Epitope mapping on fragments of beet necrotic yellow vein virus coat protein

Commandeur, Ulrich; Koenig, R.; Lesemann, D.‐E.; Torrance, L.; Burgermeister, W.; Liu, Y.; Schots, A.; Alric, Monique; Grassi, Gianpaolo

doi:10.1099/0022-1317-73-3-695

Cited by 17 publications

(12 citation statements)

References 15 publications

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“…Similarly, previous studies showed an all-ornone reaction that completely abolished the reactivity because of substitutions of critical residues in the protein (24). Previous studies on mapping epitopes of plant viruses used mutants with single or double amino acid substitutions in the coat protein (25), deletion mutants ofthe coat protein (26,27), and short peptide fragments expressed in E. coli as fusion protein or free protein (28,29). Our results provide direct molecular evidence for the critical role of a single nucleotide alteration and the resulting change in the codon on the reactivity of a monoclonal antibody with severe isolates of a plant virus.…”

Section: Discussionmentioning

confidence: 75%

Molecular characterization of a structural epitope that is largely conserved among severe isolates of a plant virus.

Pappu

Manjunath

et al. 1993

Proc. Natl. Acad. Sci. U.S.A.

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Direct molecular evidence was obtained for the critical role of a single amino acid residue in a structural epitope distinguished by the monoclonal antibody MCA-13, which reacts selectively with severe isolates of citrus tristeza virus (CTV). Different CTV isolates cause a wide range of symptoms in the diverse citrus species they affect. Severe symptoms include decline, stem pitting, and seedling yellows. Plants infected by mild isolates are essentially symptomless. The monoclonal antibody MCA-13, which discriminates severe isolates from mild isolates of the virus, was used to map its epitope on the coat protein of CTV. A diverse group of coat protein genes of geographically and biologically distinct CTV isolates which are either MCA-13-reactive or MCA-13-nonreactive was cloned and sequenced. A series of mutant coat protein genes was constructed through oligonucleotidedirected, site-specific mutagenesis. The reactivity of the wildtype and mutant coat proteins expressed in Escherchia coli was evaluated by Western blotting using MCA-13 and polyclonal antibody prepared to CTV-coat protein. A single nucleotide alteration resulting in a Phe --Tyr mutation at position 124 of the coat protein abolished the MCA-13 reactivity of a severe isolate, whereas a Tyr -* Phe mutation at the same site conferred MCA-13 reactivity on the coat protein of a previously nonreactive mild isolate of CTV.

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Section: Discussionmentioning

confidence: 75%

Molecular characterization of a structural epitope that is largely conserved among severe isolates of a plant virus.

Pappu

Manjunath

et al. 1993

Proc. Natl. Acad. Sci. U.S.A.

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“…We had previously identified five antigenic regions on the coat protein of BNYVV. Four of these are accessible on the intact particles (Commandeur et al, 1992(Commandeur et al, , 1994 and may, therefore, also contribute to the formation of discontinuous epitopes. None of the amino acid changes in the three different coat protein sequences occurs within these antigenic regions (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…4. Antigenic areas on BNYVV coat protein (Commandeur et aL, 1992(Commandeur et aL, , 1993 and amino acid (aa) exchanges in various isolates Meulewater et al, 1989;Yao et al, 1993;this paper). The underlined sequences are accessible on the intact particles and may therefore be expected to participate also in the formation of surface-located discontinuous epitopes.…”

Section: Discussionmentioning

confidence: 99%

Restriction fragment length polymorphism analysis of reverse transcription-PCR products reveals the existence of two major strain groups of beet necrotic yellow vein virus

Kruse¹,

Koenig²,

Hoffmann³

et al. 1994

Journal of General Virology

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Beet necrotic yellow vein virus (BNYVV)-infected sugarbeets were obtained from many parts of Europe and also from some sites in Asia and the U.S.A. Reverse transcription (RT)-PCR products of more than I kbp were obtained for four different regions of the viral genome which may be particularly important with respect to the pathogenic properties of the virus, i.e. for the coat protein and the 42K protein-encoding regions on RNA 2 and for major parts ofRNAs 3 and 4. Restriction fragment length polymorphism (RFLP) patterns obtained with these PCR products revealed the existence of two major strain groups of BNYVV, named type A and type B. The A type was detected in Greece, the former Yugoslavia, Slovakia, parts of Austria, Italy, Spain, parts of France, Belgium, The Netherlands and England as well as in Asia (Turkey, Kazachstan, China and Japan) and the U.S.A. The B type occurs in Germany and parts of France. Mixed infections were detected at the borderline regions between areas of the A and B types. Comparisons of published and newly determined nucleotide sequences of the respective parts of the BNYVV genome indicate that the percentage of nucleotide differences between the A and the B type is approximately 3 % for the respective regions of RNAs 2 and 3 and approximately 1.5 % for RNA 4. Nucleotide sequences appear to be remarkably stable within each of the two strain groups. The majority of the nucleotide differences between the A and B types occur in the third triplet position. The amino acid changes in the coat protein area are outside the four previously determined antigenic regions that are accessible on the surface of the virus particles and are involved in the formation of continuous and presumably also discontinuous epitopes. This may explain why serological differences between the two strain groups have not been found.

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“…A complete epitope map has been reported for a few rodshaped viruses. Beet necrotic yellow vein virus, with a 25K coat protein, exhibited seven epitopes (Commandeur et al, 1992). Ten epitopes have been reported for the 35K capsid protein of Johnsongrass mosaic virus (JGMV; Shukla & Ward, 1989) and nine epitopes were identified on the 35K coat protein of PStV, AzMV and B1CMV (Hasselmann et at., 1993).…”

Section: Discussionmentioning

confidence: 99%

Capsid protein properties of cowpea aphid-borne mosaic virus and blackeye cowpea mosaic virus confirm the existence of two major subgroups of aphid-transmitted, legume-infecting potyviruses

Huguenot

Furneaux²,

Hamilton³

1994

Journal of General Virology

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A study of the capsid proteins of different legumeinfecting potyviruses using specific monoclonal antibodies on immunoblots of crude extracts from infected plants revealed that cowpea aphid-borne mosaic virus (CAMV) and blackeye cowpea mosaic virus (B1CMV) have coat protein Mr values of 32K and 35K, respectively. Immunoblot comparisons of BICMV, peanut stripe mosaic virus (PStV), bean common mosaic virus (BCMV) and azuki bean mosaic virus (AzMV) revealed equal reactivity of their 35K coat proteins. Similar comparisons between CAMV and the necrotic strain of BCMV (isolate NL3) showed a serological relationship between their 32K coat proteins, results providing the first evidence of a possible similarity between CAMV and BCMV NL3. Peptides from trypsin digests of the coat proteins of several of these legume-infecting potyviruses were analysed by HPLC. Comparison of the peptide profiles confirmed the serological results in distinguishing the two subgroups. Peptide profiles of coat protein from B1CMV, PStV, AzMV and BCMV were almost identical, results suggesting that they could be considered as strains of one virus. In contrast, peptide profiles of various CAMV serotypes and BCMV NL3 were distinct from the first group and exhibited limited similarities to each other.

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Epitope mapping on fragments of beet necrotic yellow vein virus coat protein

Cited by 17 publications

References 15 publications

Molecular characterization of a structural epitope that is largely conserved among severe isolates of a plant virus.

Molecular characterization of a structural epitope that is largely conserved among severe isolates of a plant virus.

Restriction fragment length polymorphism analysis of reverse transcription-PCR products reveals the existence of two major strain groups of beet necrotic yellow vein virus

Capsid protein properties of cowpea aphid-borne mosaic virus and blackeye cowpea mosaic virus confirm the existence of two major subgroups of aphid-transmitted, legume-infecting potyviruses

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