The cellulose synthase 3 (CesA3) gene of oomycetes: structure, phylogeny and influence on sensitivity to carboxylic acid amide (CAA) fungicides

Blum, Mathias; Gamper, Hannes A.; Waldner, Maya; Sierotzki, Helge; Gisi, U.

doi:10.1016/j.funbio.2012.02.003

Cited by 41 publications

(24 citation statements)

References 61 publications

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“…1. The topology of the tree was very consistent with previously published oomycete phylogenies and depicted the well-established peronosporalean and saprolegnian galaxies (38,(53)(54)(55). Major clades corresponding to the Peronosporales (Phytophthora spp.…”

Section: Transcriptome Sequencing Overviewsupporting

confidence: 82%

“…The Lagenidium giganteum cellulose synthase 3 (CesA3) gene (GenBank accession number KM025055) was incorporated into a previously published oomycete CesA3 multiple-sequence alignment (TreeBASE S12300) using Clustal X (37). The alignment was optimized manually by editing the L. giganteum sequence to preserve the aligned nucleotide positions used previously to infer oomycete phylogeny (38). The final data set consisted of 3,344 characters for 26 taxa.…”

Section: Methodsmentioning

confidence: 99%

“…1). All of these clades appeared as monophyletic groups, except for Pythium spp., which have been shown to be paraphyletic (38,53,55). The entomopathogen L. giganteum was not grouped in any of the clades but appeared as a basal lineage to a cluster containing both Peronosporales and Pythiales.…”

Section: Transcriptome Sequencing Overviewmentioning

confidence: 96%

“…The 3,782-bp full-length L. giganteum cellulose synthase transcript was annotated as cellulose synthase 3 (CesA3) based on strong similarity to previously published sequences (38) and comparison with L. giganteum paralogs (data not shown). Fragments obtained using previously published CesA3-specific primers (38) were characterized by sequences identical to the sequences confirmed by RACE-PCR (not shown).…”

Section: Transcriptome Sequencing Overviewmentioning

confidence: 99%

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Transcriptome Analysis of the Entomopathogenic Oomycete Lagenidium giganteum Reveals Putative Virulence Factors

Velasquez

Abiff

Fins

et al. 2014

Appl Environ Microbiol

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A combination of 454 pyrosequencing and Sanger sequencing was used to sample and characterize the transcriptome of the entomopathogenic oomycete Lagenidium giganteum. More than 50,000 high-throughput reads were annotated through homology searches. Several selected reads served as seeds for the amplification and sequencing of full-length transcripts. Phylogenetic analyses inferred from full-length cellulose synthase alignments revealed that L giganteum is nested within the peronosporalean galaxy and as such appears to have evolved from a phytopathogenic ancestor. In agreement with the phylogeny reconstructions, full-length L. giganteum oomycete effector orthologs, corresponding to the cellulose-binding elicitor lectin (CBEL), crinkler (CRN), and elicitin proteins, were characterized by domain organizations similar to those of pathogenicity factors of plantpathogenic oomycetes. Importantly, the L. giganteum effectors provide a basis for detailing the roles of canonical CRN, CBEL, and elicitin proteins in the infectious process of an oomycete known principally as an animal pathogen. Finally, phylogenetic analyses and genome mining identified members of glycoside hydrolase family 5 subfamily 27 (GH5_27) as putative virulence factors active on the host insect cuticle, based in part on the fact that GH5_27 genes are shared by entomopathogenic oomycetes and fungi but are underrepresented in nonentomopathogenic genomes. The genomic resources gathered from the L. giganteum transcriptome analysis strongly suggest that filamentous entomopathogens (oomycetes and fungi) exhibit convergent evolution: they have evolved independently from plant-associated microbes, have retained genes indicative of plant associations, and may share similar cores of virulence factors, such as GH5_27 enzymes, that are absent from the genomes of their plant-pathogenic relatives.

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Section: Transcriptome Sequencing Overviewsupporting

confidence: 82%

Section: Methodsmentioning

confidence: 99%

Section: Transcriptome Sequencing Overviewmentioning

confidence: 96%

Section: Transcriptome Sequencing Overviewmentioning

confidence: 99%

See 2 more Smart Citations

Transcriptome Analysis of the Entomopathogenic Oomycete Lagenidium giganteum Reveals Putative Virulence Factors

Velasquez

Abiff

Fins

et al. 2014

Appl Environ Microbiol

View full text Add to dashboard Cite

show abstract

“…Alternatively, some oomycete CHS -like genes might have evolved essential functions other than the biosynthesis of structural GlcNAc-based polymers, such as the biosynthesis of glycoprotein glycans. Because of the high impact of oomycete diseases on crop and aquatic animal production, and the limits of targeting only cellulose biosynthesis to combat these pests [9], [10], it is now important to study the structure-activity relationship of oomycete CHS-like enzymes, which form a distinct group in CHS phylograms [50], [51]. This should shed new light on their putative function as cell wall biosynthetic enzymes, and may allow the identification of new key targets for herbicides and fungicides with a narrower spectrum and reduced ecotoxicity.…”

Section: Discussionmentioning

confidence: 99%

Aphanomyces euteiches Cell Wall Fractions Containing Novel Glucan-Chitosaccharides Induce Defense Genes and Nuclear Calcium Oscillations in the Plant Host Medicago truncatula

et al. 2013

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N-acetylglucosamine-based saccharides (chitosaccharides) are components of microbial cell walls and act as molecular signals during host-microbe interactions. In the legume plant Medicago truncatula, the perception of lipochitooligosaccharide signals produced by symbiotic rhizobia and arbuscular mycorrhizal fungi involves the Nod Factor Perception (NFP) lysin motif receptor-like protein and leads to the activation of the so-called common symbiotic pathway. In rice and Arabidopsis, lysin motif receptors are involved in the perception of chitooligosaccharides released by pathogenic fungi, resulting in the activation of plant immunity. Here we report the structural characterization of atypical chitosaccharides from the oomycete pathogen Aphanomyces euteiches, and their biological activity on the host Medicago truncatula. Using a combination of biochemical and biophysical approaches, we show that these chitosaccharides are linked to β-1,6-glucans, and contain a β-(1,3;1,4)-glucan backbone whose β-1,3-linked glucose units are substituted on their C-6 carbon by either glucose or N-acetylglucosamine residues. This is the first description of this type of structural motif in eukaryotic cell walls. Glucan-chitosaccharide fractions of A. euteiches induced the expression of defense marker genes in Medicago truncatula seedlings independently from the presence of a functional Nod Factor Perception protein. Furthermore, one of the glucan-chitosaccharide fractions elicited calcium oscillations in the nucleus of root cells. In contrast to the asymmetric oscillatory calcium spiking induced by symbiotic lipochitooligosaccharides, this response depends neither on the Nod Factor Perception protein nor on the common symbiotic pathway. These findings open new perspectives in oomycete cell wall biology and elicitor recognition and signaling in legumes.

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Carboxylic Acid Amide (CAA) Fungicides

Gisi

Lamberth

Mehl

et al. 2019

Modern Crop Protection Compounds

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The cellulose synthase 3 (CesA3) gene of oomycetes: structure, phylogeny and influence on sensitivity to carboxylic acid amide (CAA) fungicides

Cited by 41 publications

References 61 publications

Transcriptome Analysis of the Entomopathogenic Oomycete Lagenidium giganteum Reveals Putative Virulence Factors

Transcriptome Analysis of the Entomopathogenic Oomycete Lagenidium giganteum Reveals Putative Virulence Factors

Aphanomyces euteiches Cell Wall Fractions Containing Novel Glucan-Chitosaccharides Induce Defense Genes and Nuclear Calcium Oscillations in the Plant Host Medicago truncatula

Carboxylic Acid Amide (CAA) Fungicides

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