Chimeric virus-like particles carrying the CLEC17A carbohydrate-recognition domain significantly reduce Macrobrachium rosenbergii nodavirus infection in Sf9 cells
Issued Date
2025-12-01
Resource Type
eISSN
20452322
Scopus ID
2-s2.0-105024146390
Pubmed ID
41361223
Journal Title
Scientific Reports
Volume
15
Issue
1
Rights Holder(s)
SCOPUS
Bibliographic Citation
Scientific Reports Vol.15 No.1 (2025)
Suggested Citation
Chantunmapitak R., Boonkua S., Thongsum O., Breiman A., Weerachatyanukul W., Asuvapongpatana S., Watthammawut A., Somrit M. Chimeric virus-like particles carrying the CLEC17A carbohydrate-recognition domain significantly reduce Macrobrachium rosenbergii nodavirus infection in Sf9 cells. Scientific Reports Vol.15 No.1 (2025). doi:10.1038/s41598-025-27357-3 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/113523
Title
Chimeric virus-like particles carrying the CLEC17A carbohydrate-recognition domain significantly reduce Macrobrachium rosenbergii nodavirus infection in Sf9 cells
Corresponding Author(s)
Other Contributor(s)
Abstract
Our previous studies demonstrated that Macrobrachium rosenbergii nodavirus (MrNV) infects and replicates in Sf9 insect cells, where fucosylated N- and O-glycans (HexNAc (Fuc)HexNAc-R or Fuc-LacdiNAc) serve as essential binding molecules for viral attachment. Additionally, we showed that the virus-like particles of the virus itself (MrNV-VLPs) were able to bind to the white-tail disease (WTD)-associated tissues and infect Sf9 cells; and these processes were significantly reduced by removing 27 amino acids from the C-terminus of the protruding (P) domain. In this study, we demonstrated that icosahedral particles could still form following the truncation of the P-domain at sites adjacent to known calcium-binding domains (CBDs) present in the S-shell domain in the MrNV capsid protein. We further showed that icosahedral particles could still form after truncation of the P-domain near calcium-binding sites in the S-domain. This generated smaller but intact particles lacking protrusions, designated V250-MrNV-VLPs. The particles with their intact S-shells enabled our complete replacement of the original MrNV capsid protein P-domains with the fucose-binding carbohydrate-recognition domain (CRD) of CLEC17A lectin (Prolectin), successfully creating CLEC17A/CRD-MrNV-VLPs. The chimeric CLEC17A/CRD-MrNV-VLPs were stable icosahedral particles with P-domains structurally distinct from both the smooth V250-MrNV-VLPs and the blade-like domains of wild-type MrNV-VLPs. Furthermore, the chimeric VLPs presented specific binding activities towards immobilized fucosylated glycoconjugates and Sf9 cell protein lysates. Notably, CLEC17A/CRD-MrNV-VLPs were able to reduce MrNV binding and infection in Sf9 cells. Therefore, this study demonstrated the potential for CLEC17A/CRD-MrNV-VLPs as particles that can effectively bind to fucosylated glycans, and their potential development as nanoparticles that can significantly reduce the level of infection by MrNV in susceptible cells.