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Herpesvirus glycoprotein B (gB) is a highly conserved envelope protein found on all herpesviruses, including Herpes simplex virus type 1 (HSV‑1). It is a type I transmembrane protein that forms trimeric spikes on the viral envelope. As an essential component of the "core fusion machinery," along with other viral proteins such as gD and the gH/gL complex, gB mediates the critical step of fusing the viral envelope with host cell membranes during entry. The structure consists of five domains with specialized functions—domain I contains internal fusion loops that insert into cellular membranes; domain II interacts with other viral proteins; domain IV may interact with cellular receptors. The transition between prefusion and postfusion conformations enables membrane merger but also complicates immune recognition. Neutralizing antibodies targeting multiple domains can block infection by interfering with these processes. Due to its central role in infectivity and immunogenicity, gB is a major target for vaccine development and antiviral research against herpesvirus infections[2][3][4].
Inhibition of virus-cell membrane fusion (by neutralizing antibodies or experimental inhibitors)[3][4]
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