Use este identificador para citar ou linkar para este item: http://www.alice.cnptia.embrapa.br/alice/handle/doc/899954
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dc.contributor.authorVASCONCELOS, E. A. R.
dc.contributor.authorSANTANA, C. G.
dc.contributor.authorGODOY, C. V.
dc.contributor.authorSEIXAS, C. D. S.
dc.contributor.authorSILVA, M. S.
dc.contributor.authorMOREIRA, L. R. S.
dc.contributor.authorOLIVEIRA-NETO, O. B.
dc.contributor.authorPRICE, D.
dc.contributor.authorFITCHES, E.
dc.contributor.authorFERREIRA FILHO, E. X.
dc.contributor.authorMEHTA, A.
dc.contributor.authorGATEHOUSE, J. A.
dc.contributor.authorGROSSI-DE-SA, M. F.
dc.date.accessioned2026-02-27T05:48:51Z-
dc.date.available2026-02-27T05:48:51Z-
dc.date.created2011-09-08
dc.date.issued2011
dc.identifier.citationBMC Biotechnology, v. 11, 2011.
dc.identifier.urihttp://www.alice.cnptia.embrapa.br/alice/handle/doc/899954-
dc.descriptionBackground: Asian rust (Phakopsora pachyrhizi) is a common disease in Brazilian soybean fields and it is difficult to control. To identify a biochemical candidate with potential to combat this disease, a new chitinase-like xylanase inhibitor protein (XIP) from coffee (Coffea arabica) (CaclXIP) leaves was cloned into the pGAPZa-B vector for expression in Pichia pastoris. Results: A cDNA encoding a chitinase-like xylanase inhibitor protein (XIP) from coffee (Coffea arabica) (CaclXIP), was isolated from leaves. The amino acid sequence predicts a (b/a)8 topology common to Class III Chitinases (glycoside hydrolase family 18 proteins; GH18), and shares similarity with other GH18 members, although it lacks the glutamic acid residue essential for catalysis, which is replaced by glutamine. CaclXIP was expressed as a recombinant protein in Pichia pastoris. Enzymatic assay showed that purified recombinant CaclXIP had only residual chitinolytic activity. However, it inhibited xylanases from Acrophialophora nainiana by approx. 60% when present at 12:1 (w/w) enzyme:inhibitor ratio. Additionally, CaclXIP at 1.5 ?g/?L inhibited the germination of spores of Phakopsora pachyrhizi by 45%. Conclusions: Our data suggests that CaclXIP belongs to a class of naturally inactive chitinases that have evolved to act in plant cell defence as xylanase inhibitors. Its role on inhibiting germination of fungal spores makes it an eligible candidate gene for the control of Asian rust.
dc.language.isoeng
dc.rightsopenAccess
dc.subjectControle de praga
dc.titleA new chitinase-like xylanase inhibitor protein (XIP) from coffee (Coffea arabica) affects Soybean Asian rust (Phakopsora pachyrhizi) spore germination.
dc.typeArtigo de periódico
dc.subject.thesagroPraga de Planta
dc.subject.thesagroSoja
riaa.ainfo.id899954
riaa.ainfo.lastupdate2026-02-26
dc.identifier.doihttps://www.doi.org/10.1186/1472-6750-11-14
dc.contributor.institutionERICO A. R. VASCONCELOS
dc.contributor.institutionCELSO G. SANTANAeng
dc.contributor.institutionCLAUDIA VIEIRA GODOY, CNPSOeng
dc.contributor.institutionCLAUDINE DINALI SANTOS SEIXAS, CNPSOeng
dc.contributor.institutionMARILIA SANTOS SILVA, CPACeng
dc.contributor.institutionLEONORA R. S. MOREIRA, UNIVERSIDADE DE BRASÍLIAeng
dc.contributor.institutionOSMUNDO B. OLIVEIRA-NETOeng
dc.contributor.institutionDANIEL PRICE, DURHAM UNIVERSITYeng
dc.contributor.institutionELAINE FITCHES, DURHAM UNIVERSITYeng
dc.contributor.institutionEDIVALDO X. FERREIRA FILHO, UNIVERSIDADE DE BRASÍLIAeng
dc.contributor.institutionANGELA MEHTA DOS REIS, CENARGENeng
dc.contributor.institutionJOHN A. GATEHOUSE, UNIVERSITY DURHAMeng
dc.contributor.institutionMARIA FATIMA GROSSI DE SA, CENARGEN.eng
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