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The role of plasmodesma-located proteins in tubule-guided virus transport is limited to the plasmodesmata.
den Hollander, P W; Kieper, S N; Borst, J W; van Lent, J W M.
Afiliación
  • den Hollander PW; Laboratory of Virology, Wageningen University, Droevendaalsesteeg 1, 6708 PB, Wageningen, The Netherlands.
  • Kieper SN; Laboratory of Virology, Wageningen University, Droevendaalsesteeg 1, 6708 PB, Wageningen, The Netherlands.
  • Borst JW; Laboratory of Biochemistry, Microspectroscopy Centre, Dreijenlaan 3, 6703 HA, Wageningen, The Netherlands.
  • van Lent JW; Laboratory of Virology, Wageningen University, Droevendaalsesteeg 1, 6708 PB, Wageningen, The Netherlands. jan.vanlent@wur.nl.
Arch Virol ; 161(9): 2431-40, 2016 Sep.
Article en En | MEDLINE | ID: mdl-27339685
Intercellular spread of plant viruses involves passage of the viral genome or virion through a plasmodesma (PD). Some viruses severely modify the PD structure, as they assemble a virion carrying tubule composed of the viral movement protein (MP) inside the PD channel. Successful modulation of the host plant to allow infection requires an intimate interaction between viral proteins and both structural and regulatory host proteins. To date, however, very few host proteins are known to promote virus spread. Plasmodesmata-located proteins (PDLPs) localised in the PD have been shown to contribute to tubule formation in cauliflower mosaic virus and grapevine fanleaf virus infections. In this study, we have investigated the role of PDLPs in intercellular transport of another tubule-forming virus, cowpea mosaic virus. The MP of this virus was found to interact with PDLPs in the PD, as was shown for other tubule-forming viruses. Expression of PDLPs and MPs in protoplasts in the absence of a PD revealed that these proteins do not co-localise at the site of tubule initiation. Furthermore, we show that tubule assembly in protoplasts does not require an interaction with PDLPs at the base of the tubule, as has been observed in planta. These results suggest that a physical interaction between MPs and PDLPs is not required for assembly of the movement tubule and that the beneficial role of PDLPs in virus movement is confined to the structural context of the PD.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas de Plantas / Nicotiana / Comovirus / Plasmodesmos / Proteínas de Movimiento Viral en Plantas Idioma: En Revista: Arch Virol Año: 2016 Tipo del documento: Article País de afiliación: Países Bajos Pais de publicación: Austria

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas de Plantas / Nicotiana / Comovirus / Plasmodesmos / Proteínas de Movimiento Viral en Plantas Idioma: En Revista: Arch Virol Año: 2016 Tipo del documento: Article País de afiliación: Países Bajos Pais de publicación: Austria