Structural Analysis of Cassiicolin, a Host-selective Protein Toxin from Corynespora cassiicola

Barthe, Philippe; Pujade-Renaud, Valérie; Breton, Frédéric; Gargani, Daniel; Thaï, Robert; Roumestand, Christian; Lamotte, Frédéric de

doi:10.1016/j.jmb.2006.11.086

Cited by 55 publications

(64 citation statements)

References 54 publications

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“…The effector is able to cause necrosis on detached rubber tree leaves and on other host plants such as tobacco (Nicotiana tabacum L.) and soy (Glycine max (L.) Merr. (Barthe et al 2007;de Lamotte et al 2007). Although the deduced effector amino acid sequence did not show significant homology with other proteins, structural analysis indicates that the protein structure resembles trypsin-like inhibitors (Barthe et al 2007).…”

Section: Effectors Of Other Necrotrophic Fungimentioning

confidence: 91%

Proteinaceous necrotrophic effectors in fungal virulence

Tan

Oliver

Solomon

et al. 2010

Functional Plant Biol.

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Abstract. The host-pathogen interface can be considered as a biological battlefront. Molecules produced by both the pathogen and the host are critical factors determining the outcome of the interaction. Recent studies have revealed that an increasing number of necrotrophic fungal pathogens produce small proteinaceous effectors that are able to function as virulence factors. These molecules can cause tissue death in host plants that possess dominant sensitivity genes, leading to subsequent pathogen colonisation. Such effectors are only found in necrotrophic fungi, yet their roles in virulence are poorly understood. However, several recent key studies of necrotrophic effectors from two wheat (Triticum aestivum L.) pathogens, Pyrenophora tritici-repentis (Died.) Drechs. and Stagonospora nodorum (Berk.) Castell. & Germano, have shed light upon how these effector proteins serve to disable the host from the inside out.

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Section: Effectors Of Other Necrotrophic Fungimentioning

confidence: 91%

Proteinaceous necrotrophic effectors in fungal virulence

Tan

Oliver

Solomon

et al. 2010

Functional Plant Biol.

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“…In particular, the mature cassiicolin domain is highly conserved, with only one amino acid substitution (S instead of T) at position 2. This amino acid is especially important because it carries the sugar moiety (0-methyl-mannose) of the active cassiicolin (Barthe et al 2007;de Lamotte et al 2007). Although the role played by this sugar in toxicity is still unknown, it should be noted that Serine (S), like Threonine (T), can be 0-glycosylated.…”

Section: Discovery Of New Cassiicolin Gene Homologuesmentioning

confidence: 99%

“…A toxin called cassiicolin was purified and characterized from the culture filtrate of a rubber tree isolate (CCP) from the Philippines (Breton et al 2000;Barthe et al 2007;de Lamotte et al 2007). The toxin is a small, secreted glycosylated protein that plays an important role in C. cassiicola pathogenicity.…”

Section: Introductionmentioning

confidence: 99%

First characterization of endophytic Corynespora cassiicola isolates with variant cassiicolin genes recovered from rubber trees in Brazil

et al. 2012

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Fungal Divers. ISI Document Delivery No.: 940HT Times Cited: 0 Cited Reference Count: 69 Cited References: Atan S, 2003, J RUBBER RES, V6, P58 Barthe P, 2007, J MOL BIOL, V367, P89, DOI 10.1016/j.jmb.2006.11.086 Bendtsen JD, 2004, J MOL BIOL, V340, P783, DOI 10.1016/j.jmb.2004.05.028 Breton F., 2000, Journal of Rubber Research, V3, P115 Cai L, 2006, ANTON LEEUW INT J G, V89, P293, DOI 10.1007/s10482-005-9030-1 Chang S. J., 1993, Plant Molecular Biology Reporter, V11, P113, DOI 10.1007/BF02670468 Chaparro DF, 2009, REV IBEROAM MICOL, V26, P238, DOI 10.1016/j.riam.2009.03.005 Chee K. H., 1990, Review of Plant Pathology, V69, P423 CHEE K H, 1988, Journal of Natural Rubber Research, V3, P21 Collado J, 1999, NEW PHYTOL, V144, P525, DOI 10.1046/j.1469-8137.1999.00533.x de Lamotte F, 2007, J CHROMATOGR B, V849, P357, DOI 10.1016/j.jchromb.2006.10.051 Deon M, 2012, PLANT SCI, V185, P227, DOI 10.1016/j.plantsci.2011.10.017 Dixon LJ, 2009, PHYTOPATHOLOGY, V99, P1015, DOI 10.1094/PHYTO-99-9-1015 Drummond A., 2011, GENEIOUS V5 4 Farr D. F., 2011, FUNGAL DATABASES SYS FELSENSTEIN J, 1985, EVOLUTION, V39, P783, DOI 10.2307/2408678 FISHER PJ, 1992, NEW PHYTOL, V120, P137, DOI 10.1111/j.1469-8137.1992.tb01066.x Gazis R, 2010, FUNGAL ECOL, V3, P240, DOI 10.1016/j.funeco.2009.12.001 GOLDMAN N, 1994, MOL BIOL EVOL, V11, P725 Gond SK, 2007, WORLD J MICROB BIOT, V23, P1371, DOI 10.1007/s11274-007-9375-x Hyde KD, 2001, FUNGAL DIVERS, V7, P35 Jayasinghe CK, 1998, B RUBBER RES I SRI L, V39, P1 Jayasinghe CK, 1996, P WORKSH COR LEAF FU, P3 Jayasinghe C.K., 1986, J RUBBER RES I SRI L, V65, P47 Junqueira N. T. V., 1985, Proceedings of the regional conference on plant quarantine support for agricultural development. Kuala Lumpur, Malaysia, 10-12 December 1985., P253 Kingsland GC, 1985, ACTA HORTIC ISHS, V153, P229 Kodsueb R, 2008, FUNGAL DIVERS, V30, P37 Koenning SR, 2006, PLANT DIS, V90, P974, DOI 10.1094/PD-90-0974C Krogh A, 2001, J MOL BIOL, V305, P567, DOI 10.1006/jmbi.2000.4315 Kumar DSS, 2004, FUNGAL DIVERS, V17, P69 Lana TG, 2011, GENET MOL RES, V10, P326, DOI 10.4238/vol10-1gmr895 Lee S, 2004, FUNGAL DIVERS, V17, P91 Liyanage NIS, 1986, J RUBBER RES I SRI L, V65, P51 Martin R, 1968, ADANSONIA, V8, P475 Mostert L, 2000, SYDOWIA, V52, P46 Nei M., 2000, MOL EVOLUTION PHYLOG Newsam A, 1960, PLANT PATHOLOGY DIVI NUGAWELA A, 1989, Journal of Natural Rubber Research, V4, P233 Okane I, 2008, MYCOSCIENCE, V49, P359, DOI 10.1007/s10267-008-0440-6 Oliveira R. R., 2007, Summa Phytopathologica, V33, P297, DOI 10.1590/S0100-54052007000300016 Oliveira R. R., 2006, Fitopatologia Brasileira, V31, P509, DOI 10.1590/S0100-41582006000500012 ONESIROSAN P, 1975, PHYSIOL PLANT PATHOL, V5, P289, DOI 10.1016/0048-4059(75)90095-8 Pawirosoemardjo S., 1996, P WORKSH COR LEAF FA, P79 Pfaffl MW, 2001, NUCLEIC ACIDS RES, V29, DOI 10.1093/nar/29.9.e45 Photita W, 2004, FUNGAL DIVERS, V16, P131 Photita W, 2005, FUNGAL DIVERS, V18, P117 Pongthep K, 1987, P IRRDB S CHIANG MAI, P1 Porras-Alfaro A, 2011, ANNU REV PHYTOPATHOL, V49, P291, DOI 10.1146/annurev-phyto-080508-...

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“…In regards to the peptide activity, Barthe et al (2007) demonstrated that cassiicolin, a 27-residue peptide from Corynespora cassiicola, was able to induce cellular damage on a Hevea brasiliensis clone (PB260). Some peptides produced by different fungi may thus act as virulence factors and could participate in host invasion by the fungus in various plant organs.…”

Section: Introductionmentioning

confidence: 99%

Toxicity of extracellular proteins from Diplodia seriata and Neofusicoccum parvum involved in grapevine Botryosphaeria dieback

Bénard-Gellon¹,

Farine²,

Goddard³

et al. 2014

Protoplasma

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Botryosphaeria dieback, esca and Eutypa dieback are three economic major grapevine trunk diseases that cause severe yield reduction in vineyards worldwide. The frequency of disease symptoms has increased considerably over the past decade, and no efficient treatment is currently available to control these diseases. The different fungi associated with grapevine trunk diseases mainly induce necrotic wood and characteristic foliar symptoms. In this context, fungi virulence factors and host invasion are not well understood. We hypothesise that extracellular proteins produced by Diplodia seriata and Neofusicoccum parvum, two causal agents associated with Botryosphaeria dieback, are virulence factors responsible for the pathogenicity. In our previous work, we demonstrated that the total extracellular compounds produced by N. parvum induced more necrosis on Chardonnay calli and triggered a different defence gene expression pattern than those produced by D. seriata. Furthermore, this aggressiveness was not clearly correlated with the production of mellein, a characteristic phytotoxin of Botryosphaeriaceae, in our in vitro calli model. To characterise other potential virulence factors and to understand the mechanisms of host invasion by the fungus, we evaluated the profile, quantity and the impact of extracellular proteins produced by these fungi on Vitis vinifera calli necrosis and defence gene expression. Our results reveal that, under the same conditions, N. parvum produces more extracellular proteins and in higher concentrations than D. seriata. With Vitis vinifera cv. Chardonnay cells, we showed that equivalent concentrations of proteins secreted by N. parvum were more aggressive than those of D. seriata in producing necrosis and that they clearly induced more grapevine defence genes.

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Structural Analysis of Cassiicolin, a Host-selective Protein Toxin from Corynespora cassiicola

Cited by 55 publications

References 54 publications

Proteinaceous necrotrophic effectors in fungal virulence

Proteinaceous necrotrophic effectors in fungal virulence

First characterization of endophytic Corynespora cassiicola isolates with variant cassiicolin genes recovered from rubber trees in Brazil

Toxicity of extracellular proteins from Diplodia seriata and Neofusicoccum parvum involved in grapevine Botryosphaeria dieback

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