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The Yellow fever virus (YFV) polyprotein is a single large precursor protein that is processed into three structural proteins (C, prM, and E) and seven non-structural proteins (NS1, NS2A, NS2B, NS3, NS4A, NS4B, and NS5) [1]. These proteins function as the primary immunological targets for the host's immune system during infection and are the basis for vaccine development [2]. The Envelope (E) protein is the most significant antigen, as it mediates viral attachment and membrane fusion, and is the primary target for neutralizing antibodies [3]. Non-structural proteins like NS3 (protease/helicase) and NS5 (RNA-dependent RNA polymerase) are essential for viral replication and represent potential targets for small-molecule antiviral drugs, although none are currently approved [4]. Yellow fever is a severe mosquito-borne viral infection characterized by high fever, jaundice, and hemorrhagic symptoms, which can lead to high mortality rates in unvaccinated populations [5]. The live-attenuated 17D vaccine utilizes these viral antigens to induce robust, long-lasting humoral and cellular immunity [6]. While the vaccine is highly effective, the antigens can occasionally trigger severe adverse events such as vaccine-associated viscerotropic or neurotropic disease [5]. Monitoring of these antigens and the resulting antibody response is crucial for diagnosing infection and assessing vaccine efficacy [2].
Induction of neutralizing antibodies against the Envelope (E) protein and activation of T-cell mediated immunity to prevent viral entry and replication.
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