Comparative study of the U1, U4, and U7 strains of tobacco mosaic virus

1984 ◽  
Vol 62 (12) ◽  
pp. 2654-2659 ◽  
Author(s):  
Alain Asselin ◽  
Colette Tremblay ◽  
Guy Bellemare

Experiments were undertaken to compare three strains of tobacco mosaic virus (TMV) belonging to the tobacco group 1 of the tobamoviruses. Although the U1, U4, and U7 strains of TMV differ significantly in virulence, it was shown that these strains are very closely related. No difference was detected in the major spots of the coat protein tryptic maps and the virions from the three strains shared the same electrophoretic mobility in agarose gels with different buffer systems. The RNA fingerprints of U1 and U7 were indistinguishable and the largest T1 omega fragments of the three strains were identical in size. However, the avirulent U4 RNA fingerprint exhibited a single spot mobility difference from the U1 and U7 RNA fingerprints. This spot corresponded to the T1 phi fragment. This unique fragment is located in the so-called l2 gene between nucleotides 976 and 992 from the 3′ end. This suggests and extends the proposal that the l2 gene is most probably implicated as a factor in the control of virulence (symptomatology).

FEBS Letters ◽  
1998 ◽  
Vol 433 (3) ◽  
pp. 307-311 ◽  
Author(s):  
V.N. Orlov ◽  
S.V. Kust ◽  
P.V. Kalmykov ◽  
V.P. Krivosheev ◽  
E.N. Dobrov ◽  
...  

Biochemistry ◽  
1990 ◽  
Vol 29 (21) ◽  
pp. 5119-5126 ◽  
Author(s):  
Steven J. Shire ◽  
Patrick McKay ◽  
David W. Leung ◽  
George J. Cachianes ◽  
Eugene Jackson ◽  
...  

The Copley Medal is awarded to Dr A. Klug, F. R. S., in recognition of his outstanding contributions to our understanding of complex biological structures and the methods used for determining them. Together with D. Kaspar, Klug developed a theory that predicted the arrangement of sub-units in the protein shells of spherical viruses. This theory brought order and understanding into a confused field ; nearly all the observed structures of small spherical viruses, many of them elucidated by Klug and his collaborators, are consistent with it. After more than 20 years’ work on tobacco mosaic virus Klug and his colleagues solved the structure of its coat protein in atomic detail. They also elucidated the mechanisms by which the helical virus particle assembles itself from its RNA and its 2130 protein sub-units. Recently his group succeeded in crystallizing chromatin, and solved its structure at a resolution sufficient to see the double-helical DNA coiled around the spool of histone. Many of Klug’s successes were made possible by his introduction of Fourier image reconstruction methods into electron microscopy. Klug’s work is characterized by deep insight into the physics of diffraction and image formation and the intricate geometry of living matter.


2000 ◽  
Vol 56 (2) ◽  
pp. 71-77 ◽  
Author(s):  
VICTOR K. NOVIKOV ◽  
EKATERINA V. BELENOVICH ◽  
EVGENY N. DOBROV ◽  
SERGEI K. ZAVRIEV

Author(s):  
Jean Chatellier ◽  
Nathalie Rauffer-Bruyère ◽  
Marc H. V. Van Regenmortel ◽  
Danièle Altschuh ◽  
Etienne Weiss

Nanoscale ◽  
2018 ◽  
Vol 10 (25) ◽  
pp. 11732-11736 ◽  
Author(s):  
Sijia Gao ◽  
Xiangxiang Liu ◽  
Zhaocheng Wang ◽  
Shidong Jiang ◽  
Man Wu ◽  
...  

Fluorous ponytail modified tobacco mosaic virus coat protein can form into spherical nanoparticles through fluorous interaction induced self-assembly.


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