Characterisation of epitopes on barley mild mosaic virus coat protein recognised by a panel of novel monoclonal antibodies

2005 ◽  
Vol 150 (12) ◽  
pp. 2501-2512 ◽  
Author(s):  
D. Veliceasa ◽  
G. Tauscher ◽  
G. Surányi ◽  
P. B. Kós ◽  
I. Likó ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Coat Protein ◽  
Mosaic Virus ◽  
Mild Mosaic ◽  
Virus Coat Protein ◽  
Mild Mosaic Virus ◽  
Virus Coat

Monoclonal antibodies specific to Cucumber mosaic virus coat protein possess DNA-hydrolyzing activity

2009 ◽  
Vol 46 (7) ◽  
pp. 1527-1533 ◽  
Author(s):  
Haggag S. Zein ◽  
Jaime A. Teixeira da Silva ◽  
Kazutaka Miyatake
Keyword(s):  
Monoclonal Antibodies ◽  
Coat Protein ◽  
Cucumber Mosaic Virus ◽  
Mosaic Virus ◽  
Virus Coat Protein ◽  
Virus Coat

scholarly journals Specific amino acids of Olive mild mosaic virus coat protein are involved in transmission by Olpidium brassicae

2011 ◽  
Vol 92 (9) ◽  
pp. 2209-2213 ◽  
Author(s):  
Carla Varanda ◽  
Maria do Rosário Félix ◽  
Cláudio M. Soares ◽  
Solange Oliveira ◽  
Maria Ivone Clara
Keyword(s):  
Coat Protein ◽  
Mosaic Virus ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Mild Mosaic ◽  
Receptor Binding Site ◽  
Comparative Modelling ◽  
Mild Mosaic Virus ◽  
Olpidium Brassicae ◽  
Virus Coat

Transmission of Olive mild mosaic virus (OMMV) is facilitated by Olpidium brassicae (Wor.) Dang. An OMMV mutant (OMMVL11) containing two changes in the coat protein (CP), asparagine to tyrosine at position 189 and alanine to threonine at position 216, has been shown not to be Olpidium brassicae-transmissible owing to inefficient attachment of virions to zoospores. In this study, these amino acid changes were separately introduced into the OMMV genome through site-directed mutagenesis, and the asparagine-to-tyrosine change was shown to be largely responsible for the loss of transmission. Analysis of the structure of OMMV CP by comparative modelling approaches showed that this change is located in the interior of the virus particle and the alanine-to-threonine change is exposed on the surface. The asparagine-to-tyrosine change may indirectly affect attachment via changes in the conformation of viral CP subunits, altering the receptor binding site and thus preventing binding to the fungal zoospore.

Preparation and properties of recombinant DNA derived tobacco mosaic virus coat protein

Biochemistry ◽  
1990 ◽  
Vol 29 (21) ◽  
pp. 5119-5126 ◽  
Author(s):  
Steven J. Shire ◽  
Patrick McKay ◽  
David W. Leung ◽  
George J. Cachianes ◽  
Eugene Jackson ◽  
...  
Keyword(s):  
Coat Protein ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Recombinant Dna ◽  
Virus Coat Protein ◽  
Virus Coat

Structure of a T=1 aggregate of alfalfa mosaic virus coat protein seen at 4·5 Å resolution

1983 ◽  
Vol 167 (4) ◽  
pp. 873-890 ◽  
Author(s):  
Keiichi Fukuyama ◽  
Sherin S. Abdel-Meguid ◽  
John E. Johnson ◽  
Michael G. Rossmann ◽  
R. Huber
Keyword(s):  
Coat Protein ◽  
Mosaic Virus ◽  
Alfalfa Mosaic Virus ◽  
Virus Coat Protein ◽  
Virus Coat

Role of alfalfa mosaic virus coat protein gene in symptom formation

Virology ◽  
1991 ◽  
Vol 181 (2) ◽  
pp. 687-693 ◽  
Author(s):  
Lyda Neeleman ◽  
Antoinette C. Van Der Kuyl ◽  
John F. Bol
Keyword(s):  
Coat Protein ◽  
Mosaic Virus ◽  
Coat Protein Gene ◽  
Protein Gene ◽  
Alfalfa Mosaic Virus ◽  
Virus Coat Protein ◽  
Virus Coat ◽  
Symptom Formation
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