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dc.contributor.authorElvira, Maribel-
dc.contributor.authorMolina Galdeano, Myriam-
dc.contributor.authorGilardi, Patricia-
dc.contributor.authorGarcía-Luque, Isabel-
dc.date.accessioned2012-10-10T09:54:16Z-
dc.date.available2012-10-10T09:54:16Z-
dc.date.issued2008-04-
dc.identifier.citationJournal of Experimental Botany 59(6):1253-1265(2008)es_ES
dc.identifier.issn0022-0957-
dc.identifier.urihttp://hdl.handle.net/10261/57734-
dc.description13 páginas, 6 figuras, 1 tabla -- PAGS nros. 1253-1265es_ES
dc.description.abstractResistance conferred by the L3 gene is active against most of the tobamoviruses, including the Spanish strain (PMMoV-S), a P1,2 pathotype, but not against certain strains of pepper mild mottle virus (PMMoV), termed P1,2,3 pathotype, such as the Italian strain (PMMoV-I). Both viruses are nearly identical at their nucleotide sequence level (98%) and were used to challenge Capsicum chinense PI159236 plants harbouring the L3 gene in order to carry out a comparative proteomic analysis of PR proteins induced in this host in response to infection by either PMMoV-S or PMMoV-I. PMMoV-S induces a hypersensitive reaction (HR) in C. chinense PI159236 plant leaves with the formation of necrotic local lesions and restriction of the virus at the primary infection sites. In this paper, C. chinense PR protein isoforms belonging to the PR-1, β-1,3-glucanases (PR-2), chitinases (PR-3), osmotin-like protein (PR-5), peroxidases (PR-9), germin-like protein (PR-16), and PRp27 (PR-17) have been identified. Three of these PR protein isoforms were specifically induced during PMMoV-S-activation of C. chinense L3 gene-mediated resistance: an acidic β-1,3-glucanase isoform (PR-2) (Mr 44.6; pI 5.1), an osmotin-like protein (PR-5) (Mr 26.8; pI 7.5), and a basic PR-1 protein isoform (Mr 18; pI 9.4–10.0). In addition, evidence is presented for a differential accumulation of C. chinense PR proteins and mRNAs in the compatible (PMMoV-I)–C. chinense and incompatible (PMMoV-S)–C. chinense interactions for proteins belonging to all PR proteins detected. Except for an acidic chitinase (PR-3) (Mr 30.2; pI 5.0), an earlier and higher accumulation of PR proteins and mRNAs was detected in plants associated with HR induction. Furthermore, the accumulation rates of PR proteins and mRNA did not correlate with maximal accumulation levels of viral RNA, thus indicating that PR protein expression may reflect the physiological status of the plantes_ES
dc.description.sponsorshipThe work was supported by grants from CICYT (AGF95-0696, BIO1998-0860-C01, BIO2001-1937-C01, BIO2004-04968-C01, and BIO2007-67874-C02-01) and CAM (07B/0034/97, 07B/0030/2002). MIE was recipient of a post-doctoral fellowship from CajaMadrid; PG was supported by a CAM predoctoral fellowship, and MMG was supported by MECes_ES
dc.language.isoenges_ES
dc.publisherOxford University Presses_ES
dc.rightsclosedAccesses_ES
dc.subjectCapsicum chinensees_ES
dc.subjectcompatible interactiones_ES
dc.subjectincompatible interactiones_ES
dc.subjectHR-inductiones_ES
dc.subjectPMMoVes_ES
dc.subjectPR proteinses_ES
dc.titleProteomic analysis of pathogenesis-related proteins (PRs) induced by pepper mild mottle virus (PMMoV) in Capsicum chinense L3es_ES
dc.typeartículoes_ES
dc.identifier.doi10.1093/jxb/ern032-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttp://dx.doi.org/10.1093/jxb/ern032es_ES
dc.identifier.e-issn1460-2431-
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