Influence of the C terminus of the small protein subunit of bean pod mottle virus on the antigenicity of the virus determined using monoclonal antibodies and anti-peptide antiserum

Joisson, Carole; Regenmortel, M.H.V. Van

doi:10.1099/0022-1317-72-9-2225

Cited by 8 publications

(11 citation statements)

References 27 publications

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“…The three-dimensional structures of BPMV and of cowpea mosaic virus (CPMV), another comovirus, have been determined by X-ray crystallography [8,33]. Monoclonal antibodies to CPMV [16,17] and to BPMV [15] have been used to analyze the antigenic structure of the two viruses. In the case of BPMV, it was found that the C-terminal region of the small subunit played a dominant role in the antigenicity of the virus [15].…”

Section: Introductionmentioning

confidence: 99%

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Antigenic analysis of bean pod mottle virus using linear and cyclized synthetic peptides

Joisson

Kuster²,

Plaué³

et al. 1993

Archives of Virology

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The antigenic structure of the comovirus bean pod mottle virus (BPMV) was studied using synthetic peptides selected on the basis of the exposed location of certain regions of the viral protein. Three regions of domain A, four regions of domain B and two regions of domain C of BPMV coat protein were studied. Each of four regions were synthesized in the form of linear and cyclized peptides while the others were synthesized as linear peptides only. The peptides were tested for their ability to be recognized by antibodies directed against BPMV. The peptides were also used for producing rabbit antisera, which were tested for their ability to react with various BPMV antigens as well as with the linear and cyclized peptides. All the peptides were found to correspond to epitopes of BPMV coat protein. Several of the antigenic sites of BPMV located on exposed loops of the coat protein occupy positions which correspond to known epitopes in the structurally related picornaviruses. Only in some cases did cyclization sufficiently improve the level of conformational mimicry between peptides and the viral protein to allow cross-reactions between them to be observed.

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Section: Introductionmentioning

confidence: 99%

“…Monoclonal antibodies to CPMV [16,17] and to BPMV [15] have been used to analyze the antigenic structure of the two viruses. In the case of BPMV, it was found that the C-terminal region of the small subunit played a dominant role in the antigenicity of the virus [15].…”

Section: Introductionmentioning

confidence: 99%

Antigenic analysis of bean pod mottle virus using linear and cyclized synthetic peptides

Joisson

Kuster²,

Plaué³

et al. 1993

Archives of Virology

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“…One or more of the loops in VP 1 of many picornaviruses is antigenic (see Chapman eta[., 1990) and one in foot-andmouth disease virus VP1 is the most immunodominant (Brown, 1995). Similarly, the C terminus of the small protein of bean pod mottle comovirus, which is analogous to VP1, plays a dominant role in the antigenicity of the virus (Joisson & van Regenmortel, 1991).…”

Section: Results and Discussion Cp3 Is A Dominant Antigenic Determinamentioning

confidence: 99%

Immunological characterization of rice tungro spherical virus coat proteins and differentiation of isolates from the Philippines and India

Druka

Burns

Zhang

et al. 1996

Journal of General Virology

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Rice tungro spherical virus (RTSV) has an RNA genome of more than 12 kb with various features which classify it as a plant picornavirus. The capsid comprises three coat protein (CP) species, CPI, CP2 and CP3, with predicted molecular masses of 22"5, 22.0 and 33 kDa, respectively, which are cleaved from a polyprotein. In order to obtain information on the properties of these proteins, each was expressed in E. coil, purified as a fusion to the maltose-binding protein and used for raising a polyclonal antiserum. CP1, CP2 and CP3 with the expected molecular masses were detected specifically in virus preparations. CP3 is probably the major antigenic determinant on the surface of RTSV particles, as was shown by ELISA, Western blotting and immunogold electron microscopy using antisera obtained against whole virus particles and to each CP separately. In some cases, especially in crude extracts, CP3 antiserum detected several other proteins (40-42 kDa), which could be products of CP3 post-translational modification. No serological differences were detected between the three CPs from isolates from the Philippines, Thailand, Malaysia and India. The CP3-related 40-42 kDa proteins of the Indian RTSV isolate have a slightly higher electrophoretic mobility (42-44 kDa) and a different response to cellulolytic enzyme preparations, which allows them to be differentiated from south-east Asian isolates.

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“…Previous studies with another potyvirus, tobacco etch virus, showed that MAbs which differentiated between aphid transmissible and non-transmissible strains were also directed against the N-terminal region of the viral coat protein [6-]. The presence of epitopes in the N and C terminal regions of proteins is a common feature of the antigenic structure of plant viruses I- 3,7,10,20,23].…”

Section: Discussionmentioning

confidence: 98%

Characterization of epitopes recognized by monoclonal antibodies to aphid transmissible and non-transmissible strains of turnip mosaic virus

Kantrong

Sako

1993

Archives of Virology

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Fourteen monoclonal antibodies (MAbs) were prepared against two strains of turnip mosaic virus (TuMV) differing in aphid transmissibility. Serological specificity of fourteen MAbs against the two strains was tested by indirect ELISA. Three MAbs were able to distinguish aphid transmissible TuMV strain 1 from non-aphid transmissible strain 31 while four MAbs reacted only with strain 31. No cross-reactivity between the two strains was found using these specific MAbs. Based upon the ability of Mab to inhibit the reaction of other MAbs, antibody competition test indicated that fourteen MAbs recognized six different epitopes on the virus particle; MAbs specific to strain 1 recognized two epitopes while MAbs specific to strain 31 also recognized two epitopes. The remaining two epitopes are common. Since the six amino acid differences between the coat proteins of the two strains were found at the N-terminal regions, MAbs specific to strain 1 or 31 bound to the different epitopes on the N-terminal regions in coat proteins of the two strains.

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Influence of the C terminus of the small protein subunit of bean pod mottle virus on the antigenicity of the virus determined using monoclonal antibodies and anti-peptide antiserum

Cited by 8 publications

References 27 publications

Antigenic analysis of bean pod mottle virus using linear and cyclized synthetic peptides

Antigenic analysis of bean pod mottle virus using linear and cyclized synthetic peptides

Immunological characterization of rice tungro spherical virus coat proteins and differentiation of isolates from the Philippines and India

Characterization of epitopes recognized by monoclonal antibodies to aphid transmissible and non-transmissible strains of turnip mosaic virus

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