Detection of potyviruses with antisera to synthetic peptides

Joisson, Carole; Dubs, M.C.; Briand, Jean Paul; Regenmortel, M.H.V. Van

doi:10.1016/s0923-2516(06)80101-9

Cited by 17 publications

(7 citation statements)

References 33 publications

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“…In silico prediction and experimental validation of cross-reactivity with other potyviruses Antibodies raised against PVY show in many cases cross-reactivity with other potyviruses (Joisson et al, 1992;Jordan, 1992). The classical method to determine the specificity of monoclonal antibodies is to test them randomly with other potyviruses.…”

Section: Location Of the Epitopesmentioning

confidence: 99%

Epitope identification and in silico prediction of the specificity of antibodies binding to the coat proteins of Potato Virus Y strains

et al. 2005

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A phage library containing 2.7 · 10 9 randomly expressed peptides was used to determine the epitopes of three monoclonal antibodies that bind to the coat protein of potato virus Y. Construction of the consensus sequences for the peptides obtained after three selection rounds indicated that each antibody recognized a different epitope located within the first 50 N-terminal amino acids of the coat protein. The location of the epitopes was confirmed by heterologous expression of the N-terminal part of the coat protein in Escherichia coli, and, subsequently, by performing an immunological test with the three antibodies. The accuracy of the phage library was demonstrated by predicting in silico the cross-reactivity of the three antibodies with other potyvirus family members. ELISA and in silico predictions revealed the same results in almost every case. The potential of peptide phage libraries to optimize the use of antibodies in plant virology is discussed.

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Section: Location Of the Epitopesmentioning

confidence: 99%

Epitope identification and in silico prediction of the specificity of antibodies binding to the coat proteins of Potato Virus Y strains

et al. 2005

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“…To make a peptide, which does not contain a T-cell epitope immunogenic, it was commonly accepted that the peptide must be covalently coupled to the T-cell epitope. A common, but cumbersome, procedure to obtain antibodies against a peptide is to conjugate it to a protein or a peptide containing a potent T-cell epitope [1][2][3][4]. Lately it has been recognized that in some cases a covalent link between Tand B-cell epitopes is not mandatory [5,6].…”

Section: Introductionmentioning

confidence: 99%

Hierarchic T‐Cell Help to Non‐Linked B‐Cell Epitopes

et al. 1996

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The induction of antibodies against peptides requires the presence of a T helper cell epitope. In the absence of an added T-cell epitope only 10% of the mice, or less depending on the strain, gave an antibody response to a series of peptides of the measles virus (MV) fusion (F) protein. After coimmunization with a non-covalently coupled T-cell epitope more than 60% of the peptides became immunogenic. Considerable differences became apparent when BALB/c mice were immunized with peptides in the presence of different T-cell epitopes. An immunodominant T-cell epitope of the MV-F protein was more efficient than a subdominant or a cryptic T-cell epitope in providing help to a non-linked B-cell epitope. There is both a ranking order of the amount of help which B-cell epitopes require and a ranking order for the help T-cell epitopes are able to provide. The capability of a T-cell epitope to provide help to a B-cell epitope correlated with its own immunogenicity, i.e. the intensity of the antibody response to the peptide representing the T-cell epitope. The data suggest that for each MHC class II allele there is an optimal T-cell epitope which can provide help to a maximal number of B-cell epitopes and that such a peptide can be identified by its ability to induce antibodies against itself. By using this strategy, the authors were able to induce antibodies which cross-reacted with the MV.

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“…The most antigenic epitopes were found in the N-terminal and C-terminal regions of the PVY CP (Vihinen-Ranta et al 1994). This was confirmed for potyviruses in general by Joisson et al (1992). Although the localization of discontinuous epitopes could not be precisely determined, based on the competition ELISA, it is likely that the epitope for MAb 534 is close to either of the CP termini.…”

Section: Resultsmentioning

confidence: 78%