A new class of tetraspanins in fungi

Gourgues, Mathieu; Clergeot, Pierre-Henri; Veneault, C.; Cots, Joaquim; Sibuet, S; Simon, Adeline; Levis, Caroline; Langin, Thierry; Lebrun, Marc

doi:10.1016/s0006-291x(02)02355-0

Cited by 36 publications

(35 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…PaPls1 displays two exons of 402 bp and 273 bp, interrupted by an intron of 76 bp. MgPLS1 has an additional intron (20).…”

Section: Resultsmentioning

confidence: 99%

“…1A) as Pls1 tetraspanins (20). PaPls1 TMs have charged/polar amino acids conserved among fungal tetraspanins, and PaPls1 ECL2 displayed the same cysteine-based pattern as Pls1 tetraspanins (CCG-X 14 -C-X 10 -C [ Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Animal tetraspanins are involved in different biological processes including sperm-egg fusion, entry of parasites or viruses into host cells, cell-cell interactions in central nervous system or immune system (B-cell-T-cell immunological synapse), cell adhesion, motility, polarity, and trafficking of membrane proteins (23,33). Surprisingly, additional Pls1 orthologues were identified in saprobic fungi devoid of appressorium such as Neurospora crassa (20), Coprinopsis cinerea (26), Chaetomium globosum, Podospora anserina, Trichoderma reesei, and Phanerochete chrysosporium (31). To date, the role of Pls1 tetraspanins in these nonpathogenic fungi is unknown.…”

mentioning

confidence: 99%

See 2 more Smart Citations

The Crucial Role of the Pls1 Tetraspanin during Ascospore Germination in Podospora anserina Provides an Example of the Convergent Evolution of Morphogenetic Processes in Fungal Plant Pathogens and Saprobes

et al. 2008

View full text Add to dashboard Cite

Pls1 tetraspanins were shown for some pathogenic fungi to be essential for appressorium-mediated penetration into their host plants. We show here that Podospora anserina, a saprobic fungus lacking appressorium, contains PaPls1, a gene orthologous to known PLS1 genes. Inactivation of PaPls1 demonstrates that this gene is specifically required for the germination of ascospores in P. anserina. These ascospores are heavily melanized cells that germinate under inducing conditions through a specific pore. On the contrary, MgPLS1, which fully complements a ⌬PaPls1 ascospore germination defect, has no role in the germination of Magnaporthe grisea nonmelanized ascospores but is required for the formation of the penetration peg at the pore of its melanized appressorium. P. anserina mutants with mutation of PaNox2, which encodes the NADPH oxidase of the NOX2 family, display the same ascospore-specific germination defect as the ⌬PaPls1 mutant. Both mutant phenotypes are suppressed by the inhibition of melanin biosynthesis, suggesting that they are involved in the same cellular process required for the germination of P. anserina melanized ascospores. The analysis of the distribution of PLS1 and NOX2 genes in fungal genomes shows that they are either both present or both absent. These results indicate that the germination of P. anserina ascospores and the formation of the M. grisea appressorium penetration peg use the same molecular machinery that includes Pls1 and Nox2. This machinery is specifically required for the emergence of polarized hyphae from reinforced structures such as appressoria and ascospores. Its recurrent recruitment during fungal evolution may account for some of the morphogenetic convergence observed in fungi.Convergent evolution of trophic strategies and morphogenetic processes is a hallmark of fungi (27). For example, many fungi belonging to different fungal clades are phytopathogenic, whereas their close relatives are saprobic. These plant parasitic fungi may penetrate into their host plants using a specialized structure called the appressorium. Appressoria are attached to the surface of plants and redirect fungal growth into the host tissues underneath through the formation of a penetration peg. Due to their importance in pathogenicity, appressoria are studied in fungi such as Magnaporthe grisea, a devastating pathogen of rice (25, 54), Botrytis cinerea, a wide-host-range plant pathogen (19), and Colletotrichum lindemuthianum, an important pathogen of beans (13). These three fungi belong to two different clades of ascomycetes. M. grisea and C. lindemuthianum are in the Sordariomycetes and B. cinerea in Leotiomycetes. A significant number of species related to these three fungi are saprobic. Which of the parasitic or saprobic lifestyles displayed by these organisms arise by convergent evolution is thus crucial to understand their evolution. An answer to this question is to establish whether appressoria are homoplasious or homologous in Sordariomycetes and Leotiomycetes and whether appressorium-specific ...

show abstract

“…PaPls1 displays two exons of 402 bp and 273 bp, interrupted by an intron of 76 bp. MgPLS1 has an additional intron (20).…”

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

The Crucial Role of the Pls1 Tetraspanin during Ascospore Germination in Podospora anserina Provides an Example of the Convergent Evolution of Morphogenetic Processes in Fungal Plant Pathogens and Saprobes

et al. 2008

View full text Add to dashboard Cite

show abstract

“…Here, we undertook qRT-PCR analysis of cDNAs synthesized from RNA extracted from appressoria of strain T4. The tetraspanin gene BcPLS1 (19) was used as a reference, as the BcPLS1 protein is required for appressorium-mediated penetration (20 Fig. 2A) was carried out using a partial cDNA sequence (GenBank accession no.…”

Section: Resultsmentioning

confidence: 99%

ABotrytis cinereaEmopamil Binding Domain Protein, Required for Full Virulence, Belongs to a Eukaryotic Superfamily Which Has Expanded in Euascomycetes

et al. 2008

View full text Add to dashboard Cite

A previous transcriptomic analysis of 3,032 fungal genes identified the Botrytis cinerea PIE3 (BcPIE3) gene to be up-regulated early in planta (A. Gioti, A. Simon, P. Le Pêcheur, C. Giraud, J. M. Pradier, M. Viaud, and C. Levis, J. Mol. Biol. 358:372-386, 2006). In the present study, BcPIE3 was disrupted in order to determine its implication in pathogenicity. BcPIE3 was shown to be a virulence factor, since the ⌬BcPIE3 mutant was blocked during the colonization of tomato and bean leaves, giving lesions reduced in size by at least 74%. Within the emopamil binding domain (EBD), BcPIE3 shows significant structural similarities to mammalian emopamil binding proteins (EBPs). Mammalian EBPs function as sterol isomerases, but an analysis of the sterol content and the results of growth inhibition experiments with the ⌬BcPIE3 strain indicated that BcPIE3 is dispensable for ergosterol biosynthesis. The systematic identification of EBD-containing proteins included in public databases showed that these proteins constitute a protein superfamily present only in eukaryotes. Phylogenetic analysis showed that the ancestral EBD-encoding gene was duplicated in the common ancestor of animals and fungi after the split from plants. Finally, we present evidence that the EBP phylogenetic clade of this superfamily has further expanded exclusively in euascomycetes, especially in B. cinerea, which contains three copies of the EBP gene.Botrytis cinerea is a ubiquitous fungus capable of infecting a wide range of plants, fruits, and ornamentals at any stage of their development (15,30). In order to identify novel pathogenicity determinants, we recently studied the expression profiles of B. cinerea genes during the infection of Arabidopsis thaliana leaves. Among the genes shown to be induced in planta, one called B. cinerea PIE3 (BcPIE3) was found to be highly expressed 24 to 29 h after the inoculation of the fungus onto the plant leaves (18). To gain insight into early infection events, this gene was further studied.BcPIE3 showed strong similarity to mammalian emopamil binding proteins (EBPs). EBPs are integral, nonglycosylated proteins of the endoplasmic reticulum membrane, characterized by the presence of four transmembrane (TM) segments forming a binding domain for the drug emopamil, a phenylalkylamine Ca 2ϩ antagonist. This domain is called the emopamil binding domain (EBD). Mammalian EBPs (43, 25) have received increasing attention due to their binding properties. Indeed, the binding of sigma ligands but also of numerous, structurally diverse drugs and fungicides on the EBD (36) exerts anti-ischemic effects in animal models (43). Mammalian EBPs have been further studied because of a number of syndromes caused by EBP gene mutations, such as the genetic disorder X-linked dominant chondrodysplasia punctata, Conradi-Hünermann syndrome (5, 26), CHILD (congenital hemidysplasia with ichthyosiform erythroderma and limb defects) syndrome (21), and the "tattered" mouse phenotype (13).According to the above-mentioned studies, the molecular patholo...

show abstract

“…In addition to mammals, they have been found in Schistosomes (Wright 1990), early metazoans (Adell 2004), fungi (Gourgues 2002), and nematodes (Moribe 2004). Currently, more than 30 tetraspanins have been identified.…”

Section: Tetraspanin Structurementioning

confidence: 99%

The Tetraspanin CD9 Localizes to Platelet-Platelet Contacts and Regulates Thrombus Stability

Hill¹

View full text Add to dashboard Cite

A new class of tetraspanins in fungi

Cited by 36 publications

References 31 publications

The Crucial Role of the Pls1 Tetraspanin during Ascospore Germination in Podospora anserina Provides an Example of the Convergent Evolution of Morphogenetic Processes in Fungal Plant Pathogens and Saprobes

The Crucial Role of the Pls1 Tetraspanin during Ascospore Germination in Podospora anserina Provides an Example of the Convergent Evolution of Morphogenetic Processes in Fungal Plant Pathogens and Saprobes

ABotrytis cinereaEmopamil Binding Domain Protein, Required for Full Virulence, Belongs to a Eukaryotic Superfamily Which Has Expanded in Euascomycetes

The Tetraspanin CD9 Localizes to Platelet-Platelet Contacts and Regulates Thrombus Stability

Contact Info

Product

Resources

About