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      • Record: found
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      Hypothiocyanite and Hypothiocyanite/Lactoferrin Mixture Exhibit Virucidal Activity In Vitro against SARS-CoV-2

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          Abstract

          SARS-CoV-2 replicates efficiently in the upper airways during the prodromal stage, resulting in environmental viral shedding from patients with active COVID-19 as well as from asymptomatic individuals. There is a need to find pharmacological interventions to mitigate the spread of COVID-19. Hypothiocyanite and lactoferrin are molecules of the innate immune system with a large spectrum cidal activity. The Food and Drug Administration and the European Medicines Agency designated the hypothiocyanite and lactoferrin combination as an orphan drug. We report an in vitro study showing that micromolar concentrations of hypothiocyanite exhibit dose- and time-dependent virucidal activity against SARS-CoV-2 and that the latter is slightly enhanced by the simultaneous presence of lactoferrin.

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          Inhibition of SARS Pseudovirus Cell Entry by Lactoferrin Binding to Heparan Sulfate Proteoglycans

          Jianshe Lang, Ning Yang, Jiejie Deng … (2011)
          It has been reported that lactoferrin (LF) participates in the host immune response against Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV) invasion by enhancing NK cell activity and stimulating neutrophil aggregation and adhesion. We further investigated the role of LF in the entry of SARS pseudovirus into HEK293E/ACE2-Myc cells. Our results reveal that LF inhibits SARS pseudovirus infection in a dose-dependent manner. Further analysis suggested that LF was able to block the binding of spike protein to host cells at 4°C, indicating that LF exerted its inhibitory function at the viral attachment stage. However, LF did not disrupt the interaction of spike protein with angiotensin-converting enzyme 2 (ACE2), the functional receptor of SARS-CoV. Previous studies have shown that LF colocalizes with the widely distributed cell-surface heparan sulfate proteoglycans (HSPGs). Our experiments have also confirmed this conclusion. Treatment of the cells with heparinase or exogenous heparin prevented binding of spike protein to host cells and inhibited SARS pseudovirus infection, demonstrating that HSPGs provide the binding sites for SARS-CoV invasion at the early attachment phase. Taken together, our results suggest that, in addition to ACE2, HSPGs are essential cell-surface molecules involved in SARS-CoV cell entry. LF may play a protective role in host defense against SARS-CoV infection through binding to HSPGs and blocking the preliminary interaction between SARS-CoV and host cells. Our findings may provide further understanding of SARS-CoV pathogenesis and aid in treatment of this deadly disease.
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            Quantification of SARS-CoV-2 neutralizing antibody by a pseudotyped virus-based assay

            Jianhui Nie, Qianqian Li, Jiajing Wu … (2020)
            Pseudotyped viruses are useful virological tools because of their safety and versatility. On the basis of a vesicular stomatitis virus (VSV) pseudotyped virus production system, we developed a pseudotyped virus-based neutralization assay against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) in biosafety level 2 facilities. Compared with the binding antibody test, the neutralization assay could discriminate the protective agents from the antibody family. This protocol includes production and titration of the SARS-CoV-2 S pseudotyped virus and the neutralization assay based on it. Various types of samples targeting virus attachment and entry could be evaluated for their potency, including serum samples derived from animals and humans, monoclonal antibodies and fusion inhibitors (peptides or small molecules). If the pseudotyped virus stock has been prepared in advance, it will take 2 days to get the potency data for the candidate samples. Experience in handling cells is needed before implementing this protocol.
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              Generation of VSV pseudotypes using recombinant ΔG-VSV for studies on virus entry, identification of entry inhibitors, and immune responses to vaccines.

              Michael A Whitt (2010)
              Vesicular stomatitis virus (VSV) is a prototypic enveloped animal virus that has been used extensively to study virus entry, replication and assembly due to its broad host range and robust replication properties in a wide variety of mammalian and insect cells. Studies on VSV assembly led to the creation of a recombinant VSV in which the glycoprotein (G) gene was deleted. This recombinant (rVSV-ΔG) has been used to produce VSV pseudotypes containing the envelope glycoproteins of heterologous viruses, including viruses that require high-level biocontainment; however, because the infectivity of rVSV-ΔG pseudotypes is restricted to a single round of replication the analysis can be performed using biosafety level 2 (BSL-2) containment. As such, rVSV-ΔG pseudotypes have facilitated the analysis of virus entry for numerous viral pathogens without the need for specialized containment facilities. The pseudotypes also provide a robust platform to screen libraries for entry inhibitors and to evaluate the neutralizing antibody responses following vaccination. This manuscript describes methods to produce and titer rVSV-ΔG pseudotypes. Procedures to generate rVSV-ΔG stocks and to quantify virus infectivity are also described. These protocols should allow any laboratory knowledgeable in general virological and cell culture techniques to produce successfully replication-restricted rVSV-ΔG pseudotypes for subsequent analysis. Copyright © 2010 Elsevier B.V. All rights reserved.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Pathogens
                Journal ID (iso-abbrev): Pathogens
                Journal ID (publisher-id): pathogens
                Title: Pathogens
                Publisher: MDPI
                ISSN (Electronic): 2076-0817
                Publication date (Electronic): 19 February 2021
                Publication date Collection: February 2021
                Volume: 10
                Issue: 2
                Electronic Location Identifier: 233
                Affiliations
                [1 ]Public Health Department, Local Health Unit N.2 “Marca Trevigiana”, 31100 Treviso, Italy
                [2 ]Department of Molecular Medicine, University of Padova, 35121 Padova, Italy; mattia.mirandola@ 123456gmail.com (M.M.); claudio.salaris@ 123456studenti.unipd.it (C.S.); mariavittoria.salvati@ 123456phd.unipd.it (M.V.S.)
                [3 ]Department of Cardiac, Thoracic, Vascular Sciences & Public Health, University of Padova, 35121 Padova, Italy; giuseppe.mastrangelo@ 123456unipd.it
                Author notes
                [* ]Correspondence: l.cegolon@ 123456gmail.com (L.C.); cristiano.salata@ 123456unipd.it (C.S.); Tel.: +39-(0)4-9827-2364 (L.C. & C.S.); Fax: +39-(0)4-9827-2355 (L.C. & C.S.)
                Author information
                https://orcid.org/0000-0002-6285-7355
                https://orcid.org/0000-0001-7145-3443
                https://orcid.org/0000-0002-6998-8550
                https://orcid.org/0000-0002-5136-7406
                Article
                Publisher ID: pathogens-10-00233
                DOI: 10.3390/pathogens10020233
                PMC ID: 7922920
                PubMed ID: 33669635
                SO-VID: 3be2496a-e212-4a7e-82e5-da52c3558ce9
                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 : 14 January 2021
                Date accepted : 17 February 2021
                Categories
                Subject: Article

                Keywords: hypothiocyanite,lactoferrin,lactoperoxidase system,alx-009,sars-cov-2,covid-19
                Data availability:
                Keywords: hypothiocyanite, lactoferrin, lactoperoxidase system, alx-009, sars-cov-2, covid-19

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