Defensins from Insects and Plants Interact with Fungal Glucosylceramides

Thevissen, Karin; Warnecke, Dirk; François, Isabelle; Leipelt, Martina; Heinz, Ernst; Ott, Claudia; Zähringer, Ulrich; Thomma, B.P.H.J.; Ferket, Kathelijne K.A.; Cammue, Bruno P. A.

doi:10.1074/jbc.m311165200

Cited by 326 publications

(326 citation statements)

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“…An array of resistance mechanisms to AMPs are known in pathogens, some of which are involved in a single gene product [67,68]. In some cases, derived microbial strains are more resistant than the wild type [69], which is consistent with the hypothesis that positive selection on microbial genomes can result in increased resistance to AMPs. However, it could be more likely that resistance is easy to evolve and happens frequently.…”

Section: Discussionsupporting

confidence: 67%

Adaptive evolution after duplication of penaeidin antimicrobial peptides

Padhi

Verghese

Otta

et al. 2007

Fish & Shellfish Immunology

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Penaeidin antimicrobial peptides in penaeid shrimps are an important component of their innate immune system that provides immunity against infection caused by several gram-positive bacteria and filamentous fungal species. Despite the knowledge on the identification and characterization of these peptides in penaeid shrimps, little is known about the evolutionary pattern of these peptides and the underlying genetic mechanisms that maintain high sequence diversities in the penaeidin gene family. Based on the phylogenetic analyses and maximum likelihood-based codon substitution analyses, here we present the convincing evidence that multiple copies of penaeidins have evolved by gene duplication, and positive Darwinian selection (adaptive evolution) is the likely cause of accelerated rate of amino acid substitutions among these duplicated genes.While the average ratio of non-synonymous to synonymous substitutions (u) for the entire coding region of both active domains is 0.9805, few codon sites showed significantly higher u (3.73). The likelihood ratio tests that compare models incorporating positive selection (u > 1) at certain codon sites with models not incorporating positive selection (u < 1), failed to reject (p ¼ 0) the evidence of positive Darwinian selection. The rapid adaptive evolution of this gene family might be directed by the pathogens and the faster rate of amino acid substitutions in the N-terminal proline-rich and C-terminal cysteine-rich domains could be due to their direct involvement in the protection against pathogens. When the host expose to different habitats/environment an accelerated rate of amino acid substitutions in both the active domains may also be expected.

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Section: Discussionsupporting

confidence: 67%

Adaptive evolution after duplication of penaeidin antimicrobial peptides

Padhi

Verghese

Otta

et al. 2007

Fish & Shellfish Immunology

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“…Fungal glucosylceramides can elicit defense responses in rice plants and cell suspension cultures of rice, and treatment with these fungal glucosylceramides protects rice plants against fungal infection (19 -21). The plant defensin RsAFP2 from radish seeds interacts specifically with fungal glucosylceramides (22). Pichia pastoris and Candida albicans strains deficient in the gene responsible for glucosylceramide synthesis are resistant to RsAFP2 (22).…”

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confidence: 99%

Identification of Fungal Sphingolipid C9-methyltransferases by Phylogenetic Profiling

Ternes

Sperling

Albrecht

et al. 2006

Journal of Biological Chemistry

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Fungal glucosylceramides play an important role in plant-pathogen interactions enabling plants to recognize the fungal attack and initiate specific defense responses. A prime structural feature distinguishing fungal glucosylceramides from those of plants and animals is a methyl group at the C9-position of the sphingoid base, the biosynthesis of which has never been investigated. Using information on the presence or absence of C9-methylated glucosylceramides in different fungal species, we developed a bioinformatics strategy to identify the gene responsible for the biosynthesis of this C9-methyl group. This phylogenetic profiling allowed the selection of a single candidate out of 24 -71 methyltransferase sequences present in each of the fungal species with C9-methylated glucosylceramides. A Pichia pastoris knock-out strain lacking the candidate sphingolipid C9-methyltransferase was generated, and indeed, this strain contained only non-methylated glucosylceramides. In a complementary approach, a Saccharomyces cerevisiae strain was engineered to produce glucosylceramides suitable as a substrate for C9-methylation. C9-methylated sphingolipids were detected in this strain expressing the candidate from P. pastoris, demonstrating its function as a sphingolipid C9-methyltransferase. The enzyme belongs to the superfamily of S-adenosylmethionine-(SAM)-dependent methyltransferases and shows highest sequence similarity to plant and bacterial cyclopropane fatty acid synthases. An in vitro assay showed that sphingolipid C9-methylation is membranebound and requires SAM and ⌬4,8-desaturated ceramide as substrates.

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“…Their evolutionary relationship with DTAFPs is strengthened by the discovery that heliomicin and plant defensins interact with the same target in the fungal plasma membrane 23 . These newly discovered sequences are distributed in four Orders of Insecta (Arthopoda) that include Lepidoptera, Hemiptera, Neuroptera and Coleoptera, and species from Tardigrada (Fig.…”

Section: Restricted Distribution Ofmentioning

confidence: 99%