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      Entry of Phenuiviruses into Mammalian Host Cells

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          Abstract

          Phenuiviridae is a large family of arthropod-borne viruses with over 100 species worldwide. Several cause severe diseases in both humans and livestock. Global warming and the apparent geographical expansion of arthropod vectors are good reasons to seriously consider these viruses potential agents of emerging diseases. With an increasing frequency and number of epidemics, some phenuiviruses represent a global threat to public and veterinary health. This review focuses on the early stage of phenuivirus infection in mammalian host cells. We address current knowledge on each step of the cell entry process, from virus binding to penetration into the cytosol. Virus receptors, endocytosis, and fusion mechanisms are discussed in light of the most recent progress on the entry of banda-, phlebo-, and uukuviruses, which together constitute the three prominent genera in the Phenuiviridae family.

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          Virus entry by endocytosis.

          Jason Mercer, Mario Schelhaas, Ari Helenius (2010)
          Although viruses are simple in structure and composition, their interactions with host cells are complex. Merely to gain entry, animal viruses make use of a repertoire of cellular processes that involve hundreds of cellular proteins. Although some viruses have the capacity to penetrate into the cytosol directly through the plasma membrane, most depend on endocytic uptake, vesicular transport through the cytoplasm, and delivery to endosomes and other intracellular organelles. The internalization may involve clathrin-mediated endocytosis (CME), macropinocytosis, caveolar/lipid raft-mediated endocytosis, or a variety of other still poorly characterized mechanisms. This review focuses on the cell biology of virus entry and the different strategies and endocytic mechanisms used by animal viruses.
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            Fever with thrombocytopenia associated with a novel bunyavirus in China.

            Xue-Jie Yu, Mi-Fang Liang, Shou-Yin Zhang … (2011)
            Heightened surveillance of acute febrile illness in China since 2009 has led to the identification of a severe fever with thrombocytopenia syndrome (SFTS) with an unknown cause. Infection with Anaplasma phagocytophilum has been suggested as a cause, but the pathogen has not been detected in most patients on laboratory testing. We obtained blood samples from patients with the case definition of SFTS in six provinces in China. The blood samples were used to isolate the causal pathogen by inoculation of cell culture and for detection of viral RNA on polymerase-chain-reaction assay. The pathogen was characterized on electron microscopy and nucleic acid sequencing. We used enzyme-linked immunosorbent assay, indirect immunofluorescence assay, and neutralization testing to analyze the level of virus-specific antibody in patients' serum samples. We isolated a novel virus, designated SFTS bunyavirus, from patients who presented with fever, thrombocytopenia, leukocytopenia, and multiorgan dysfunction. RNA sequence analysis revealed that the virus was a newly identified member of the genus phlebovirus in the Bunyaviridae family. Electron-microscopical examination revealed virions with the morphologic characteristics of a bunyavirus. The presence of the virus was confirmed in 171 patients with SFTS from six provinces by detection of viral RNA, specific antibodies to the virus in blood, or both. Serologic assays showed a virus-specific immune response in all 35 pairs of serum samples collected from patients during the acute and convalescent phases of the illness. A novel phlebovirus was identified in patients with a life-threatening illness associated with fever and thrombocytopenia in China. (Funded by the China Mega-Project for Infectious Diseases and others.).
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              Viral membrane fusion.

              Stephen C. Harrison (2015)
              Membrane fusion is an essential step when enveloped viruses enter cells. Lipid bilayer fusion requires catalysis to overcome a high kinetic barrier; viral fusion proteins are the agents that fulfill this catalytic function. Despite a variety of molecular architectures, these proteins facilitate fusion by essentially the same generic mechanism. Stimulated by a signal associated with arrival at the cell to be infected (e.g., receptor or co-receptor binding, proton binding in an endosome), they undergo a series of conformational changes. A hydrophobic segment (a "fusion loop" or "fusion peptide") engages the target-cell membrane and collapse of the bridging intermediate thus formed draws the two membranes (virus and cell) together. We know of three structural classes for viral fusion proteins. Structures for both pre- and postfusion conformations of illustrate the beginning and end points of a process that can be probed by single-virion measurements of fusion kinetics.
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                Author and article information

                Contributors
                Esther Schnettler: Role: Academic Editor
                Benjamin Brennan: Role: Academic Editor
                Journal
                Journal ID (nlm-ta): Viruses
                Journal ID (iso-abbrev): Viruses
                Journal ID (publisher-id): viruses
                Title: Viruses
                Publisher: MDPI
                ISSN (Electronic): 1999-4915
                Publication date (Electronic): 14 February 2021
                Publication date Collection: February 2021
                Volume: 13
                Issue: 2
                Electronic Location Identifier: 299
                Affiliations
                [1 ]CellNetworks—Cluster of Excellence and Center for Integrative Infectious Diseases Research (CIID), Department of Infectious Diseases, Virology, University Hospital Heidelberg, 69120 Heidelberg, Germany; jana.koch@ 123456med.uni-heidelberg.de
                [2 ]INRAE, EPHE, Viral Infections and Comparative Pathology (IVPC), UMR754-University Lyon, 69007 Lyon, France; qilin.xin@ 123456etu.univ-lyon1.fr
                [3 ]Fundación Ciencia & Vida, Molecular Virology Laboratory, Universidad San Sebastián, 7780272 Santiago, Chile; ntischler@ 123456cienciavida.org
                Author notes
                [†]

                These authors contributed equally to this work.

                Author information
                https://orcid.org/0000-0002-3574-0805
                https://orcid.org/0000-0002-1087-2422
                https://orcid.org/0000-0002-4578-4780
                https://orcid.org/0000-0002-9966-1452
                Article
                Publisher ID: viruses-13-00299
                DOI: 10.3390/v13020299
                PMC ID: 7918600
                PubMed ID: 33672975
                SO-VID: 0f6658fb-7bd2-4c88-aaab-984c5a43c03b
                Copyright © © 2021 by the authors.
                License:

                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 ( http://creativecommons.org/licenses/by/4.0/).

                History
                Date received : 16 January 2021
                Date accepted : 11 February 2021
                Categories
                Subject: Review

                ScienceOpen disciplines: Microbiology & Virology
                Keywords: arbovirus,arthropod,bandavirus,cell entry,emerging virus,endocytosis,fusion,heartland,phlebovirus,receptor,rift,rna virus,sftsv,toscana,uukuniemi,uukuvirus
                Data availability:
                ScienceOpen disciplines: Microbiology & Virology
                Keywords: arbovirus, arthropod, bandavirus, cell entry, emerging virus, endocytosis, fusion, heartland, phlebovirus, receptor, rift, rna virus, sftsv, toscana, uukuniemi, uukuvirus

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