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Canine distemper virus (CDV) antigens, specifically the hemagglutinin (H) and fusion (F) glycoproteins, are the primary targets for both preventive and therapeutic interventions against canine distemper. The H protein is responsible for binding to host cell receptors such as SLAM (CD150) and Nectin-4, while the F protein mediates the fusion of the viral envelope with the host cell membrane (UniProt, P0DOG1). These surface antigens are the critical components of commercial vaccines, which aim to elicit a robust neutralizing antibody response to block viral entry (PubMed, 25231301). In addition to the surface glycoproteins, the nucleocapsid (N) protein is a major target for diagnostic assays due to its high expression levels during viral replication. While vaccination remains the primary method of control, research into small-molecule antivirals focuses on inhibiting the H-F protein complex or the viral polymerase to treat active infections (Journal of Virology, 2011). Understanding the structural biology of these antigens is vital for addressing the virus's broad host range, which includes various terrestrial and aquatic carnivores.
Vaccines targeting these antigens induce the production of neutralizing antibodies and cell-mediated immunity, primarily directed against the hemagglutinin (H) and fusion (F) proteins to prevent viral attachment and entry into host cells (Merck Veterinary Manual). Experimental small-molecule inhibitors like AS-136 act as fusion inhibitors by blocking the conformational changes of the F protein, while others like ERDRP-0519 target the viral RNA-dependent RNA polymerase to inhibit replication (Journal of Virology, 2014).
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