TIP, A Novel Host Factor Linking Callose Degradation with the Cell-to-Cell Movement of Potato virus X
The cell-to-cell movement of Potato virus X (PVX) requires four virus-encoded proteins, the triple gene block (TGB) proteins (TGB25K, TGB12K, and TGB8K) and the coat protein. TGB12K increases the plasmodesmal size exclusion limit (SEL) and may, therefore, interact directly with components of the cel...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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The American Phytopathological Society
2003-02-01
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| Series: | Molecular Plant-Microbe Interactions |
| Subjects: | |
| Online Access: | https://apsjournals.apsnet.org/doi/10.1094/MPMI.2003.16.2.132 |
| _version_ | 1811275693339705344 |
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| author | Ingela Fridborg Jef Grainger Anthony Page Mark Coleman Kim Findlay Susan Angell |
| author_facet | Ingela Fridborg Jef Grainger Anthony Page Mark Coleman Kim Findlay Susan Angell |
| author_sort | Ingela Fridborg |
| collection | DOAJ |
| description | The cell-to-cell movement of Potato virus X (PVX) requires four virus-encoded proteins, the triple gene block (TGB) proteins (TGB25K, TGB12K, and TGB8K) and the coat protein. TGB12K increases the plasmodesmal size exclusion limit (SEL) and may, therefore, interact directly with components of the cell wall or with plant proteins associated with bringing about this change. A yeast two-hybrid screen using TGB12K as bait identified three TGB12K-interacting proteins (TIP1, TIP2, and TIP3). All three TIPs interacted specifically with TGB12K but not with TGB25K or TGB8K. Similarly, all three TIPs interacted with β-1,3-glucanase, the enzyme that may regulate plasmodesmal SEL through callose degradation. Sequence analyses revealed that the TIPs encode very similar proteins and that TIP1 corresponds to the tobacco ankyrin repeat-containing protein HBP1. A TIP1::GFP fusion protein localized to the cytoplasm. Coexpression of this fusion protein with TGB12K induced cellular changes manifested as deposits of additional cytoplasm at the cell periphery. This work reports a direct link between a viral movement protein required to increase plasmodesmal SEL and a host factor that has been implicated as a key regulator of plasmodesmal SEL. We propose that the TIPs are susceptibility factors that modulate the plasmodesmal SEL. |
| first_indexed | 2024-04-12T23:42:21Z |
| format | Article |
| id | doaj.art-48d9e821e5824679afda1ab706244691 |
| institution | Directory Open Access Journal |
| issn | 0894-0282 1943-7706 |
| language | English |
| last_indexed | 2024-04-12T23:42:21Z |
| publishDate | 2003-02-01 |
| publisher | The American Phytopathological Society |
| record_format | Article |
| series | Molecular Plant-Microbe Interactions |
| spelling | doaj.art-48d9e821e5824679afda1ab7062446912022-12-22T03:11:56ZengThe American Phytopathological SocietyMolecular Plant-Microbe Interactions0894-02821943-77062003-02-0116213214010.1094/MPMI.2003.16.2.132TIP, A Novel Host Factor Linking Callose Degradation with the Cell-to-Cell Movement of Potato virus XIngela FridborgJef GraingerAnthony PageMark ColemanKim FindlaySusan AngellThe cell-to-cell movement of Potato virus X (PVX) requires four virus-encoded proteins, the triple gene block (TGB) proteins (TGB25K, TGB12K, and TGB8K) and the coat protein. TGB12K increases the plasmodesmal size exclusion limit (SEL) and may, therefore, interact directly with components of the cell wall or with plant proteins associated with bringing about this change. A yeast two-hybrid screen using TGB12K as bait identified three TGB12K-interacting proteins (TIP1, TIP2, and TIP3). All three TIPs interacted specifically with TGB12K but not with TGB25K or TGB8K. Similarly, all three TIPs interacted with β-1,3-glucanase, the enzyme that may regulate plasmodesmal SEL through callose degradation. Sequence analyses revealed that the TIPs encode very similar proteins and that TIP1 corresponds to the tobacco ankyrin repeat-containing protein HBP1. A TIP1::GFP fusion protein localized to the cytoplasm. Coexpression of this fusion protein with TGB12K induced cellular changes manifested as deposits of additional cytoplasm at the cell periphery. This work reports a direct link between a viral movement protein required to increase plasmodesmal SEL and a host factor that has been implicated as a key regulator of plasmodesmal SEL. We propose that the TIPs are susceptibility factors that modulate the plasmodesmal SEL.https://apsjournals.apsnet.org/doi/10.1094/MPMI.2003.16.2.132plasmodesmatavirus movement |
| spellingShingle | Ingela Fridborg Jef Grainger Anthony Page Mark Coleman Kim Findlay Susan Angell TIP, A Novel Host Factor Linking Callose Degradation with the Cell-to-Cell Movement of Potato virus X Molecular Plant-Microbe Interactions plasmodesmata virus movement |
| title | TIP, A Novel Host Factor Linking Callose Degradation with the Cell-to-Cell Movement of Potato virus X |
| title_full | TIP, A Novel Host Factor Linking Callose Degradation with the Cell-to-Cell Movement of Potato virus X |
| title_fullStr | TIP, A Novel Host Factor Linking Callose Degradation with the Cell-to-Cell Movement of Potato virus X |
| title_full_unstemmed | TIP, A Novel Host Factor Linking Callose Degradation with the Cell-to-Cell Movement of Potato virus X |
| title_short | TIP, A Novel Host Factor Linking Callose Degradation with the Cell-to-Cell Movement of Potato virus X |
| title_sort | tip a novel host factor linking callose degradation with the cell to cell movement of potato virus x |
| topic | plasmodesmata virus movement |
| url | https://apsjournals.apsnet.org/doi/10.1094/MPMI.2003.16.2.132 |
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