                0966-842X
                1878-4380
                26 February 2014
                April 2014
                26 February 2014
                : 22
                : 4
                : 183-191
                Affiliations
                [1 ]CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chineses Academy of Sciences, Beijing 100101, China
                [2 ]University of Chinese Academy of Sciences, Chinese Academy of Sciences, Beijing 100049, China
                [3 ]Research Network of Immunity and Health (RNIH), Beijing Institutes of Life Science, Chinese Academy of Sciences, Beijing 100101, China
                [4 ]Office of Director-General, Chinese Center for Disease Control and Prevention (China CDC), Beijing 102206, China
                Article
                S0966-842X(14)00022-5
                10.1016/j.tim.2014.01.010
                7127364
                24582528
                ca1cff72-fad2-456a-a4d0-c5f3081ae061
                Copyright © 2014 Elsevier Ltd. All rights reserved.

                Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.

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                Article

                Microbiology & Virology
                bat-derived influenza-like virus,hemagglutinin (ha),neuraminidase (na),pa,reassortment,h17n10,h18n11

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