Multivalent display of VP28 on chimeric virus-like particles enhances binding to shrimp target tissues: A novel antiviral strategy against white spot syndrome virus

Vet World Vol.18 August-2025 Article - 4

Research Article

Veterinary World, 18(8): 2194-2205

https://doi.org/10.14202/vetworld.2025.2194-2205

Somkid Jaranathummakul¹, Pitchanee Jariyapong², Orawan Thongsum¹, Supawich Boonkua¹, Charoonroj Chotwiwatthanakun³, Monsicha Somrit¹, Somluk Asuvapongpatana¹, Attaboon Wathammawut⁴, and Wattana Weerachatyanukul¹

1. Department of Anatomy, Faculty of Science, Mahidol University, Bangkok, Thailand.

2. Department of Medical Science, School of Medicine, Walailak University, Thasala District, Nakhonsrithammarat, Thailand.

3. Academic and Curriculum Division, Nakhonsawan Campus, Mahidol University, Nakhonsawan, Thailand.

4. Department of Anatomy, Faculty of Medicine, Sri Nakharinwiroj University, Bangkok, Thailand.

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.

Keywords: aquaculture vaccines, Macrobrachium rosenbergii nodavirus, shrimp immunity, tissue binding, virus-like particles, viral protein 28, white spot syndrome virus.

How to cite this article: Jaranathummakul S, Jariyapong P, Thongsum O, Boonkua S, Chotwiwatthanakun C, Somrit M, Asuvapongpatana S, Wathammawut A, and Weerachatyanukul W (2025) 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, 18(8): 2194-2205.

Received: 25-03-2025 Accepted: 09-07-2025 Published online: 02-08-2025

Corresponding author: Wattana Weerachatyanukul E-mail: wattana.wee@mahidol.ac.th

DOI: 10.14202/vetworld.2025.2194-2205

Copyright: Jaranathummakul, et al. This article is an open access article distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http:// creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.