In situ Degradation of the Protein Chain of Potato Virus X at the N- and C-termini

Koenig, R.; Tremaine, J. H.; Shepard, James F.

doi:10.1099/0022-1317-38-2-329

Cited by 61 publications

(27 citation statements)

References 17 publications

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“…The C terminus of the PVX capsid protein also seems to be located on the virus surface, since PAbs react with the 48 amino acid C-terminal CNBr fragment (Radavsky et al, 1988). Our results are in accord with those of Koenig et al (1978), which showed that N-and C-terminal portions of the capsid protein can be split off with proteases and that the resulting PVX particles can be distinguished by their reactions with PAbs (Koenig, 1972(Koenig, , 1978. Using rat MAbs to PVX, Koenig & Torrance (1986) clearly distinguished PVX particles with capsid proteins lacking N or C termini and found three antigenic determinants on the protein subunits of the B strain of PVX.…”

Section: Discussionsupporting

confidence: 80%

Antigenic Characterization of Potato Virus X with Monoclonal Antibodies

Söber¹,

Järvekülg

Toots

et al. 1988

Journal of General Virology

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SUMMARYA panel of mouse monoclonal antibodies (MAbs) against potato virus X (PVX) was obtained and three of these which had high affinity to the antigen were characterized in detail. These three antibodies defined two epitopes on PVX and recognized native virus, viral coat protein and denatured viral coat protein in various immunological assays. Two of the MAbs and rabbit anti-PVX polyclonal antibodies bound to the 68 amino acid N-terminal peptide of the PVX coat protein. This implies that the N terminus of the PVX coat protein is exposed at the virus surface and forms a highly immunogenic antigenic determinant. In double antibody sandwich (DAS) ELISA, MAbs and their horseradish peroxidase conjugates reacted with PVX at 10 to 20 ng/ml. Monoclonal antibodies to PVX reacted with virus in potato leaves and tubers and detected the virus in DAS ELISA in various combinations, including in combination with polyclonal antibodies.

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Section: Discussionsupporting

confidence: 80%

Antigenic Characterization of Potato Virus X with Monoclonal Antibodies

Söber¹,

Järvekülg

Toots

et al. 1988

Journal of General Virology

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“…Our results suggest that the quaternary structure of BNYVV may resemble that of other elongated plant viruses, such as tobacco mosaic virus (TMV) (Bloomer et al, 1978), potato virus X (PVX) (Koenig et al, 1978;Sawyer et al, 1987) and potyviruses (Allison et al, t985;Shukla et al, 1988), in that the C terminus of the coat protein is exposed. The C terminus of the BNYVV coat protein apparently carries the continuous epitope 4 which seems to be strongly immunogenic.…”

Section: Resultsmentioning

confidence: 91%

Antigenic analysis of the coat protein of beet necrotic yellow vein virus by means of monoclonal antibodies

Koenig

Commandeur

Lesemann

et al. 1990

Journal of General Virology

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“…Thus the 59K protein may contain the sequence between amino acid 838 and the end of the 150K polyprotein, and the 57K protein may arise from it by the loss of the C-terminal amino acids. It is known that proteases can remove amino acids from the C termini of the coat proteins of tobacco mosaic virus (Harris & Knight, 1952), potato virus X (Koenig et al, 1978) and potyviruses (Shukla et al, 1988). Presumably, as with these viruses, the C-terminal amino acids of TBRV coat protein protrude from the virus particle surface and can be removed without disrupting the virion.…”

Section: Discussionmentioning

confidence: 99%

Virus-specific proteins in cells infected with tomato black ring nepovirus: evidence for proteolytic processing in vivo

Demangeat

Hemmer²,

Reinbolt³

et al. 1992

Journal of General Virology

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The synthesis of proteins encoded by the RNA of tomato black ring virus (TBRV) in vivo was studied in protoplasts by direct labelling with [35S]methionine, and in protoplasts and plants by immunoblotting experiments with specific antisera. Comparison of the proteins synthesized in infected and mock-inoculated protoplasts suggested that proteins of Mr 120K, 90K, 80K, 57K and 46K were virus-specific. The proteins derived from the RNA-l-encoded polyprotein detected by immunoblotting were a stable 120K protein and, only in protoplasts, small amounts of a 90K protein which contains the C-terminal part of the 120K protein and the polymerase domain. The results suggest that the polymerase and the adjacent protease function in vivo largely or solely when combined in a 120K protein.The proteins derived from the RNA-2-encoded polyprotein detected by immunoblotting were 59K and 57K proteins, which reacted with antiserum to TBRV particles, and a 46K protein. In extracts of infected Nicotiana clevelandii and Chenopodium quinoa made soon after inoculation, the 59K protein was more abundant than the 57K protein; later samples contained similar quantities of each protein. The 57K protein comigrated with protein extracted from virus particles. The results of amino acid sequencing suggested that the 57K protein is derived from the 59K protein by the loss of nine C-terminal amino acids. Antiserum to a peptide adjacent to the 57K protein in the 150K polyprotein detected a 46K protein in protoplasts and plant tissue. The results support the processing scheme for TBRV polyproteins proposed after analysis of the products of in vitro translation.

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In situ Degradation of the Protein Chain of Potato Virus X at the N- and C-termini

Cited by 61 publications

References 17 publications

Antigenic Characterization of Potato Virus X with Monoclonal Antibodies

Antigenic Characterization of Potato Virus X with Monoclonal Antibodies

Antigenic analysis of the coat protein of beet necrotic yellow vein virus by means of monoclonal antibodies

Virus-specific proteins in cells infected with tomato black ring nepovirus: evidence for proteolytic processing in vivo

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