POLARITY OF BINDING OF MONOCLONAL-ANTIBODIES TO TOBACCO MOSAIC-VIRUS RODS AND STACKED DISKS

被引:21
作者
DORE, I
RUHLMANN, C
OUDET, P
CAHOON, M
CASPAR, DLD
VANREGENMORTEL, MHV
机构
[1] CNRS,INST BIOL MOLEC & CELLULAIRE,15 RUE DESCARTES,F-67084 STRASBOURG,FRANCE
[2] BRANDEIS UNIV,ROSENSTIEL BASIC MED SCI RES CTR,WALTHAM,MA 02254
[3] FAC MED STRASBOURG,CNRS,GENET MOLEC EUCARYOTES LAB,F-67085 STRASBOURG,FRANCE
关键词
D O I
10.1016/0042-6822(90)90226-H
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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 α-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. © 1990.
引用
收藏
页码:25 / 29
页数:5
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