Work

Class B scavenger receptor resists WSSV replication by recognizing the viral lipid molecule and promoting phagocytosis

Year: 2025

Type: article

Abstract: ABSTRACT Class B scavenger receptors (SRBs) have been well-studied in bacteria-induced immune responses in invertebrates. However, the status of SRB-defending viruses remains unclear. In this study, we identified a scavenger receptor in Procambarus clarkii (crayfish), which is homologous to mammalian SRBs, and designated it as Pc SRB. The expression of Pc SRB was upregulated after the WSSV challenge. The survival rate of crayfish was decreased, but the WSSV copy number increased after Pc SRB knockdown during virus invasion. In addition, Pc SRB bound to WSSV. Furthermore, we detected how Pc SRB interacted with WSSV, and we found that Pc SRB could bind to cholesta-3,5-diene, (CD3,5), a novel WSSV lipid ligand, rather than dibutyl phthalate (DBP). Besides, Pc SRB could bind to VP19, VP26, and VP28, rather than VP24. Mutant-binding experiments demonstrated that the hydrophobic domain (130–180 aa) of Pc SRB is important for recognizing WSSV. Furthermore, Pc SRB might promote lysosomal eliminating function to degrade WSSV. Altogether, we identified a new mechanism for scavenger receptor recognition and resistance to WSSV. IMPORTANCE Pc SRB could bind to WSSV directly. Pc SRB could interact with WSSV via binding to lipid molecule CD3,5 and viral envelope proteins. Pc SRB could influence lysosomal activation.

Source: Journal of Virology

DOI: 10.1128/jvi.01700-24

Authors: Yi-Heng Huang, Xin-Lu Guo, Meng-Ke Shan, Gui-Wen Yang, Hui-Ting Yang

Institution: Shandong Normal University

Language: English

Topic: Invertebrate Immune Response Mechanisms

Subfield: Immunology

Field: Immunology and Microbiology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: diamond

Funders: Department of Science and Technology of Shandong Province, Natural Science Foundation of Shandong Province