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Vaccinia virus B5R is a 42-kDa type I membrane glycoprotein that is a critical component of the extracellular enveloped virus (EEV) membrane [3, 4]. It belongs to the complement control protein (CCP) superfamily and contains four short consensus repeats (SCRs) in its extracellular domain [3, 4]. B5R is essential for the wrapping of intracellular mature virions (IMV) to form intracellular enveloped virions (IEV) and for the induction of actin tails that facilitate cell-to-cell spread [3, 15]. As a major target for neutralizing antibodies, B5R is a key determinant of the protective efficacy of smallpox and mpox vaccines [5, 12, 14]. Therapeutic interventions, such as Vaccinia Immune Globulin (VIG), primarily target B5R to neutralize EEV and prevent the systemic dissemination of the virus [5, 17]. Its conservation across orthopoxviruses makes it a significant target for the development of broad-spectrum poxvirus therapeutics and vaccines [4, 14].
Neutralization of extracellular enveloped virus (EEV) and inhibition of viral spread by binding to the B5R protein on the EEV membrane.
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