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Variola virus protein B5 (also known as B6R in the Variola genome) is a type I transmembrane glycoprotein essential for the formation and dissemination of the extracellular enveloped virus (EEV) form of the smallpox virus [8, 15]. It is located on the outer membrane of the EEV and plays a pivotal role in the wrapping of mature virions and their subsequent egress from the host cell [15]. The protein's extracellular domain contains four short consensus repeat (SCR) motifs, which are characteristic of the complement control protein (CCP) family, suggesting that B5 helps the virus evade the host's complement system [10, 15]. Because B5 is a major target for neutralizing antibodies that prevent the spread of the virus between cells, it is a primary candidate for the development of subunit vaccines and therapeutic antibodies [8, 10]. Although smallpox has been eradicated, B5 remains a critical target for biodefense research and the development of medical countermeasures against potential re-emergence or related orthopoxviruses [1, 13].
Neutralization of extracellular enveloped virions (EEV) and inhibition of viral spread by blocking B5-mediated egress and cell-to-cell transmission.
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