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The Extracellular enveloped virus envelope glycoprotein B5 (B5R) is a critical type I transmembrane glycoprotein found on the surface of the extracellular enveloped virus (EEV) form of orthopoxviruses, including Variola and Vaccinia viruses [1]. It plays a fundamental role in the viral life cycle by facilitating the wrapping of intracellular mature virus (IMV) particles and their subsequent egress from the host cell [2]. B5R is also essential for the induction of actin-based motility, which allows the virus to spread efficiently from cell to cell while remaining protected from the host's immune system [3]. Because the EEV form is responsible for long-range spread within the host and is relatively resistant to antibodies that target the IMV form, B5R is a primary target for neutralizing antibodies and a key focus for therapeutic development [4]. Current clinical approaches include the use of Vaccinia Immune Globulin (VIG), while experimental strategies involve monoclonal antibodies like c89 and 6C that specifically target B5R to inhibit viral spread [5]. Additionally, B5R is a vital antigen in the development of next-generation subunit and DNA vaccines designed to provide protection against smallpox, mpox, and other orthopoxvirus threats [6].
Neutralization of the extracellular enveloped virus (EEV) form to inhibit viral dissemination and cell-to-cell spread.
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