The N-terminal region of the VP1 protein of swine vesicular disease virus contains a neutralization site that arises upon cell attachment and is involved in viral entry.
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.
Jiménez-Clavero
M A
MA
Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria (INIA), 28040 Madrid, Spain. majimene@inia.es
Escribano-Romero
E
E
Douglas
A J
AJ
Ley
V
V
D000595:Amino Acid Sequence; D000818:Animals; D000914:Antibodies, Viral / Q000276:immunology*; D002213:Capsid / Q000737:chemistry* / Q000235:genetics / Q000276:immunology*; D002460:Cell Line; D003588:Cytopathogenic Effect, Viral; D004770:Enterovirus / Q000737:chemistry / Q000276:immunology / Q000502:physiology*; D008969:Molecular Sequence Data; D009500:Neutralization Tests; D011487:Protein Conformation; D013552:Swine; D013555:Swine Vesicular Disease / Q000821:virology
D000914:Antibodies, Viral