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The Classical Swine Fever Virus (CSFV) envelope glycoprotein E2 is the most immunogenic protein of the virus and a critical component for viral entry into host cells (UniProt P19712). It exists as a 55 kDa glycoprotein that typically forms disulfide-linked homodimers or heterodimers with the E1 protein on the viral surface (PubMed: 31336624). E2 is responsible for binding to porcine cellular receptors and facilitating the fusion of the viral envelope with the host endosomal membrane. Because it contains the primary neutralizing epitopes of the virus, E2 is the central target for the development of both modified live and subunit vaccines, as well as diagnostic assays (PubMed: 28655821). In the context of the porcine immune system, recognition of E2 by B-cells and T-cells is essential for clearing the infection and providing long-term immunity against Classical Swine Fever (PubMed: 30203145). Therapeutic strategies focus on eliciting high titers of anti-E2 antibodies to neutralize the virus before it can establish systemic infection.
Induction of neutralizing antibodies and T-cell responses to block viral entry and replication.
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