The SVDV capsid undergoes a temperature-independent conformational change upon cell binding that exposes the N-terminus of VP1, making it a target for neutralizing antibodies.
Exploiting attachment-exposed VP1 epitopes may guide antibody design; leaves open translation beyond animal models.
The N-terminal region of VP1 of swine vesicular disease virus (SVDV) is highly antigenic in swine, despite its internal location in the capsid. Here we show that antibodies to this region can block infection and that allowing the virus to attach to cells increases this blockage significantly. The results indicate that upon binding to the cell, SVDV capsid undergoes a conformational change that is temperature independent and that exposes the N terminus of VP1. This process makes this region accessible to antibodies which block virus entry.
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Jiménez‐Clavero et al. (2001) studied this question.
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