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Bovine respiratory syncytial virus (BRSV) antigens are the primary molecular targets for the prevention and treatment of respiratory disease in cattle. BRSV is an enveloped, negative-sense, single-stranded RNA virus belonging to the family Pneumoviridae [3, 12]. The most significant antigens are the fusion (F) and attachment (G) glycoproteins, which mediate viral entry and are the main targets for neutralizing antibodies [1, 16]. The F protein is responsible for the fusion of the viral envelope with the host cell membrane and the formation of multinucleated syncytia, a hallmark of the infection [7, 17]. The G protein facilitates attachment to host cells via sialic acid residues or CX3CR1 receptors [7, 12]. Other antigens include the nucleocapsid (N) protein, which is involved in RNA replication, and non-structural proteins (NS1 and NS2) that antagonize the host's interferon response [6, 12]. Therapeutic strategies primarily involve vaccines (modified-live or inactivated) that aim to induce protective immunity [1, 13]. However, a major challenge in BRSV target engagement is the risk of vaccine-enhanced respiratory disease (VAERD), particularly with formalin-inactivated antigens, which can lead to severe pulmonary inflammation and a Th2-biased immune response [7, 16]. Experimental small-molecule fusion inhibitors and monoclonal antibodies are also being explored as potential treatments [4, 15].
Vaccines induce neutralizing antibodies and T-cell responses against viral proteins (primarily F and G) to prevent infection and disease. Fusion inhibitors (e.g., GS1) bind to the F protein to block the fusion of the viral envelope with the host cell membrane. Monoclonal antibodies (e.g., palivizumab) neutralize the virus by binding to specific epitopes on the F protein, preventing viral entry.
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