Why the study?
To better understand the structure and function of the porcine reproductive and respiratory syndrome virus E protein.
The PRRSV E protein plays a critical role in viral infectivity, ion channel activity, and modulation of the host immune response.
E protein deletion blocks transmissible PRRSV particles; leaves open its utility for live-attenuated vaccines pending validation.
Porcine reproductive and respiratory syndrome (PRRS) is an economically important disease impacting the global pig industry, and it is characterized by reproductive disorder in sows and respiratory disorder in pigs of all ages. The PRRSV E protein is a nonglycosylated structural protein encoded by the ORF2b gene. The E protein is not necessary for the assembly of virus particles, but deletion of the E protein leads to transmissible virus particles not being produced. To better understand the structure and function of the E protein, we reviewed its genetic and evolutionary analysis, characteristics, subcellular localization and topology, ion channel activity, cellular immune response, additional biological functions, interactions with host proteins, interactions with PRRSV proteins, roles in infection, pathogenicity, and drugs. Therefore, this review can provide a theoretical basis for gaining an in-depth understanding of the E protein of PRRSV-2.
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Chen et al. (2023) studied this question.
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