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scmv hcpro  (HCPro Inc)

 
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    Structured Review

    HCPro Inc scmv hcpro
    HCPro site 247 in diverse potyviruses determines Ny tbr recognition. Representative images of callose deposition responses and callose counts/mm 2 following transient expression of the indicated proteins following water or flg22 treatment. Callose counts/mm 2 are shown <t>from</t> <t>PVY,</t> TuMV and <t>SCMV</t> HCPro expressions in (a) Premier Russet (PR) plants ( n ≥ 20); (b) PR plants with flg22 ( n ≥ 15). Callose counts/mm 2 are also shown for the mutant SCMV HCPro S247A in (c) PR plants ( n ≥ 45); (d) PR plants with flg22 ( n ≥ 50). Kruskal–Wallis test ( α < 0.05) was used to test for statistical significance. Means marked with the same letter are not statistically different according to Dunn's test ( p < 0.05).
    Scmv Hcpro, supplied by HCPro Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/scmv hcpro/product/HCPro Inc
    Average 90 stars, based on 1 article reviews
    scmv hcpro - by Bioz Stars, 2026-06
    90/100 stars

    Images

    1) Product Images from "A single phosphorylatable amino acid residue is essential for the recognition of multiple potyviral HCPro effectors by potato Ny tbr"

    Article Title: A single phosphorylatable amino acid residue is essential for the recognition of multiple potyviral HCPro effectors by potato Ny tbr

    Journal: Molecular Plant Pathology

    doi: 10.1111/mpp.70027

    HCPro site 247 in diverse potyviruses determines Ny tbr recognition. Representative images of callose deposition responses and callose counts/mm 2 following transient expression of the indicated proteins following water or flg22 treatment. Callose counts/mm 2 are shown from PVY, TuMV and SCMV HCPro expressions in (a) Premier Russet (PR) plants ( n ≥ 20); (b) PR plants with flg22 ( n ≥ 15). Callose counts/mm 2 are also shown for the mutant SCMV HCPro S247A in (c) PR plants ( n ≥ 45); (d) PR plants with flg22 ( n ≥ 50). Kruskal–Wallis test ( α < 0.05) was used to test for statistical significance. Means marked with the same letter are not statistically different according to Dunn's test ( p < 0.05).
    Figure Legend Snippet: HCPro site 247 in diverse potyviruses determines Ny tbr recognition. Representative images of callose deposition responses and callose counts/mm 2 following transient expression of the indicated proteins following water or flg22 treatment. Callose counts/mm 2 are shown from PVY, TuMV and SCMV HCPro expressions in (a) Premier Russet (PR) plants ( n ≥ 20); (b) PR plants with flg22 ( n ≥ 15). Callose counts/mm 2 are also shown for the mutant SCMV HCPro S247A in (c) PR plants ( n ≥ 45); (d) PR plants with flg22 ( n ≥ 50). Kruskal–Wallis test ( α < 0.05) was used to test for statistical significance. Means marked with the same letter are not statistically different according to Dunn's test ( p < 0.05).

    Techniques Used: Expressing, Mutagenesis

    Sequence identity of potyviral HCPro proteins compared to the PVY O HCPro and conservation among potyviruses at sites within the HCPro signature motif distinguishing the PVY O from PVY N strain groups.
    Figure Legend Snippet: Sequence identity of potyviral HCPro proteins compared to the PVY O HCPro and conservation among potyviruses at sites within the HCPro signature motif distinguishing the PVY O from PVY N strain groups.

    Techniques Used: Sequencing

    Structural conservation of HCPro proteins that induced Ny tbr + defence. (a) Structural alignment of the HCPro proteins from PVY O , BsMoV, SCMV, and SCMoV. Each model was given a unique colour, and the regions of the BsMoV, SCMV, and SCMoV HCPro models that match the reference structure (PVY O HCPro) are in full colour, while unaligned regions are lighter. The regions highlighted correspond to residues 236, 238, 247, 252, 262, 269, 270, and 301 that define the signature region distinguishing PVY O from PVY N and that are within the central domain of HCPro, which encompasses residue 100–311. (b) The structure of the region encompassing amino acids 227–327 that includes the PVY signature residues from each virus are depicted individually. In both (a) and (b), the serine from each potyviral HCPro protein that aligns with the PVY O HCPro S247 is highlighted and indicated with an arrow.
    Figure Legend Snippet: Structural conservation of HCPro proteins that induced Ny tbr + defence. (a) Structural alignment of the HCPro proteins from PVY O , BsMoV, SCMV, and SCMoV. Each model was given a unique colour, and the regions of the BsMoV, SCMV, and SCMoV HCPro models that match the reference structure (PVY O HCPro) are in full colour, while unaligned regions are lighter. The regions highlighted correspond to residues 236, 238, 247, 252, 262, 269, 270, and 301 that define the signature region distinguishing PVY O from PVY N and that are within the central domain of HCPro, which encompasses residue 100–311. (b) The structure of the region encompassing amino acids 227–327 that includes the PVY signature residues from each virus are depicted individually. In both (a) and (b), the serine from each potyviral HCPro protein that aligns with the PVY O HCPro S247 is highlighted and indicated with an arrow.

    Techniques Used: Residue, Virus



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    HCPro site 247 in diverse potyviruses determines Ny tbr recognition. Representative images of callose deposition responses and callose counts/mm 2 following transient expression of the indicated proteins following water or flg22 treatment. Callose counts/mm 2 are shown <t>from</t> <t>PVY,</t> TuMV and <t>SCMV</t> HCPro expressions in (a) Premier Russet (PR) plants ( n ≥ 20); (b) PR plants with flg22 ( n ≥ 15). Callose counts/mm 2 are also shown for the mutant SCMV HCPro S247A in (c) PR plants ( n ≥ 45); (d) PR plants with flg22 ( n ≥ 50). Kruskal–Wallis test ( α < 0.05) was used to test for statistical significance. Means marked with the same letter are not statistically different according to Dunn's test ( p < 0.05).
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    HCPro site 247 in diverse potyviruses determines Ny tbr recognition. Representative images of callose deposition responses and callose counts/mm 2 following transient expression of the indicated proteins following water or flg22 treatment. Callose counts/mm 2 are shown <t>from</t> <t>PVY,</t> TuMV and <t>SCMV</t> HCPro expressions in (a) Premier Russet (PR) plants ( n ≥ 20); (b) PR plants with flg22 ( n ≥ 15). Callose counts/mm 2 are also shown for the mutant SCMV HCPro S247A in (c) PR plants ( n ≥ 45); (d) PR plants with flg22 ( n ≥ 50). Kruskal–Wallis test ( α < 0.05) was used to test for statistical significance. Means marked with the same letter are not statistically different according to Dunn's test ( p < 0.05).
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    HCPro site 247 in diverse potyviruses determines Ny tbr recognition. Representative images of callose deposition responses and callose counts/mm 2 following transient expression of the indicated proteins following water or flg22 treatment. Callose counts/mm 2 are shown <t>from</t> <t>PVY,</t> TuMV and <t>SCMV</t> HCPro expressions in (a) Premier Russet (PR) plants ( n ≥ 20); (b) PR plants with flg22 ( n ≥ 15). Callose counts/mm 2 are also shown for the mutant SCMV HCPro S247A in (c) PR plants ( n ≥ 45); (d) PR plants with flg22 ( n ≥ 50). Kruskal–Wallis test ( α < 0.05) was used to test for statistical significance. Means marked with the same letter are not statistically different according to Dunn's test ( p < 0.05).
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    Image Search Results


    HCPro site 247 in diverse potyviruses determines Ny tbr recognition. Representative images of callose deposition responses and callose counts/mm 2 following transient expression of the indicated proteins following water or flg22 treatment. Callose counts/mm 2 are shown from PVY, TuMV and SCMV HCPro expressions in (a) Premier Russet (PR) plants ( n ≥ 20); (b) PR plants with flg22 ( n ≥ 15). Callose counts/mm 2 are also shown for the mutant SCMV HCPro S247A in (c) PR plants ( n ≥ 45); (d) PR plants with flg22 ( n ≥ 50). Kruskal–Wallis test ( α < 0.05) was used to test for statistical significance. Means marked with the same letter are not statistically different according to Dunn's test ( p < 0.05).

    Journal: Molecular Plant Pathology

    Article Title: A single phosphorylatable amino acid residue is essential for the recognition of multiple potyviral HCPro effectors by potato Ny tbr

    doi: 10.1111/mpp.70027

    Figure Lengend Snippet: HCPro site 247 in diverse potyviruses determines Ny tbr recognition. Representative images of callose deposition responses and callose counts/mm 2 following transient expression of the indicated proteins following water or flg22 treatment. Callose counts/mm 2 are shown from PVY, TuMV and SCMV HCPro expressions in (a) Premier Russet (PR) plants ( n ≥ 20); (b) PR plants with flg22 ( n ≥ 15). Callose counts/mm 2 are also shown for the mutant SCMV HCPro S247A in (c) PR plants ( n ≥ 45); (d) PR plants with flg22 ( n ≥ 50). Kruskal–Wallis test ( α < 0.05) was used to test for statistical significance. Means marked with the same letter are not statistically different according to Dunn's test ( p < 0.05).

    Article Snippet: Despite a generally low degree of amino acid sequence similarity to PVY O HCPro, a similar response was observed with the unrelated SCMV HCPro, which bears a phosphorylatable residue at position 247.

    Techniques: Expressing, Mutagenesis

    Sequence identity of potyviral HCPro proteins compared to the PVY O HCPro and conservation among potyviruses at sites within the HCPro signature motif distinguishing the PVY O from PVY N strain groups.

    Journal: Molecular Plant Pathology

    Article Title: A single phosphorylatable amino acid residue is essential for the recognition of multiple potyviral HCPro effectors by potato Ny tbr

    doi: 10.1111/mpp.70027

    Figure Lengend Snippet: Sequence identity of potyviral HCPro proteins compared to the PVY O HCPro and conservation among potyviruses at sites within the HCPro signature motif distinguishing the PVY O from PVY N strain groups.

    Article Snippet: Despite a generally low degree of amino acid sequence similarity to PVY O HCPro, a similar response was observed with the unrelated SCMV HCPro, which bears a phosphorylatable residue at position 247.

    Techniques: Sequencing

    Structural conservation of HCPro proteins that induced Ny tbr + defence. (a) Structural alignment of the HCPro proteins from PVY O , BsMoV, SCMV, and SCMoV. Each model was given a unique colour, and the regions of the BsMoV, SCMV, and SCMoV HCPro models that match the reference structure (PVY O HCPro) are in full colour, while unaligned regions are lighter. The regions highlighted correspond to residues 236, 238, 247, 252, 262, 269, 270, and 301 that define the signature region distinguishing PVY O from PVY N and that are within the central domain of HCPro, which encompasses residue 100–311. (b) The structure of the region encompassing amino acids 227–327 that includes the PVY signature residues from each virus are depicted individually. In both (a) and (b), the serine from each potyviral HCPro protein that aligns with the PVY O HCPro S247 is highlighted and indicated with an arrow.

    Journal: Molecular Plant Pathology

    Article Title: A single phosphorylatable amino acid residue is essential for the recognition of multiple potyviral HCPro effectors by potato Ny tbr

    doi: 10.1111/mpp.70027

    Figure Lengend Snippet: Structural conservation of HCPro proteins that induced Ny tbr + defence. (a) Structural alignment of the HCPro proteins from PVY O , BsMoV, SCMV, and SCMoV. Each model was given a unique colour, and the regions of the BsMoV, SCMV, and SCMoV HCPro models that match the reference structure (PVY O HCPro) are in full colour, while unaligned regions are lighter. The regions highlighted correspond to residues 236, 238, 247, 252, 262, 269, 270, and 301 that define the signature region distinguishing PVY O from PVY N and that are within the central domain of HCPro, which encompasses residue 100–311. (b) The structure of the region encompassing amino acids 227–327 that includes the PVY signature residues from each virus are depicted individually. In both (a) and (b), the serine from each potyviral HCPro protein that aligns with the PVY O HCPro S247 is highlighted and indicated with an arrow.

    Article Snippet: Despite a generally low degree of amino acid sequence similarity to PVY O HCPro, a similar response was observed with the unrelated SCMV HCPro, which bears a phosphorylatable residue at position 247.

    Techniques: Residue, Virus