scholarly journals Mapping antigenic epitopes of potato virus Y with antibodies affinity-purified by using overlapping synthetic peptides

1994 ◽  
Vol 3 (2) ◽  
pp. 207-211
Author(s):  
Maija Vihanen-Rantanen ◽  
Reijo Sironen ◽  
Matti Vuento
Keyword(s):  
Amino Acid ◽  
Coat Protein ◽  
Amino Acid Sequence ◽  
Potato Virus ◽  
Synthetic Peptides ◽  
Potato Virus Y ◽  
Detection Methods ◽  
Polyclonal Antisera ◽  
Antigenic Epitopes

Synthetic, overlapping peptides representing the entire amino acid sequence of potato virus Y (PVY) coat protein were used to affinity-purify antibodies from polyclonal antisera to PVY. In testing the binding of the purified antibodies to PVY particles, antigenic epitopes were identified. The N-terminal and C-terminal regions of the PVY coat protein were found to contain most of the antigenic epitopes. The results will facilitate the development of detection methods for PVY based on synthetic peptides.

Coat protein of potyviruses 2. amino acid sequence of the coat protein of potato virus Y

Virology ◽  
1986 ◽  
Vol 152 (1) ◽  
pp. 118-125 ◽  
Author(s):  
Dharma D. Shukla ◽  
Adam S. Inglis ◽  
Neil M. McKern ◽  
Keith H. Gough
Keyword(s):  
Amino Acid ◽  
Coat Protein ◽  
Amino Acid Sequence ◽  
Potato Virus ◽  
Potato Virus Y

scholarly journals Prediction of antigenic epitopes for coat protein of Potato virus Y, Egypt

2019 ◽  
Vol 3 (2) ◽  
pp. 297-313
Author(s):  
Seham Abdel-Shafi ◽  
Ghaly Mohamed Farouk ◽  
Mohamed Taha ◽  
Khalid El-Dougdoug
Keyword(s):  
Coat Protein ◽  
Potato Virus ◽  
Potato Virus Y ◽  
Antigenic Epitopes

Prediction of Antigenic Epitopes for Coat Protein of Potato virus Y

2011 ◽  
Vol 183-185 ◽  
pp. 1204-1208
Author(s):  
Shi Hui Guo ◽  
Chun Lei Wang ◽  
Hong Yi Yang ◽  
Na Na Zhang ◽  
Xin Zhuang ◽  
...  
Keyword(s):  
Coat Protein ◽  
Potato Virus ◽  
Potato Virus Y ◽  
Amino Acid Position ◽  
Computer Assisted ◽  
Coil Structure ◽  
Α Helix ◽  
Assisted Analysis ◽  
Β Sheet ◽  
Antigenic Epitopes

Potato virus Y (PVY) is one of the most important viruses that infect Solanaceous crops. In the study, the antigenic epitopes were predicted using computer-assisted analysis, and many potential regions of antigenic epitopes were located. Many properties of coat protein, such as the antigenic index, α-helix, β-sheet, β-turn, coil structure, hydrophilicity, surface probability, and flexibility, were analyzed with several algorithms in some softwares. Based on the rules for location the antigenic epitopes in the regions including β-turns and coil structures with the high hydrophilicity and surface probability, the predicted epitopes were located in the region of amino acid position 8-22, 24-38, 45-55, 240-255, respectively. It is helpful to prepare the antiserum of PVY based on the prediction result of antigenic epitope.

Molecular characterization of coat protein genes of serologically distinct isolates of potato virus Y necrotic strain

1997 ◽  
Vol 43 (7) ◽  
pp. 677-683 ◽  
Author(s):  
A. K. Dhar ◽  
R. P. Singh
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Coat Protein ◽  
Potato Virus ◽  
Sequence Comparison ◽  
Potato Virus Y ◽  
Protein Gene ◽  
Hydrophobic Amino Acids ◽  
Amino Acid Levels

The coat protein (CP) genes of two potato virus Y necrotic isolates (N27 and a mutant strain N27-92), which differed in their reactivity to a monoclonal antibody (mab), were characterized. Both isolates could be detected by mab 4E7, but mab VN295.5 selectively reacted to N27 and not to N27-92. The CP genes of both isolates coded for 267 amino acids with ~99.0% identity at both the nucleotide and the amino acid levels. Nucleotide sequence comparison indicated five substitutions in N27-92 compared with N27. Three of these changes resulted in substitution of amino acids. Two transitions (A→G) in N27-92 changed threonine to alanine and lysine to arginine at positions 7 and 55, respectively, whereas a A→T transversion changed asparagine to isoleucine at position 27. The surface probability curves of both the isolates could almost be superimposed, except at amino acid positions 7 and 27. Since amino acid substitution at position 55 is conservative, changes from polar to hydrophobic amino acids (threonine→alanine and asparagine→isoleucine) at positions 7 and 27 might have changed the epitope(s) of N27-92, abolishing its detection by mab VN295.5.Key words: potato virus Y, PVYN, coat protein gene.

scholarly journals Characterization of Antigenic Epitopes of the Coat Protein of Potato Virus X by Systematic Immunochemical Analysis of Synthetic Peptides.

1993 ◽  
Vol 47 ◽  
pp. 994-998
Author(s):  
Matti Vuento ◽  
Maija Vihinen-Ranta ◽  
Katariina Paananen ◽  
Soile Blomqvist ◽  
Aarne Kurppa ◽  
...  
Keyword(s):  
Coat Protein ◽  
Potato Virus ◽  
Synthetic Peptides ◽  
Potato Virus X ◽  
Immunochemical Analysis ◽  
Antigenic Epitopes

scholarly journals Evidence for diversifying selection in Potato virus Y and in the coat protein of other potyviruses

2002 ◽  
Vol 83 (10) ◽  
pp. 2563-2573 ◽  
Author(s):  
Benoît Moury ◽  
Caroline Morel ◽  
Elisabeth Johansen ◽  
Mireille Jacquemond
Keyword(s):  
Amino Acid ◽  
Coat Protein ◽  
Mosaic Virus ◽  
Potato Virus ◽  
Potato Virus Y ◽  
Yellow Mosaic Virus ◽  
Likelihood Method ◽  
Evolutionary Constraints ◽  
Coat Proteins ◽  
Diversifying Selection

The modes of evolution of the proteins of Potato virus Y were investigated with a maximum-likelihood method based on estimation of the ratio between non-synonymous and synonymous substitution rates. Evidence for diversifying selection was obtained for the 6K2 protein (one amino acid position) and coat protein (24 amino acid positions). Amino acid sites in the coat proteins of other potyviruses (Bean yellow mosaic virus, Yam mosaic virus) were also found to be under diversifying selection. Most of the sites belonged to the N-terminal domain, which is exposed to the exterior of the virion particle. Several of these amino acid positions in the coat proteins were shared between some of these three potyviruses. Identification of diversifying selection events in these different proteins will help to unravel their biological functions and is essential to an understanding of the evolutionary constraints exerted on the potyvirus genome. The hypothesis of a link between evolutionary constraints due to host plants and occurrence of diversifying selection is discussed.

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