“…While aph1 is able to differentiate penetration pegs, the development of this structure is probably affected in the cst1 mutant (Tsuji et al 2003). A third mutant, designated 82335, was also shown to have a defect in penetration-peg formation (Katoh et al 1988). APH1 encodes a predicted tRNA methyltransferase, CST1 a putative transcription factor related to yeast STE12, while the molecular lesion in mutant 82335 is unknown (Y. Takano and N. Takayanagi, unpublished data; Tsuji et al 2003).…”
Section: Papillary Callose Formation Is Induced By Penetration-peg Fomentioning
Pathogenesis of nonadapted fungal pathogens is often terminated coincident with their attempted penetration into epidermal cells of nonhost plants. The genus Colletotrichum represents an economically important group of fungal plant pathogens that are amenable to molecular genetic analysis. Here, we investigated interactions between Arabidopsis and Colletotrichum to gain insights in plant and pathogen processes activating nonhost resistance responses. Three tested nonadapted Colletotrichum species differentiated melanized appressoria on Arabidopsis leaves but failed to form intracellular hyphae. Plant cells responded to Colletotrichum invasion attempts by the formation of PMR4/GSL5-dependent papillary callose. Appressorium differentiation and melanization were insufficient to trigger this localized plant cell response, but analysis of nonpathogenic C. lagenarium mutants implicates penetration-peg formation as the inductive cue. We show that Arabidopsis PEN1 syntaxin controls timely accumulation of papillary callose but is functionally dispensable for effective preinvasion (penetration) resistance in nonhost interactions. Consistent with this observation, green fluorescent protein-tagged PEN1 did not accumulate at sites of attempted penetration by either adapted or nonadapted Colletotrichum species, in contrast to the pronounced focal accumulations of PEN1 associated with entry of powdery mildews. We observed extensive reorganization of actin microfilaments leading to polar orientation of large actin bundles towards appressorial contact sites in interactions with the nonadapted Colletotrichum species. Pharmacological inhibition of actin filament function indicates a functional contribution of the actin cytoskeleton for both preinvasion resistance and papillary callose formation. Interestingly, the incidence of papilla formation at entry sites was greatly reduced in interactions with C. higginsianum isolates, indicating that this adapted pathogen may suppress preinvasion resistance at the cell periphery.
“…While aph1 is able to differentiate penetration pegs, the development of this structure is probably affected in the cst1 mutant (Tsuji et al 2003). A third mutant, designated 82335, was also shown to have a defect in penetration-peg formation (Katoh et al 1988). APH1 encodes a predicted tRNA methyltransferase, CST1 a putative transcription factor related to yeast STE12, while the molecular lesion in mutant 82335 is unknown (Y. Takano and N. Takayanagi, unpublished data; Tsuji et al 2003).…”
Section: Papillary Callose Formation Is Induced By Penetration-peg Fomentioning
Pathogenesis of nonadapted fungal pathogens is often terminated coincident with their attempted penetration into epidermal cells of nonhost plants. The genus Colletotrichum represents an economically important group of fungal plant pathogens that are amenable to molecular genetic analysis. Here, we investigated interactions between Arabidopsis and Colletotrichum to gain insights in plant and pathogen processes activating nonhost resistance responses. Three tested nonadapted Colletotrichum species differentiated melanized appressoria on Arabidopsis leaves but failed to form intracellular hyphae. Plant cells responded to Colletotrichum invasion attempts by the formation of PMR4/GSL5-dependent papillary callose. Appressorium differentiation and melanization were insufficient to trigger this localized plant cell response, but analysis of nonpathogenic C. lagenarium mutants implicates penetration-peg formation as the inductive cue. We show that Arabidopsis PEN1 syntaxin controls timely accumulation of papillary callose but is functionally dispensable for effective preinvasion (penetration) resistance in nonhost interactions. Consistent with this observation, green fluorescent protein-tagged PEN1 did not accumulate at sites of attempted penetration by either adapted or nonadapted Colletotrichum species, in contrast to the pronounced focal accumulations of PEN1 associated with entry of powdery mildews. We observed extensive reorganization of actin microfilaments leading to polar orientation of large actin bundles towards appressorial contact sites in interactions with the nonadapted Colletotrichum species. Pharmacological inhibition of actin filament function indicates a functional contribution of the actin cytoskeleton for both preinvasion resistance and papillary callose formation. Interestingly, the incidence of papilla formation at entry sites was greatly reduced in interactions with C. higginsianum isolates, indicating that this adapted pathogen may suppress preinvasion resistance at the cell periphery.
“…The penetration hypha of M. grisea and C. lagenarium is small in diameter compared to the pore (Katoh et al, 1988;Howard et al, 1991a). This suggests that forces other than turgor pressure alone are responsible for the extension of the tip of the penetration hypha.…”
SUMMARY
Many fungi differentiate specific infection structures in order to infect the host plant. The spore attaches to the host surface, the cuticle, and the germ tube may recognize suitable penetration sites, over which an appressorium is formed. Additional wall layers in appressoria of many fungi suggest that this structure supports increasing pressure during the penetration process. During appressorium formation, synthesis of polymer‐degrading enzymes is often initiated. Cutinases, cellulases and pectin‐degrading enzymes can be formed in a developmentally controlled or adaptive, i.e. substrate‐dependent, fashion. The penetration hypha develops below the appressorium. This hypha has a new wall structure and exhibits features which serve to breach the plant cell wall. However, at present it is not clear whether penetration hyphae arising from appressoria are more efficient in penetration or induce less damage than hyphae which penetrate without detectable special adaptations. The infection hypha differentiates within the host. During differentiation a characteristic set of enzymes is synthesized to enable successful establishment of the host‐pathogen relationship. If, as in most cases, multiple forms of cell wall‐degrading enzymes are formed by the pathogen, mutagenesis or deletion of a gene encoding one of these enzymes very often has no effect on pathogenicity or even virulence. Proof is missing very often that an enzyme is needed at the right time and at the right site of infection.
Events occurring during differentiation of fungal infection structures are reviewed with special emphasis on Magnaporthe grisea, Colletotrichum spp., and rust fungi, and common features which may be of importance to the success of infection are discussed.
“…Melanin also provides cell wall rigidity to the appressoria, which is necessary for focusing the turgor forces for vertical penetration (9). Besides melanin biosynthesis, synthesis and secretion of cellulase (21) and penetration peg formation (8,17) have been reported as essential factors for penetration. However, cutinase may not be needed for penetration by Colletotrichum lagenarium (2,3).…”
Appressoria of the phytopathogenic fungus Colletotrichum lagenarium contain melanin, which has been implicated as an important factor in the penetration of host plants. A cDNA clone containing the melanin biosynthetic gene encoding scytalone dehydratase (SCD1) from C. lagenarium was identified by hybridization with a heterologous cDNA probe from Magnaporthe grisea. The cDNA clone was used to identify a cosmid containing SCD1 in a genomic library of C. lagenarium, and the nucleotide sequence was determined for both the cDNA and genomic clones. The SCD1 gene contained one open reading frame composed of 188 codons and two deduced introns of 57 and 67 nucleotides. The deduced amino acid sequence of the N-terminal region of SCD1 showed high similarity to the amino acid sequence of scytalone dehydratase from Cochliobolus miyabeanus. A plasmid containing the SCD1 gene transformed the melanin-deficient mutant 9201Y (Scd ؊) to the wild phenotype but did not complement the conditional scytalone dehydratase-deficient mutant C. lagenarium 8015. Genomic DNA analysis indicated that the SCD1 gene is a single locus in C. lagenarium. Transcripts of the SCD1 gene were detected 2 h after the start of conidial germination.
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