3
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: not found

      Cell membrane proteins with high N-glycosylation, high expression and multiple interaction partners are preferred by mammalian viruses as receptors

      research-article

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Motivation

          Receptor mediated entry is the first step for viral infection. However, the question of how viruses select receptors remains unanswered.

          Results

          Here, by manually curating a high-quality database of 268 pairs of mammalian virus–host receptor interaction, which included 128 unique viral species or sub-species and 119 virus receptors, we found the viral receptors are structurally and functionally diverse, yet they had several common features when compared to other cell membrane proteins: more protein domains, higher level of N-glycosylation, higher ratio of self-interaction and more interaction partners, and higher expression in most tissues of the host. This study could deepen our understanding of virus–receptor interaction.

          Availability and implementation

          The database of mammalian virus–host receptor interaction is available at http://www.computationalbiology.cn: 5000/viralReceptor.

          Supplementary information

          Supplementary data are available at Bioinformatics online.

          Related collections

          Most cited references22

          • Record: found
          • Abstract: found
          • Article: found

          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.
            Bookmark
            • Record: found
            • Abstract: found
            • Article: found
            Is Open Access

            Sodium taurocholate cotransporting polypeptide is a functional receptor for human hepatitis B and D virus

            Human hepatitis B virus (HBV) infection and HBV-related diseases remain a major public health problem. Individuals coinfected with its satellite hepatitis D virus (HDV) have more severe disease. Cellular entry of both viruses is mediated by HBV envelope proteins. The pre-S1 domain of the large envelope protein is a key determinant for receptor(s) binding. However, the identity of the receptor(s) is unknown. Here, by using near zero distance photo-cross-linking and tandem affinity purification, we revealed that the receptor-binding region of pre-S1 specifically interacts with sodium taurocholate cotransporting polypeptide (NTCP), a multiple transmembrane transporter predominantly expressed in the liver. Silencing NTCP inhibited HBV and HDV infection, while exogenous NTCP expression rendered nonsusceptible hepatocarcinoma cells susceptible to these viral infections. Moreover, replacing amino acids 157–165 of nonfunctional monkey NTCP with the human counterpart conferred its ability in supporting both viral infections. Our results demonstrate that NTCP is a functional receptor for HBV and HDV. DOI: http://dx.doi.org/10.7554/eLife.00049.001
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Virus entry: molecular mechanisms and biomedical applications

              Key Points Virus entry into animal cells is initiated by attachment to receptors and is followed by important conformational changes of viral proteins, penetration through (non-enveloped viruses) or fusion with (enveloped viruses) cellular membranes. The process ends with transfer of viral genomes inside host cells. Viral proteins mediating entry are very diverse, but many share common three-dimensional structural motifs. Conformational changes in the viral proteins that drive entry are typically initiated by high-affinity interactions with receptors, or changes in pH after receptor binding and internalization. They include formation of coiled-coils in class I fusion proteins, dimer to trimer transitions in class II fusion proteins, movement of capsid proteins in non-enveloped viruses and exposure of membrane destabilizing sequences. Fusion with, or penetration through, cell membranes might involve multimolecular protein complexes and requires structural rearrangements of membrane lipids. Inhibitors of virus entry can prevent virus attachment, or bind to entry intermediates; small organic molecules, peptides, soluble receptors and antibodies are in clinical trials. Six virus-specific polyclonal human immunoglobulins, one monoclonal antibody and one peptide have been approved by the US Food and Drug Administration for clinical use. Viral proteins involved in entry can induce immune responses and be used as vaccine immunogens. Viral entry machineries could be beneficial for human physiology and retargeted for the treatment of cancer and other diseases.
                Bookmark

                Author and article information

                Contributors
                Role: Associate Editor
                Journal
                Bioinformatics
                Bioinformatics
                bioinformatics
                Bioinformatics
                Oxford University Press
                1367-4803
                1367-4811
                01 March 2019
                09 August 2018
                01 March 2020
                : 35
                : 5
                : 723-728
                Affiliations
                [1 ]College of Biology, Hunan University, Changsha, China
                [2 ]College of Computer Science and Electronic Engineering, Hunan University, Changsha, China
                [3 ]Center of System Medicine, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences & Peking Union Medical College, Beijing, China
                [4 ]Suzhou Institute of Systems Medicine, Suzhou, China
                [5 ]School of Life Sciences, Central South University, Changsha, China
                [6 ]State Key Laboratory of Chemo/Biosensing and Chemometrics, Hunan University, Changsha, China
                Author notes

                The authors wish it to be known that, in their opinion, the first two authors should be regarded as Joint First Authors.

                Article
                bty694
                10.1093/bioinformatics/bty694
                7109886
                30102334
                6bdcdd81-b44b-43be-8a6c-9f0c67b04e79
                © The Author(s) 2018. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com

                This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model ( https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model)

                This article is made available via the PMC Open Access Subset for unrestricted re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the COVID-19 pandemic or until permissions are revoked in writing. Upon expiration of these permissions, PMC is granted a perpetual license to make this article available via PMC and Europe PMC, consistent with existing copyright protections.

                History
                : 02 April 2018
                : 12 June 2018
                : 08 August 2018
                Page count
                Pages: 6
                Funding
                Funded by: National Key Plan for Scientific Research and Development of China
                Award ID: 2016YFD0500300
                Award ID: 2016YFC1200200
                Funded by: National Natural Science Foundation of China 10.13039/501100001809
                Award ID: 31500126
                Award ID: 31671371
                Award ID: 81730064
                Award ID: 81571985
                Award ID: U1603126
                Funded by: National Science and Technology Major Project
                Award ID: 2017ZX10202201
                Funded by: Chinese Academy of Medical Sciences 10.13039/501100005150
                Award ID: 2016-I2M-1-005
                Categories
                Discovery Note
                Data and Text Mining

                Bioinformatics & Computational biology
                Bioinformatics & Computational biology

                Comments

                Comment on this article