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      Persistence of serum and saliva antibody responses to SARS-CoV-2 spike antigens in COVID-19 patients.

      Author(s): 1 , 2 , 3 , 1 , 4 , 5 , 2 , 2 , 3 , 1 , 1 , 1 , 1 , 6 , 7 , 2 , 2 , 3 , 6 , 8 , 5 , 5 , 1 , 9 , 2 , 2 , 3 , 2 , 2 , 3 , 10 , 3 , 6 , 11 , 9 , 2 , 1 , 12 , 13 , 3 , 14 , 7 , 2 , 4 , 5 , 15 , 16 , 3
      Publication date (Electronic):
      Journal: Science immunology
      Publisher: American Association for the Advancement of Science (AAAS)

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          Abstract

          While the antibody response to SARS-CoV-2 has been extensively studied in blood, relatively little is known about the antibody response in saliva and its relationship to systemic antibody levels. Here, we profiled by enzyme-linked immunosorbent assays (ELISAs) IgG, IgA and IgM responses to the SARS-CoV-2 spike protein (full length trimer) and its receptor-binding domain (RBD) in serum and saliva of acute and convalescent patients with laboratory-diagnosed COVID-19 ranging from 3-115 days post-symptom onset (PSO), compared to negative controls. Anti-SARS-CoV-2 antibody responses were readily detected in serum and saliva, with peak IgG levels attained by 16-30 days PSO. Longitudinal analysis revealed that anti-SARS-CoV-2 IgA and IgM antibodies rapidly decayed, while IgG antibodies remained relatively stable up to 105 days PSO in both biofluids. Lastly, IgG, IgM and to a lesser extent IgA responses to spike and RBD in the serum positively correlated with matched saliva samples. This study confirms that serum and saliva IgG antibodies to SARS-CoV-2 are maintained in the majority of COVID-19 patients for at least 3 months PSO. IgG responses in saliva may serve as a surrogate measure of systemic immunity to SARS-CoV-2 based on their correlation with serum IgG responses.

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          Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation

          Daniel Wrapp, Nianshuang Wang, Kizzmekia S. Corbett … (2020)
          Structure of the nCoV trimeric spike The World Health Organization has declared the outbreak of a novel coronavirus (2019-nCoV) to be a public health emergency of international concern. The virus binds to host cells through its trimeric spike glycoprotein, making this protein a key target for potential therapies and diagnostics. Wrapp et al. determined a 3.5-angstrom-resolution structure of the 2019-nCoV trimeric spike protein by cryo–electron microscopy. Using biophysical assays, the authors show that this protein binds at least 10 times more tightly than the corresponding spike protein of severe acute respiratory syndrome (SARS)–CoV to their common host cell receptor. They also tested three antibodies known to bind to the SARS-CoV spike protein but did not detect binding to the 2019-nCoV spike protein. These studies provide valuable information to guide the development of medical counter-measures for 2019-nCoV. Science, this issue p. 1260
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            Virological assessment of hospitalized patients with COVID-2019

            Roman Wölfel, Victor M Corman, Wolfgang Guggemos … (2020)
            Coronavirus disease 2019 (COVID-19) is an acute infection of the respiratory tract that emerged in late 20191,2. Initial outbreaks in China involved 13.8% of cases with severe courses, and 6.1% of cases with critical courses3. This severe presentation may result from the virus using a virus receptor that is expressed predominantly in the lung2,4; the same receptor tropism is thought to have determined the pathogenicity-but also aided in the control-of severe acute respiratory syndrome (SARS) in 20035. However, there are reports of cases of COVID-19 in which the patient shows mild upper respiratory tract symptoms, which suggests the potential for pre- or oligosymptomatic transmission6-8. There is an urgent need for information on virus replication, immunity and infectivity in specific sites of the body. Here we report a detailed virological analysis of nine cases of COVID-19 that provides proof of active virus replication in tissues of the upper respiratory tract. Pharyngeal virus shedding was very high during the first week of symptoms, with a peak at 7.11 × 108 RNA copies per throat swab on day 4. Infectious virus was readily isolated from samples derived from the throat or lung, but not from stool samples-in spite of high concentrations of virus RNA. Blood and urine samples never yielded virus. Active replication in the throat was confirmed by the presence of viral replicative RNA intermediates in the throat samples. We consistently detected sequence-distinct virus populations in throat and lung samples from one patient, proving independent replication. The shedding of viral RNA from sputum outlasted the end of symptoms. Seroconversion occurred after 7 days in 50% of patients (and by day 14 in all patients), but was not followed by a rapid decline in viral load. COVID-19 can present as a mild illness of the upper respiratory tract. The confirmation of active virus replication in the upper respiratory tract has implications for the containment of COVID-19.
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              Functional assessment of cell entry and receptor usage for SARS-CoV-2 and other lineage B betacoronaviruses

              Michael Letko, Andrea Marzi, Vincent Munster (2020)
              Over the past 20 years, several coronaviruses have crossed the species barrier into humans, causing outbreaks of severe, and often fatal, respiratory illness. Since SARS-CoV was first identified in animal markets, global viromics projects have discovered thousands of coronavirus sequences in diverse animals and geographic regions. Unfortunately, there are few tools available to functionally test these viruses for their ability to infect humans, which has severely hampered efforts to predict the next zoonotic viral outbreak. Here, we developed an approach to rapidly screen lineage B betacoronaviruses, such as SARS-CoV and the recent SARS-CoV-2, for receptor usage and their ability to infect cell types from different species. We show that host protease processing during viral entry is a significant barrier for several lineage B viruses and that bypassing this barrier allows several lineage B viruses to enter human cells through an unknown receptor. We also demonstrate how different lineage B viruses can recombine to gain entry into human cells, and confirm that human ACE2 is the receptor for the recently emerging SARS-CoV-2.
              Article 0 comments Cited 1565 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Journal ID (iso-abbrev): Sci Immunol
                Title: Science immunology
                Publisher: American Association for the Advancement of Science (AAAS)
                ISSN (Electronic): 2470-9468
                ISSN (Print): 2470-9468
                Publication date (Electronic): October 08 2020
                Volume: 5
                Issue: 52
                Affiliations
                [1 ] Department of Immunology, University of Toronto, Toronto, ON, Canada.
                [2 ] Lunenfeld-Tanenbaum Research Institute at Mount Sinai Hospital, Sinai Health System, Toronto, ON, Canada.
                [3 ] Department of Molecular Genetics, University of Toronto, Toronto, ON, Canada.
                [4 ] Institute of Health Policy, Management and Evaluation, University of Toronto, Toronto, ON, Canada.
                [5 ] Department of Microbiology, at Mount Sinai Hospital, Sinai Health System, Toronto, ON, Canada.
                [6 ] Combined Containment Level 3 Unit, University of Toronto, Toronto, ON, Canada.
                [7 ] Mammalian Cell Expression, Human Health Therapeutics Research Centre, National Research Council Canada, Montréal, QC, Canada.
                [8 ] Institute of Medical Science, University of Toronto, Toronto, ON, Canada.
                [9 ] College of Dentistry, University of Saskatchewan, Saskatoon, SK, Canada.
                [10 ] Department of Laboratory Medicine and Molecular Diagnostics, Division of Microbiology, Sunnybrook Health Sciences Centre; Biological Sciences, Sunnybrook Research Institute; and Division of Infectious Diseases, Sunnybrook Health Sciences Centre, Toronto, ON, Canada; Department of Laboratory Medicine and Pathology, University of Toronto, Toronto, ON, Canada.
                [11 ] Canadian Blood Services, Edmonton, AB & Department of Laboratory Medicine and Pathology, University of Alberta, Edmonton, AB, Canada.
                [12 ] St. Michael's Hospital, Toronto, ON, Canada; Li Ka Shing Knowledge Institute.
                [13 ] Department of Medicine, University of Toronto, Toronto, ON, Canada.
                [14 ] Department of Biochemistry, University of Toronto, Toronto, ON, Canada.
                [15 ] Department of Immunology, University of Toronto, Toronto, ON, Canada. jen.gommerman@utoronto.ca gingras@lunenfeld.ca.
                [16 ] Lunenfeld-Tanenbaum Research Institute at Mount Sinai Hospital, Sinai Health System, Toronto, ON, Canada. jen.gommerman@utoronto.ca gingras@lunenfeld.ca.
                Article
                Publisher Item ID: 5/52/eabe5511
                DOI: 10.1126/sciimmunol.abe5511
                PubMed ID: 33033173
                SO-VID: 22b9d6a8-2c7d-4527-8f26-52e6b6e10cb4
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