Multivalent display of VP28 on chimeric virus-like particles enhances binding to shrimp target tissues: A novel antiviral strategy against white spot syndrome virus
Issued Date
2025-08-01
Resource Type
ISSN
09728988
eISSN
22310916
Scopus ID
2-s2.0-105016126068
Journal Title
Veterinary World
Volume
18
Issue
8
Start Page
2194
End Page
2205
Rights Holder(s)
SCOPUS
Bibliographic Citation
Veterinary World Vol.18 No.8 (2025) , 2194-2205
Suggested Citation
Jaranathummakul S., Jariyapong P., Thongsum O., Boonkua S., Chotwiwatthanakun C., Somrit M., Asuvapongpatana S., Wathammawut A., Weerachatyanukul W. Multivalent display of VP28 on chimeric virus-like particles enhances binding to shrimp target tissues: A novel antiviral strategy against white spot syndrome virus. Veterinary World Vol.18 No.8 (2025) , 2194-2205. 2205. doi:10.14202/vetworld.2025.2194-2205 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/112195
Title
Multivalent display of VP28 on chimeric virus-like particles enhances binding to shrimp target tissues: A novel antiviral strategy against white spot syndrome virus
Corresponding Author(s)
Other Contributor(s)
Abstract
Background and Aim: White spot syndrome virus (WSSV) is a devastating pathogen in shrimp aquaculture, with viral protein 28 (VP28) playing a critical role in host cell attachment and entry. The extracellular domain of VP28 (residues 35–95) is immunogenic and essential for infection; however, its receptor interaction mechanisms remain incompletely elucidated. This study aimed to evaluate the tissue-binding affinity of full-length VP28 and its derived peptides (P1: Residues 35–65; P2: Residues 66–95) as well as a multimeric chimeric virus-like particle (K5-VLP) displaying VP28 on the surface of Macrobrachium rosenbergii nodavirus capsids to enhance host tissue interaction. Materials and Methods: Recombinant VP28, synthetic peptides (P1, P2), and chimeric K5-VLP were produced and characterized. Binding and inhibition assays were performed using enzyme-linked immunosorbent assay and immunofluorescence microscopy on shrimp gill, hemocyte, muscle, stomach, and hepatopancreas tissues. Results: Full-length VP28 exhibited strong binding to gill, hemocyte, and muscle tissues. The P1 and P2 peptides showed moderate binding compared to rVP28. Notably, K5-VLP demonstrated a 1.7-fold higher binding affinity than rVP28 in gill tissues and significantly outperformed P1 and P2 peptides. Inhibition assays confirmed that K5-VLP more effectively interfered with VP28 binding than peptides. Structural analysis and transmission electron microscopy confirmed correct assembly and surface presentation of VP28 on the VLPs. Conclusion: Multimeric display of VP28 on K5-VLP enhances its binding affinity to shrimp tissues compared to monomeric or peptide forms. This suggests a promising platform for antiviral strategies, including competitive inhibition of WSSV entry and targeted therapeutic delivery in shrimp aquaculture.