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Evidence that Maackia amurensis seed lectin (MASL) exerts pleiotropic actions on oral squamous cells to inhibit SARS-CoV-2 infection and COVID-19 disease progression
COVID-19 was declared an international public health emergency in January, and a pandemic in March of 2020. There are over 23 million confirmed COVID-19 cases that have cause over 800 thousand deaths worldwide as of August 19th, 2020. COVID-19 is caused by the SARS-CoV-2 virus. SARS-CoV-2 presents a...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Journal Experts
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7587785/ https://www.ncbi.nlm.nih.gov/pubmed/33106801 http://dx.doi.org/10.21203/rs.3.rs-93851/v1 |
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author | Sheehan, Stephanie A. Hamilton, Kelly L. Retzbach, Edward P. Balachandran, Premalatha Krishnan, Harini Leone, Paola Goldberg, Gary S. |
author_facet | Sheehan, Stephanie A. Hamilton, Kelly L. Retzbach, Edward P. Balachandran, Premalatha Krishnan, Harini Leone, Paola Goldberg, Gary S. |
author_sort | Sheehan, Stephanie A. |
collection | PubMed |
description | COVID-19 was declared an international public health emergency in January, and a pandemic in March of 2020. There are over 23 million confirmed COVID-19 cases that have cause over 800 thousand deaths worldwide as of August 19th, 2020. COVID-19 is caused by the SARS-CoV-2 virus. SARS-CoV-2 presents a surface “spike” protein that binds to the ACE2 receptor to infect host cells. In addition to the respiratory tract, SARS-Cov-2 can also infect cells of the oral mucosa, which also express the ACE2 receptor. The spike and ACE2 proteins are highly glycosylated with sialic acid modifications that direct viral-host interactions and infection. Maackia amurensis seed lectin (MASL) has a strong affinity for sialic acid modified proteins and can be used as an antiviral agent. Here, we report that MASL targets the ACE2 receptor, decreases ACE2 expression and glycosylation, suppresses binding of the SARS-CoV-2 spike protein, and decreases expression of inflammatory mediators by oral epithelial cells that cause ARDS in COVID-19 patients. This work identifies MASL as an agent with potential to inhibit SARS-CoV-2 infection and COVID-19 related inflammatory syndromes. |
format | Online Article Text |
id | pubmed-7587785 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | American Journal Experts |
record_format | MEDLINE/PubMed |
spelling | pubmed-75877852020-10-27 Evidence that Maackia amurensis seed lectin (MASL) exerts pleiotropic actions on oral squamous cells to inhibit SARS-CoV-2 infection and COVID-19 disease progression Sheehan, Stephanie A. Hamilton, Kelly L. Retzbach, Edward P. Balachandran, Premalatha Krishnan, Harini Leone, Paola Goldberg, Gary S. Res Sq Article COVID-19 was declared an international public health emergency in January, and a pandemic in March of 2020. There are over 23 million confirmed COVID-19 cases that have cause over 800 thousand deaths worldwide as of August 19th, 2020. COVID-19 is caused by the SARS-CoV-2 virus. SARS-CoV-2 presents a surface “spike” protein that binds to the ACE2 receptor to infect host cells. In addition to the respiratory tract, SARS-Cov-2 can also infect cells of the oral mucosa, which also express the ACE2 receptor. The spike and ACE2 proteins are highly glycosylated with sialic acid modifications that direct viral-host interactions and infection. Maackia amurensis seed lectin (MASL) has a strong affinity for sialic acid modified proteins and can be used as an antiviral agent. Here, we report that MASL targets the ACE2 receptor, decreases ACE2 expression and glycosylation, suppresses binding of the SARS-CoV-2 spike protein, and decreases expression of inflammatory mediators by oral epithelial cells that cause ARDS in COVID-19 patients. This work identifies MASL as an agent with potential to inhibit SARS-CoV-2 infection and COVID-19 related inflammatory syndromes. American Journal Experts 2020-10-23 /pmc/articles/PMC7587785/ /pubmed/33106801 http://dx.doi.org/10.21203/rs.3.rs-93851/v1 Text en https://creativecommons.org/licenses/by/4.0/This work is licensed under aCreative Commons Attribution 4.0 International License (https://creativecommons.org/licenses/by/4.0/) , which allows reusers to distribute, remix, adapt, and build upon the material in any medium or format, so long as attribution is given to the creator. The license allows for commercial use. |
spellingShingle | Article Sheehan, Stephanie A. Hamilton, Kelly L. Retzbach, Edward P. Balachandran, Premalatha Krishnan, Harini Leone, Paola Goldberg, Gary S. Evidence that Maackia amurensis seed lectin (MASL) exerts pleiotropic actions on oral squamous cells to inhibit SARS-CoV-2 infection and COVID-19 disease progression |
title | Evidence that Maackia amurensis seed lectin (MASL) exerts pleiotropic actions on oral squamous cells to inhibit SARS-CoV-2 infection and COVID-19 disease progression |
title_full | Evidence that Maackia amurensis seed lectin (MASL) exerts pleiotropic actions on oral squamous cells to inhibit SARS-CoV-2 infection and COVID-19 disease progression |
title_fullStr | Evidence that Maackia amurensis seed lectin (MASL) exerts pleiotropic actions on oral squamous cells to inhibit SARS-CoV-2 infection and COVID-19 disease progression |
title_full_unstemmed | Evidence that Maackia amurensis seed lectin (MASL) exerts pleiotropic actions on oral squamous cells to inhibit SARS-CoV-2 infection and COVID-19 disease progression |
title_short | Evidence that Maackia amurensis seed lectin (MASL) exerts pleiotropic actions on oral squamous cells to inhibit SARS-CoV-2 infection and COVID-19 disease progression |
title_sort | evidence that maackia amurensis seed lectin (masl) exerts pleiotropic actions on oral squamous cells to inhibit sars-cov-2 infection and covid-19 disease progression |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7587785/ https://www.ncbi.nlm.nih.gov/pubmed/33106801 http://dx.doi.org/10.21203/rs.3.rs-93851/v1 |
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