http://www.cnr.it/ontology/cnr/individuo/prodotto/ID198517

Lolium latent virus (Alphaflexiviridae) coat proteins: expression and functions in infected plant tissue (Articolo in rivista)

Type

Label

Lolium latent virus (Alphaflexiviridae) coat proteins: expression and functions in infected plant tissue (Articolo in rivista) (literal)

Anno

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Alternative label

Vaira A.M., Lim H.-S., Bauchan G.R., Owens R.A., Natilla A., Dienelt M.M., Reinsel M.D., Hammond J. (2012)
Lolium latent virus (Alphaflexiviridae) coat proteins: expression and functions in infected plant tissue
in Journal of general virology (Print); Society for general microbiology, Reading (Regno Unito)
(literal)

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Vaira A.M., Lim H.-S., Bauchan G.R., Owens R.A., Natilla A., Dienelt M.M., Reinsel M.D., Hammond J. (literal)

Pagina inizio

Pagina fine

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Studio sulle funzioni del N terminale della proteina del capside di lolium latent virus, genere Lolavirus, famiglia Alphaflexiviridae (literal)

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Rivista

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V.A.M.: Istituto di Virologia Vegetal, CNR, Torino, Italy D.M.M., R.M.D. & H.J.:USDA-ARS, USNA, Floral and Nursery Plants Research Unit, Beltsville, MD, USA L.H.S.: Department of Applied Biology, Chungnam National University, Daejeon, 305-764, South Korea B.G.: USDA-ARS, PSI, Electron and Confocal Microscopy Unit, 10300 Baltimore Ave. Beltsville, MD, USA O.R.A. & N.A.: USDA-ARS, PSI, Molecular Plant Pathology Laboratory, 10300 Baltimore Ave. Beltsville, MD, USA (literal)

Titolo

Lolium latent virus (Alphaflexiviridae) coat proteins: expression and functions in infected plant tissue (literal)

Abstract

The genome of Lolium latent virus (LoLV; genus Lolavirus, family Alphaflexiviridae) is encapsidated by two carboxy-coterminal coat protein (CP) variants (about 28 and 33 kDa), in equimolar proportions. The CP ORF contains two 5?-proximal AUGs encoding Met 1 and Met 49, respectively promoting translation of the 33 and 28 kDa CP variants. The 33 kDa CP N-terminal domain includes a 42 aa sequence encoding a putative chloroplast transit peptide, leading to protein cleavage and alternative derivation of the approximately 28 kDa CP. Mutational analysis of the two in-frame start codons and of the putative proteolytic-cleavage site showed that the N-terminal sequence is crucial for efficient cell-to-cell movement, functional systemic movement, homologous CP interactions and particle formation, but is not required for virus replication. Blocking production of the 28 kDa CP by internal initiation shows no major outcome, whereas additional mutation to prevent proteolytic cleavage at the chloroplast membrane has a dramatic effect on virus infection. (literal)

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