Polarity of binding of monoclonal antibodies to tobacco mosaic virus rods and stacked disks.
Monoclonal antibodies to tobacco mosaic virus that bind only to one end of the viral rods have been shown to recognize the surface of the protein subunit designated as the bottom, which contains the right radial and left radial alpha-helices. The specificity of the antibody binding was established by immunoelectron microscopy of complexes in which the 5' end of the RNA had been exposed at the bottom of the helical virus particle. These antibodies have been shown to bind to both ends of the stacked disk aggregate of TMV protein, which is therefore bipolar. The observations on the bipolarity of this structure are inconsistent with the presumption that stacked disks are formed by aggregation of polar two-layer disks.
Dore
I
I
Institut de Biologie Moléculaire et Cellulaire du CNRS, Strasbourg, France.
Ruhlmann
C
C
Oudet
P
P
Cahoon
M
M
Caspar
D L
DL
Van Regenmortel
M H
MH
D000911:Antibodies, Monoclonal; D000918:Antibody Specificity; D012367:RNA, Viral / Q000648:ultrastructure; D014027:Tobacco Mosaic Virus / Q000276:immunology* / Q000648:ultrastructure; D014764:Viral Proteins / Q000648:ultrastructure
D000911:Antibodies, Monoclonal; D012367:RNA, Viral; D014764:Viral Proteins