Monoclonal antibodies which show restricted binding to four Colletotrichum species: C. lindemuthianum, C. malvarum, C. orbiculare and C. trifolii

Pain, Naomi A.; O’Connell, Richard J.; Bailey, J. A.; Green, J.R.

doi:10.1016/0885-5765(92)90004-f

Cited by 46 publications

(69 citation statements)

References 27 publications

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“…The carbohydrate epitopes recognised by MAbs UB20 and UB22 (see below) were well preserved by aldehyde fixation, dehydration by the Progressive Lowering of Temperature method [11] and low temperature embedding in LR White resin [52]. However, the protein epitopes recognised by MAbs UB25, UB26 and UB27 (see below) were poorly preserved by this method.…”

Section: Localisation Of Antigensmentioning

confidence: 94%

“…MAbs were prepared using mice inoculated with two types of immunogen; homogenates of conidia with short germ-tubes grown in liquid culture [52], or homogenates of infection structures isolated from bean leaves [SO]. The latter were obtained by homogenizing infected bean leaves, removing plant debris by filtration through a 45 /lm nylon mesh and collecting the fungal structures by isopycnic centrifugation (IPC) on Percoll, an inert suspension of colloidal silica [62].…”

Section: Production Of Mabsmentioning

confidence: 99%

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Use of Monoclonal Antibodies to Study Differentiation of Colletotrichum Infection Structures

O’Connell

Pain

Bailey

et al. 1996

Developments in Plant Pathology

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Section: Localisation Of Antigensmentioning

confidence: 94%

Section: Production Of Mabsmentioning

confidence: 99%

Use of Monoclonal Antibodies to Study Differentiation of Colletotrichum Infection Structures

O’Connell

Pain

Bailey

et al. 1996

Developments in Plant Pathology

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“…Br. & Cav., race k (LARS 137) was cultured as described by Pain et al (1992). Excised primary leaves of P. vulgaris L. cv.…”

Section: Methodsmentioning

confidence: 99%

Expression cloning of a fungal proline‐rich glycoprotein specific to the biotrophic interface formed in the Colletotrichum–bean interaction

et al. 1998

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SummaryThe monoclonal antibody, UB25, recognises a glycoprotein specifically located at the biotrophic interface formed in the Colletotrichum lindemuthianum-bean interaction. The antibody labels the walls of intracellular hyphae and the interfacial matrix which separates them from the invaginated host plasma membrane. In Western blots, UB25 recognises a ladder of bands which are multiples of M r 40.5 kDa. A full length cDNA encoding the glycoprotein recognised by UB25 has been isolated by expression cloning and designated CIH1 (Colletotrichum Intracellular Hypha 1). In vitro transcription/translation of CIH1, and transfection of mammalian COS cells, showed that UB25 recognised the expressed product in both procedures confirming that the clones isolated were true positives. Southern analysis of bean and C. lindemuthianum genomic DNA indicated that the CIH1 glycoprotein is fungally encoded and Northern analysis showed that it is only expressed in planta. Analysis of the deduced amino acid sequence of CIH1 indicates the presence of an N-terminal signal sequence and two possible sites for N-glycosylation. The N-terminal domain of the mature protein is rich in proline and contains several short repetitive motifs. CIH1 is thus a fungal proline-rich glycoprotein which appears to form a cross-linked structure in planta and, as such, resembles plant cell wall proline-and hydroxyproline-rich proteins. Possible functions for the CIH1 protein in the establishment and maintenance of biotrophy are discussed.

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“…The graph to the right of each panel indicates the relative kinase activity calculated by comparison with activity at 0 h. Kinase activity was determined in silenced plants in two biological replicates. One set of representative data is shown in this figure. extracellular matrix glycoproteins recognized by monoclonal antibody UB20 (Pain et al, 1992;Hughes et al, 1999) were significantly more abundant on the surface of conidia of ssd1 mutants RCD1 and RCD2 than on that of the wild type (Figure 8). To test the hypothesis that fungal cell surface components induce SIPK and WIPK, we examined kinase activity in leaves infiltrated with conidia of the wild type and ssd1 mutant.…”

Section: Cell Surface Components Of the Ssd1 Mutant Induce Sipk And Wmentioning

confidence: 99%

“…ROS accumulation was detected by staining with DAB . Extracellular matrix glycoproteins were labeled on conidia germinating on glass microscope slides using monoclonal antibody UB20 for immunofluorescence microscopy (Pain et al, 1992;Hughes et al, 1999). Fluorescence was imaged with a Leica TCS SP2 confocal microscope and the 488-nm line of an argon laser.…”

Section: Pathogen Inoculation and Cytological Assaysmentioning

confidence: 99%

TheColletotrichum orbiculare ssd1Mutant EnhancesNicotiana benthamianaBasal Resistance by Activating a Mitogen-Activated Protein Kinase Pathway

et al. 2009

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Plant basal resistance is activated by virulent pathogens in susceptible host plants. A Colletotrichum orbiculare fungal mutant defective in the SSD1 gene, which regulates cell wall composition, is restricted by host basal resistance responses. Here, we identified the Nicotiana benthamiana signaling pathway involved in basal resistance by silencing the defenserelated genes required for restricting the growth of the C. orbiculare mutant. Only silencing of MAP Kinase Kinase2 or of both Salicylic Acid Induced Protein Kinase (SIPK) and Wound Induced Protein Kinase (WIPK), two mitogen-activated protein (MAP) kinases, allowed the mutant to infect and produce necrotic lesions similar to those of the wild type on inoculated leaves. The fungal mutant penetrated host cells to produce infection hyphae at a higher frequency in SIPK WIPK-silenced plants than in nonsilenced plants, without inducing host cellular defense responses. Immunocomplex kinase assays revealed that SIPK and WIPK were more active in leaves inoculated with mutant fungus than with the wild type, suggesting that induced resistance correlates with MAP kinase activity. Infiltration of heat-inactivated mutant conidia induced both SIPK and WIPK more strongly than did those of the wild type, while conidial exudates of the wild type did not suppress MAP kinase induction by mutant conidia. Therefore, activation of a specific MAP kinase pathway by fungal cell surface components determines the effective level of basal plant resistance.

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Monoclonal antibodies which show restricted binding to four Colletotrichum species: C. lindemuthianum, C. malvarum, C. orbiculare and C. trifolii

Cited by 46 publications

References 27 publications

Use of Monoclonal Antibodies to Study Differentiation of Colletotrichum Infection Structures

Use of Monoclonal Antibodies to Study Differentiation of Colletotrichum Infection Structures

Expression cloning of a fungal proline‐rich glycoprotein specific to the biotrophic interface formed in the Colletotrichum–bean interaction

TheColletotrichum orbiculare ssd1Mutant EnhancesNicotiana benthamianaBasal Resistance by Activating a Mitogen-Activated Protein Kinase Pathway

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