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The St. Louis encephalitis virus (SLEV) envelope protein is the primary surface glycoprotein of the virus and a member of the Flaviviridae family [1]. It plays a critical role in the viral life cycle by mediating attachment to host cell receptors and facilitating the fusion of the viral envelope with the host endosomal membrane during entry [2]. Structurally, the E protein exists as a head-to-tail homodimer on the surface of mature virions and undergoes a significant conformational change at low pH to trigger fusion [3]. As the principal target for neutralizing antibodies, it is the focus of vaccine development and therapeutic antibody research [4]. While no specific antiviral drugs are currently approved to target this protein, it remains a key candidate for entry inhibitors [5]. Understanding its structure is also vital for diagnostic purposes, as it is the primary antigen used in serological assays [1]. However, cross-reactivity with other flaviviruses like West Nile virus presents a significant diagnostic and therapeutic challenge [6].
Neutralization of viral infection by inhibiting attachment to host receptors or preventing the low-pH-induced conformational change necessary for membrane fusion [2, 3].
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