التفاصيل البيبلوغرافية
| العنوان: |
The Antiviral Activity of the Lectin Griffithsin against SARS-CoV-2 Is Enhanced by the Presence of Structural Proteins |
| المؤلفون: |
Arjan Bains, Kathryn Fischer, Wenyan Guan, Patricia J. LiWang |
| المصدر: |
Viruses, Vol 15, Iss 12, p 2452 (2023) |
| بيانات النشر: |
MDPI AG, 2023. |
| سنة النشر: |
2023 |
| المجموعة: |
LCC:Microbiology |
| مصطلحات موضوعية: |
COVID-19, SARS-CoV-2, DC-SIGN, Griffithsin, M protein, trans-infection, Microbiology, QR1-502 |
| الوصف: |
Although COVID-19 transmission has been reduced by the advent of vaccinations and a variety of rapid monitoring techniques, the SARS-CoV-2 virus itself has shown a remarkable ability to mutate and persist. With this long track record of immune escape, researchers are still exploring prophylactic treatments to curtail future SARS-CoV-2 variants. Specifically, much focus has been placed on the antiviral lectin Griffithsin in preventing spike protein-mediated infection via the hACE2 receptor (direct infection). However, an oft-overlooked aspect of SARS-CoV-2 infection is viral capture by attachment receptors such as DC-SIGN, which is thought to facilitate the initial stages of COVID-19 infection in the lung tissue (called trans-infection). In addition, while immune escape is dictated by mutations in the spike protein, coronaviral virions also incorporate M, N, and E structural proteins within the particle. In this paper, we explored how several structural facets of both the SARS-CoV-2 virion and the antiviral lectin Griffithsin can affect and attenuate the infectivity of SARS-CoV-2 pseudovirus. We found that Griffithsin was a better inhibitor of hACE2-mediated direct infection when the coronaviral M protein is present compared to when it is absent (possibly providing an explanation regarding why Griffithsin shows better inhibition against authentic SARS-CoV-2 as opposed to pseudotyped viruses, which generally do not contain M) and that Griffithsin was not an effective inhibitor of DC-SIGN-mediated trans-infection. Furthermore, we found that DC-SIGN appeared to mediate trans-infection exclusively via binding to the SARS-CoV-2 spike protein, with no significant effect observed when other viral proteins (M, N, and/or E) were present. These results provide etiological data that may help to direct the development of novel antiviral treatments, either by leveraging Griffithsin binding to the M protein as a novel strategy to prevent SARS-CoV-2 infection or by narrowing efforts to inhibit trans-infection to focus on DC-SIGN binding to SARS-CoV-2 spike protein. |
| نوع الوثيقة: |
article |
| وصف الملف: |
electronic resource |
| اللغة: |
English |
| تدمد: |
1999-4915 |
| Relation: |
https://www.mdpi.com/1999-4915/15/12/2452; https://doaj.org/toc/1999-4915 |
| DOI: |
10.3390/v15122452 |
| URL الوصول: |
https://doaj.org/article/fbd961e09f9a43f6b07685aa0fe932e8 |
| رقم الانضمام: |
edsdoj.fbd961e09f9a43f6b07685aa0fe932e8 |
| قاعدة البيانات: |
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