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The Porcine epidemic diarrhea virus spike protein subunit 1 (PEDV-S1) is the N-terminal subunit of the large spike glycoprotein, playing a fundamental role in the initial stages of viral pathogenesis. It contains the receptor-binding domain (RBD) and multiple neutralizing epitopes, making it the primary target for host immune responses and vaccine development (Li et al., 2016, Journal of Virology). The S1 subunit facilitates viral attachment by binding to host cell receptors, including porcine aminopeptidase N (pAPN) and various sialic acid residues, which triggers the subsequent membrane fusion mediated by the S2 subunit (Nam & Lee, 2021, Viruses). In the field, PEDV-S1 is the driver of Porcine Epidemic Diarrhea, a disease causing high mortality in neonatal piglets due to severe malabsorptive diarrhea and dehydration. From a therapeutic perspective, most recombinant vaccines and neutralizing antibodies are designed to target the S1 region to prevent viral entry. However, significant genetic diversity and frequent mutations within the S1 gene lead to the emergence of new strains, posing a challenge for the efficacy of traditional vaccines and the development of universal therapeutic agents (Sun et al., 2018, Vaccine).
Neutralization of viral infection by blocking the receptor-binding domain (RBD) within the S1 subunit, preventing the virus from attaching to host receptors such as porcine aminopeptidase N (pAPN) or sialic acids.
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