A PERK-Like receptor Kinase interacts with the geminivirus nuclear shuttle protein and potentiates viral infection

dc.creatorFlorentino, Lilian H.
dc.creatorSantos, Anésia A.
dc.creatorFontenelle, Mariana R.
dc.creatorPinheiro, Guilherme L.
dc.creatorZerbini, Francisco M.
dc.creatorBaracat-Pereira, Maria C.
dc.creatorFontes, Elizabeth P. B.
dc.date2018-04-24T14:14:27Z
dc.date2018-04-24T14:14:27Z
dc.date2006-04-09
dc.date.accessioned2023-09-27T21:27:28Z
dc.date.available2023-09-27T21:27:28Z
dc.identifier10985514
dc.identifierhttps://doi.org/10.1128/JVI.00173-06
dc.identifierhttp://www.locus.ufv.br/handle/123456789/19078
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8960938
dc.descriptionThe nuclear shuttle protein (NSP) from bipartite geminiviruses facilitates the intracellular transport of viral DNA from the nucleus to the cytoplasm and acts in concert with the movement protein (MP) to promote the cell-to-cell spread of the viral DNA. A proline-rich extensin-like receptor protein kinase (PERK) was found to interact specifically with NSP of Cabbage leaf curl virus (CaLCuV) and of tomato-infecting geminiviruses through a yeast two-hybrid screening. The PERK-like protein, which we designated NsAK (for NSP-associated kinase), is structurally organized into a proline-rich N-terminal domain, followed by a transmembrane segment and a C-terminal serine/threonine kinase domain. The viral protein interacted stably with defective versions of the NsAK kinase domain, but not with the potentially active enzyme, in an in vitro binding assay. In vitro-translated NsAK enhanced the phosphorylation level of NSP, indicating that NSP functions as a substrate for NsAK. These results demonstrate that NsAK is an authentic serine/threonine kinase and suggest a functional link for NSP-NsAK complex formation. This interpretation was corroborated by in vivo infectivity assays showing that loss of NsAK function reduces the efficiency of CaLCuV infection and attenuates symptom development. Our data implicate NsAK as a positive contributor to geminivirus infection and suggest it may regulate NSP function.
dc.formatpdf
dc.formatapplication/pdf
dc.languageeng
dc.publisherJournal of Virology
dc.relationv. 80, n. 13, p. 6648-6656, July 2006
dc.rightsAmerican Society for Microbiology
dc.subjectKinase interacts
dc.subjectViral infection
dc.titleA PERK-Like receptor Kinase interacts with the geminivirus nuclear shuttle protein and potentiates viral infection
dc.typeArtigo


Este ítem pertenece a la siguiente institución