Replacing protruding domains of MrNV virus-like particles with sialic acid binding domains enhances binding to SARS-CoV-2 susceptible cells and reduces pseudovirus infection
Abstract The SARS-CoV-2 virus continues to pose a public health threat due to its ability to rapidly mutate into multiple variants via mutation in its spike (S1/2) proteins. These mutations can lead to viral variants capable of escaping antibody neutralization. The interaction between the SARS-CoV-2...
Saved in:
| Main Authors: | , , , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2025-07-01
|
| Series: | Scientific Reports |
| Subjects: | |
| Online Access: | https://doi.org/10.1038/s41598-025-10792-7 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1849237722514849792 |
|---|---|
| author | Supawich Boonkua Orawan Thongsum Rueangtip Chantunmapitak Purimpuch Soongnart Somkid Jaranathummakul Kitima Srisanga Patompon Wongtrakoongate Somluk Asuvapongpatana Wattana Weerachatyanukul Atthaboon Watthammawut Monsicha Somrit |
| author_facet | Supawich Boonkua Orawan Thongsum Rueangtip Chantunmapitak Purimpuch Soongnart Somkid Jaranathummakul Kitima Srisanga Patompon Wongtrakoongate Somluk Asuvapongpatana Wattana Weerachatyanukul Atthaboon Watthammawut Monsicha Somrit |
| author_sort | Supawich Boonkua |
| collection | DOAJ |
| description | Abstract The SARS-CoV-2 virus continues to pose a public health threat due to its ability to rapidly mutate into multiple variants via mutation in its spike (S1/2) proteins. These mutations can lead to viral variants capable of escaping antibody neutralization. The interaction between the SARS-CoV-2 spike protein and the host ACE2 receptor is influenced by carbohydrate-mediated mechanisms, as the spike is heavily glycosylated with terminal sialic acids, making these sugar moieties attractive targets for therapeutic intervention. We aimed to study the complete replacement of their protrusion domains of Macrobrachium rosenbergii nodavirus capsid protein with the larger ligands in the form of carbohydrate-recognition domain derived from a terminal sialic acid-binding lectin (tsCRD). We produced chimeric virus-like particles MrNV-VLPs to display the tsCRD peptide sequence of the Sambucus Nigra Agglutinin (SNA-I). The tsCRD-MrNV-VLPs maintained their icosahedral structure and increased binding and uptake into ACE2-overexpressing cells. Additionally, these particles exhibited significant blocking capability against various SARS-CoV-2 pseudo-virus variants such as Wuhan, Delta, and Omicron. Our results demonstrated that tsCRD-MrNV-VLPs have the potential to be developed into an effective agent to block and reduce SARS-CoV-2 infection in susceptible cells and present the potential of these VLPs for protective applications. |
| format | Article |
| id | doaj-art-da6c0a3a5f5145c1bf9f2d1058a64c44 |
| institution | Kabale University |
| issn | 2045-2322 |
| language | English |
| publishDate | 2025-07-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj-art-da6c0a3a5f5145c1bf9f2d1058a64c442025-08-20T04:01:52ZengNature PortfolioScientific Reports2045-23222025-07-0115111410.1038/s41598-025-10792-7Replacing protruding domains of MrNV virus-like particles with sialic acid binding domains enhances binding to SARS-CoV-2 susceptible cells and reduces pseudovirus infectionSupawich Boonkua0Orawan Thongsum1Rueangtip Chantunmapitak2Purimpuch Soongnart3Somkid Jaranathummakul4Kitima Srisanga5Patompon Wongtrakoongate6Somluk Asuvapongpatana7Wattana Weerachatyanukul8Atthaboon Watthammawut9Monsicha Somrit10Department of Anatomy, Faculty of Science, Mahidol UniversityDepartment of Anatomy, Faculty of Science, Mahidol UniversityDepartment of Anatomy, Faculty of Science, Mahidol UniversityDepartment of Anatomy, Faculty of Science, Mahidol UniversityDepartment of Anatomy, Faculty of Science, Mahidol UniversityDepartment of Biochemistry, Faculty of Science, Mahidol UniversityDepartment of Biochemistry, Faculty of Science, Mahidol UniversityDepartment of Anatomy, Faculty of Science, Mahidol UniversityDepartment of Anatomy, Faculty of Science, Mahidol UniversityCenter for Neuroscience, Faculty of Science, Mahidol UniversityDepartment of Anatomy, Faculty of Science, Mahidol UniversityAbstract The SARS-CoV-2 virus continues to pose a public health threat due to its ability to rapidly mutate into multiple variants via mutation in its spike (S1/2) proteins. These mutations can lead to viral variants capable of escaping antibody neutralization. The interaction between the SARS-CoV-2 spike protein and the host ACE2 receptor is influenced by carbohydrate-mediated mechanisms, as the spike is heavily glycosylated with terminal sialic acids, making these sugar moieties attractive targets for therapeutic intervention. We aimed to study the complete replacement of their protrusion domains of Macrobrachium rosenbergii nodavirus capsid protein with the larger ligands in the form of carbohydrate-recognition domain derived from a terminal sialic acid-binding lectin (tsCRD). We produced chimeric virus-like particles MrNV-VLPs to display the tsCRD peptide sequence of the Sambucus Nigra Agglutinin (SNA-I). The tsCRD-MrNV-VLPs maintained their icosahedral structure and increased binding and uptake into ACE2-overexpressing cells. Additionally, these particles exhibited significant blocking capability against various SARS-CoV-2 pseudo-virus variants such as Wuhan, Delta, and Omicron. Our results demonstrated that tsCRD-MrNV-VLPs have the potential to be developed into an effective agent to block and reduce SARS-CoV-2 infection in susceptible cells and present the potential of these VLPs for protective applications.https://doi.org/10.1038/s41598-025-10792-7Virus-like particles (VLPs)Macrobrachium rosenbergii nodavirus (MrNV)NanotechnologyGenetic modification |
| spellingShingle | Supawich Boonkua Orawan Thongsum Rueangtip Chantunmapitak Purimpuch Soongnart Somkid Jaranathummakul Kitima Srisanga Patompon Wongtrakoongate Somluk Asuvapongpatana Wattana Weerachatyanukul Atthaboon Watthammawut Monsicha Somrit Replacing protruding domains of MrNV virus-like particles with sialic acid binding domains enhances binding to SARS-CoV-2 susceptible cells and reduces pseudovirus infection Scientific Reports Virus-like particles (VLPs) Macrobrachium rosenbergii nodavirus (MrNV) Nanotechnology Genetic modification |
| title | Replacing protruding domains of MrNV virus-like particles with sialic acid binding domains enhances binding to SARS-CoV-2 susceptible cells and reduces pseudovirus infection |
| title_full | Replacing protruding domains of MrNV virus-like particles with sialic acid binding domains enhances binding to SARS-CoV-2 susceptible cells and reduces pseudovirus infection |
| title_fullStr | Replacing protruding domains of MrNV virus-like particles with sialic acid binding domains enhances binding to SARS-CoV-2 susceptible cells and reduces pseudovirus infection |
| title_full_unstemmed | Replacing protruding domains of MrNV virus-like particles with sialic acid binding domains enhances binding to SARS-CoV-2 susceptible cells and reduces pseudovirus infection |
| title_short | Replacing protruding domains of MrNV virus-like particles with sialic acid binding domains enhances binding to SARS-CoV-2 susceptible cells and reduces pseudovirus infection |
| title_sort | replacing protruding domains of mrnv virus like particles with sialic acid binding domains enhances binding to sars cov 2 susceptible cells and reduces pseudovirus infection |
| topic | Virus-like particles (VLPs) Macrobrachium rosenbergii nodavirus (MrNV) Nanotechnology Genetic modification |
| url | https://doi.org/10.1038/s41598-025-10792-7 |
| work_keys_str_mv | AT supawichboonkua replacingprotrudingdomainsofmrnvviruslikeparticleswithsialicacidbindingdomainsenhancesbindingtosarscov2susceptiblecellsandreducespseudovirusinfection AT orawanthongsum replacingprotrudingdomainsofmrnvviruslikeparticleswithsialicacidbindingdomainsenhancesbindingtosarscov2susceptiblecellsandreducespseudovirusinfection AT rueangtipchantunmapitak replacingprotrudingdomainsofmrnvviruslikeparticleswithsialicacidbindingdomainsenhancesbindingtosarscov2susceptiblecellsandreducespseudovirusinfection AT purimpuchsoongnart replacingprotrudingdomainsofmrnvviruslikeparticleswithsialicacidbindingdomainsenhancesbindingtosarscov2susceptiblecellsandreducespseudovirusinfection AT somkidjaranathummakul replacingprotrudingdomainsofmrnvviruslikeparticleswithsialicacidbindingdomainsenhancesbindingtosarscov2susceptiblecellsandreducespseudovirusinfection AT kitimasrisanga replacingprotrudingdomainsofmrnvviruslikeparticleswithsialicacidbindingdomainsenhancesbindingtosarscov2susceptiblecellsandreducespseudovirusinfection AT patomponwongtrakoongate replacingprotrudingdomainsofmrnvviruslikeparticleswithsialicacidbindingdomainsenhancesbindingtosarscov2susceptiblecellsandreducespseudovirusinfection AT somlukasuvapongpatana replacingprotrudingdomainsofmrnvviruslikeparticleswithsialicacidbindingdomainsenhancesbindingtosarscov2susceptiblecellsandreducespseudovirusinfection AT wattanaweerachatyanukul replacingprotrudingdomainsofmrnvviruslikeparticleswithsialicacidbindingdomainsenhancesbindingtosarscov2susceptiblecellsandreducespseudovirusinfection AT atthaboonwatthammawut replacingprotrudingdomainsofmrnvviruslikeparticleswithsialicacidbindingdomainsenhancesbindingtosarscov2susceptiblecellsandreducespseudovirusinfection AT monsichasomrit replacingprotrudingdomainsofmrnvviruslikeparticleswithsialicacidbindingdomainsenhancesbindingtosarscov2susceptiblecellsandreducespseudovirusinfection |