A group of over 20 organisations from the public sector, charities and the private sector have got together to produce two videos to help tackle the threat posed to our plant nurseries, gardens, woodlands and countryside from two devastating Phytophthora pathogens, Phytophthora ramorum and Phytophthora kernoviae.
This film is aimed more at professionals who work in environments where the diseases may be present or that could easily be contaminated. It describes the diseases in more detail and offers advice on appropriate biosecurity measures to help prevent the spread. It may also appeal to those studying life sciences at college or university.
Prior to 2007, late blight was not reported as a serious threat to tomato cultivation in India although the disease has been known on potato since 1953. During the July–December cropping season of 2009 and 2010, severe late blight epidemics were observed in Karnataka state of India, causing crop losses up to 100%. Nineteen Phytophthora isolates, recovered from late blight affected tomato tissues from different localities in Karnataka state between 2009 and 2010, were identified as Phytophthora infestans based on morphology, a similarity search of ITS sequences at GenBank and species-specific PCR using PINF/ITS5 primer pair. The isolates were further assessed for metalaxyl sensitivity, mating type, mitochondrial DNA (mtDNA) haplotype, DNA fingerprinting patterns based on simple sequence repeats (SSR) and RFLPs using the RG57 probe and aggressiveness on tomato. All isolates were metalaxyl resistant, A2 mating type, mtDNA haplotype Ia and had identical SSR and RG57 fingerprints and highly aggressive on tomato. The phenotypic and genotypic characters of isolates examined in this study were found to be similar to that of 13_A2 genotype of P. infestans population reported in Europe. Thus, appearance of new population similar to 13_A2 genotype was responsible for severe late blight epidemics on tomato in South-West India.
A virus designated Phytophthora infestans RNA virus 3 (PiRV-3) was characterized from an isolate of P. infestans that was co-infected with a second previously described virus, PiRV-4, a member of the virus family Narnaviridae (Cai et al., 2012). The genome of PiRV-3 is 8112 nt and one strand, designated the positive strand, has two deduced overlapping open reading frames linked by a potential frameshift sequence. The first open reading frame (ORF1) is predicted to encode a protein of unknown function, and ORF2 is predicted to encode an RNA-dependent RNA polymerase (RdRp) most closely related to six unclassified dsRNA viruses of filamentous fungi. The genome organizations of five of the related viruses are similar to PiRV-3, indicating taxonomic linkage among those viruses. We suggest that PiRV-3 and related viruses should be collected into a new virus taxon.
In 2007, Comparative Fungal Genomics Platform (CFGP; http://cfgp.snu.ac.kr/) was publicly open with 65 genomes corresponding to 58 fungal and Oomycete species. The CFGP provided six bioinformatics tools, including a novel tool entitled BLASTMatrix that enables search homologous genes to queries in multiple species simultaneously. CFGP also introduced Favorite, a personalized virtual space for data storage and analysis with these six tools. Since 2007, CFGP has grown to archive 283 genomes corresponding to 152 fungal and Oomycete species as well as 201 genomes that correspond to seven bacteria, 39 plants and 105 animals. In addition, the number of tools in Favorite increased to 27. The Taxonomy Browser of CFGP 2.0 allows users to interactively navigate through a large number of genomes according to their taxonomic positions. The user interface of BLASTMatrix was also improved to facilitate subsequent analyses of retrieved data. A newly developed genome browser, Seoul National University Genome Browser (SNUGB), was integrated into CFGP 2.0 to support graphical presentation of diverse genomic contexts. Based on the standardized genome warehouse of CFGP 2.0, several systematic platforms designed to support studies on selected gene families have been developed. Most of them are connected through Favorite to allow of sharing data across the platforms.
Background - Oomycetes are fungal-like microorganisms evolutionary distinct from true fungi, belonging to the Stramenopile lineage and comprising major plant pathogens. Both oomycetes and fungi express proteins able to interact with cellulose, a major component of plant and oomycete cell walls, through the presence of carbohydrate-binding module belonging to the family 1 (CBM1). Fungal CBM1-containing proteins were implicated in cellulose degradation whereas in oomycetes, the Cellulose Binding Elicitor Lectin (CBEL), a well-characterized CBM1-protein from Phytophthora parasitica, was implicated in cell wall integrity, adhesion to cellulosic substrates and induction of plant immunity.
Results - To extend our knowledge on CBM1-containing proteins in oomycetes, we have conducted a comprehensive analysis on 60 fungi and 7 oomycetes genomes leading to the identification of 518 CBM1-containing proteins. In plant-interacting microorganisms, the larger number of CBM1-protein coding genes is expressed by necrotroph and hemibiotrophic pathogens, whereas a strong reduction of these genes is observed in symbionts and biotrophs. In fungi, more than 70% of CBM1-containing proteins correspond to enzymatic proteins in which CBM1 is associated with a catalytic unit involved in cellulose degradation. In oomycetes more than 90% of proteins are similar to CBEL in which CBM1 is associated with a non-catalytic PAN/Apple domain, known to interact with specific carbohydrates or proteins. Distinct Stramenopile genomes like diatoms and brown algae are devoid of CBM1 coding genes. A CBM1-PAN/Apple association 3D structural modeling was built allowing the identification of amino acid residues interacting with cellulose and suggesting the putative interaction of the PAN/Apple domain with another type of glucan. By Surface Plasmon Resonance experiments, we showed that CBEL binds to glycoproteins through galactose or N-acetyl-galactosamine motifs.
Conclusions - This study provides insight into the evolution and biological roles of CBM1-containing proteins from oomycetes. We show that while CBM1s from fungi and oomycetes are similar, they team up with different protein domains, either in proteins implicated in the degradation of plant cell wall components in the case of fungi or in proteins involved in adhesion to polysaccharidic substrates in the case of oomycetes. This work highlighted the unique role and evolution of CBM1 proteins in oomycete among the Stramenopile lineage.
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