Porcine reproductive and respiratory syndrome (PRRS) is a highly contagious immunosuppressive disease caused by the porcine reproductive and respiratory syndrome virus (PRRSV) that is characterized by a highly variable gene sequence and a high rate of recombination, thereby contributing to difficulties in the clinical prevention and control of this virus. Glycosylated protein 3 (GP3) is the most glycosylated protein in PRRSV, and is closely associated with the composition of PRRSV virus particles, infection, and immune evasion. This review summarizes the structural features, genetic evolutionary patterns, glycosylation of GP3 and its interactions with other PRRSV and host proteins, associations with PRRSV infection and virulence, and immunomodulatory roles. Additionally, it provides an overview of research progress on monoclonal antibodies and vaccines targeting GP3. This study aims to provide a theoretical foundation for better understanding the structure and function of GP3, of the mechanisms of PRRSV infection, and the development of novel vaccines.

Porcine reproductive and respiratory syndrome (PRRS) is a highly contagious and virulent infectious disease caused by the porcine reproductive and respiratory syndrome virus (PRRSV), which has substantial economic losses in the pig industry worldwide, and PRRSV attenuated vaccines and inactivated vaccines do have limitations in immune protection. The discovery of new antiviral targets has become a new research field. The proteomic studies have shown that the PRRSV NSP2 protein interacts with tripartite motif protein 4 (TRIM4), but it was still unknown whether TRIM4 regulates PRRSV infections. In this study, the TRIM4 gene from Marc-145 cells was cloned, and it was proved that TRIM4 overexpression inhibits PRRSV replication, whereas TRIM4 small-interfering-RNA knockdown resulted in increased virus titers. Mechanism investigation indicated that TRIM4 inhibits PRRSV replication through ubiquitination and degradation of the NSP2 protein. Protease inhibitor MG132 (carbobenzoxy-Leu-Leu-leucinal) attenuated the TRIM4-driven degradation of NSP2. Taken together, TRIM4 impairs PRRSV proliferation via ubiquitination and degradation of NSP2.

Background: Porcine reproductive and respiratory syndrome (PRRS) has been present in China for about 30 years, and because of the high mutability of PRRSV, it causes huge economic losses to pig enterprises every year. PRRSV-2 is widely prevalent in China, and the detection rate of PRRSV-1 is also on the rise. Nonstructural protein 2 (NSP2) is a highly variable protein with multiple biological functions, such as PRRSV replication, which plays an important role in understanding PRRSV variation and epidemic alerts. Objectives: The epidemic characteristics and recombination of PRRSV-1 NSP2 are still unknown. The purpose of this study is to study the epidemic characteristics of PRRSV-1 NSP2 and lay a foundation for the prevention and control of PRRSV-1. Methods: In this study, we collected several PRRSV-1 and PRRSV-2 NSP2 gene sequences for gene sequence and recombination analyses, aiming to analyze the recombination pattern and genetic variation in the PRRSV-1 NSP2 genes in China. Results: The genetic similarity results showed that the 69 PRRSV-1 NSP2 gene sequences collected in this study showed nucleotide similarity ranging from 67.3% to 100.0% and amino acid similarity ranging from 64.3% to 100.0%. Amino acid sequence comparison showed that PRRSV-1 had more amino acid deletion or substitution sites than PRRSV-2. NSP2 also contains special amino acid regions such as the highly immunogenic region. PRRSV-1 can be categorized into four strains, NMEU09-1-like, BJEU06-1-like, HKEU-16-like and Amervac-like isolates, and are at different positions in the ML and NJ phylogenetic trees. In the ninety selected PRRSVs, six recombination events were detected using recombination analysis, two of which occurred in Chinese PRRSV-1 strains. Therefore, sequence analysis of NSP2 helps us to understand the prevalence and variation in PRRSV-1 in China over the past two decades and provides a theoretical basis for studying the epidemiology and evolution of NSP2.

The Akabane virus (AKAV) is a significant member of the Orthobunyavirus genus, with its envelope glycoprotein Gc, focusing on its molecular structural features, immunoregulatory mechanisms, and application value in pathogen diagnosis and vaccine design. As a key structural protein of AKAV, Gc mediates virus adsorption and neutralizing antibody recognition through the N-terminal highly variable region (HVR), while the C-terminal conserved region (CR) dominates the membrane fusion process, and its glycosylation modification has a significant regulatory effect on protein function. In clinical diagnostics, serological assays based on Gc proteins (e.g., ELISA, immunochromatographic test strips) have been standardized; in vaccine development, the neutralizing epitope of Gc proteins has become a core target for subunit vaccine design. Follow-up studies were deeply needed to analyze the structure-function interaction mechanism of Gc proteins to provide theoretical support for the construction of a new type of AKAV prevention and control system.