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      Porcine epidemic diarrhea virus: Molecular mechanisms of attenuation and vaccines

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          Abstract

          Porcine epidemic diarrhea virus (PEDV) causes an emerging and re-emerging coronavirus disease characterized by vomiting, acute diarrhea, dehydration, and up to 100% mortality in neonatal suckling piglets, leading to huge economic losses in the global swine industry. Vaccination remains the most promising and effective way to prevent and control PEDV. However, effective vaccines for PEDV are still under development. Understanding the genomic structure and function of PEDV and the influence of the viral components on innate immunity is essential for developing effective vaccines. In the current review, we systematically describe the recent developments in vaccine against PEDV and the roles of structural proteins, non-structural proteins and accessory proteins of PEDV in affecting viral virulence and regulating innate immunity, which will provide insight into the rational design of effective and safe vaccines for PEDV or other coronaviruses.

          Highlights

          • •

            Advances in vaccines of PEDV, such as inactivated and attenuated live vaccines, subunit vaccines, DNA vaccines, and mRNA vaccines.

          • •

            The application of reverse genetics in the development of live attenuated PEDV vaccines.

          • •

            The role of structural proteins, non-structural proteins and accessory proteins of PEDV in affecting viral virulence and regulating innate immunity.

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          Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor

          Jun Lan, Jiwan Ge, Jinfang Yu … (2020)
          A new and highly pathogenic coronavirus (severe acute respiratory syndrome coronavirus-2, SARS-CoV-2) caused an outbreak in Wuhan city, Hubei province, China, starting from December 2019 that quickly spread nationwide and to other countries around the world1-3. Here, to better understand the initial step of infection at an atomic level, we determined the crystal structure of the receptor-binding domain (RBD) of the spike protein of SARS-CoV-2 bound to the cell receptor ACE2. The overall ACE2-binding mode of the SARS-CoV-2 RBD is nearly identical to that of the SARS-CoV RBD, which also uses ACE2 as the cell receptor4. Structural analysis identified residues in the SARS-CoV-2 RBD that are essential for ACE2 binding, the majority of which either are highly conserved or share similar side chain properties with those in the SARS-CoV RBD. Such similarity in structure and sequence strongly indicate convergent evolution between the SARS-CoV-2 and SARS-CoV RBDs for improved binding to ACE2, although SARS-CoV-2 does not cluster within SARS and SARS-related coronaviruses1-3,5. The epitopes of two SARS-CoV antibodies that target the RBD are also analysed for binding to the SARS-CoV-2 RBD, providing insights into the future identification of cross-reactive antibodies.
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            Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2

            Qihui Wang, Yanfang Zhang, Lili Wu … (2020)
            Summary The recent emergence of a novel coronavirus (SARS-CoV-2) in China has caused significant public health concerns. Recently, ACE2 was reported as an entry receptor for SARS-CoV-2. In this study, we present the crystal structure of the C-terminal domain of SARS-CoV-2 (SARS-CoV-2-CTD) spike (S) protein in complex with human ACE2 (hACE2), which reveals a hACE2-binding mode similar overall to that observed for SARS-CoV. However, atomic details at the binding interface demonstrate that key residue substitutions in SARS-CoV-2-CTD slightly strengthen the interaction and lead to higher affinity for receptor binding than SARS-RBD. Additionally, a panel of murine monoclonal antibodies (mAbs) and polyclonal antibodies (pAbs) against SARS-CoV-S1/receptor-binding domain (RBD) were unable to interact with the SARS-CoV-2 S protein, indicating notable differences in antigenicity between SARS-CoV and SARS-CoV-2. These findings shed light on the viral pathogenesis and provide important structural information regarding development of therapeutic countermeasures against the emerging virus.
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              Structure, Function, and Evolution of Coronavirus Spike Proteins

              Fang Li (2016)
              The coronavirus spike protein is a multifunctional molecular machine that mediates coronavirus entry into host cells. It first binds to a receptor on the host cell surface through its S1 subunit and then fuses viral and host membranes through its S2 subunit. Two domains in S1 from different coronaviruses recognize a variety of host receptors, leading to viral attachment. The spike protein exists in two structurally distinct conformations, prefusion and postfusion. The transition from prefusion to postfusion conformation of the spike protein must be triggered, leading to membrane fusion. This article reviews current knowledge about the structures and functions of coronavirus spike proteins, illustrating how the two S1 domains recognize different receptors and how the spike proteins are regulated to undergo conformational transitions. I further discuss the evolution of these two critical functions of coronavirus spike proteins, receptor recognition and membrane fusion, in the context of the corresponding functions from other viruses and host cells.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Microb Pathog
                Journal ID (iso-abbrev): Microb. Pathog
                Title: Microbial Pathogenesis
                Publisher: Published by Elsevier Ltd.
                ISSN (Print): 0882-4010
                ISSN (Electronic): 1096-1208
                Publication date PMC-release: 1 October 2020
                Publication date (Electronic): 1 October 2020
                Electronic Location Identifier: 104553
                Affiliations
                [1]College of Veterinary Medicine, Northwest A&F University, Yangling, Shaanxi, China
                Author notes
                [∗ ]Corresponding author. College of Veterinary Medicine Northwest A&F University, 22 Xining Road, Yangling, Shaanxi, 712100, China.
                [1]

                These authors contributed equally to this work.

                Article
                Publisher Item ID: S0882-4010(20)30919-0 Publisher ID: 104553
                DOI: 10.1016/j.micpath.2020.104553
                PMC ID: 7527827
                PubMed ID: 33011361
                SO-VID: cf16959e-c3b2-4ec8-9781-c2540712d268
                Copyright © © 2020 Published by Elsevier Ltd.
                License:

                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.

                History
                Date received : 10 July 2020
                Date revision received : 29 September 2020
                Date accepted : 29 September 2020
                Categories
                Subject: Article

                ScienceOpen disciplines: Microbiology & Virology
                Keywords: porcine epidemic diarrhea virus,vaccine,virulence,genetics
                Data availability:
                ScienceOpen disciplines: Microbiology & Virology
                Keywords: porcine epidemic diarrhea virus, vaccine, virulence, genetics

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