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Francis Martin - One of the best experts on this subject based on the ideXlab platform.
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Fatty acid metabolism in the ectomycorrhizal fungus Laccaria bicolor
New Phytologist, 2009Co-Authors: Marlis Reich, Francis Martin, Annegret Kohler, Cornelia Göbel, Marc Buee, Ivo Feussner, Andrea PolleAbstract:Here, the genome sequence of the ectomycorrhizal basidiomycete Laccaria bicolor was explored with the aim of constructing a genome-wide inventory of genes involved in fatty acid metabolism. Sixty-three genes of the major pathways were annotated and validated by the detection of the corresponding transcripts. Seventy-one per cent belonged to multigene families of up to five members. In the mycelium of L. bicolor, 19 different fatty acids were detected, including at low concentrations palmitvaccenic acid (16:1(11Z)), which is known to be a marker for arbuscular mycorrhizal fungi. The pathways of fatty acid biosynthesis and degradation in L. bicolor were reconstructed using lipid composition, gene annotation and transcriptional analysis. Annotation results indicated that saturated fatty acids were degraded in mitochondria, whereas degradation of modified fatty acids was confined to peroxisomes. Fatty acid synthase (FAS) was the second largest protein annotated in L. bicolor. Phylogenetic analysis indicated that L. bicolor, Ustilago maydis and Coprinopsis cinerea have a vertebrate-like type I FAS encoded as a single protein, whereas in other Basidiomycetes, including the human pathogenic basidiomycete Cryptococcus neoformans, and in most ascomycetes FAS is composed of the two structurally distinct subunits α and β.
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Fungi have three tetraspanin families with distinct functions
BMC Genomics, 2008Co-Authors: Karine Lambou, Catherine Sirven, Ellen M. Kellner, Crystel Barbisan, Adrienne Sexton, Francis Martin, Melanie Marguerettaz, Annegret Kohler, Didier Tharreau, Barbara J. HowlettAbstract:Tetraspanins are small membrane proteins that belong to a superfamily encompassing 33 members in human and mouse. These proteins act as organizers of membrane-signalling complexes. So far only two tetraspanin families have been identified in fungi. These are Pls1, which is required for pathogenicity of the plant pathogenic ascomycetes, Magnaporthe grisea, Botrytis cinerea and Colletotrichum lindemuthianum, and Tsp2, whose function is unknown. In this report, we describe a third family of tetraspanins (Tsp3) and a new family of tetraspanin-like proteins (Tpl1) in fungi. We also describe expression of some of these genes in M. grisea and a basidiomycete, Laccaria bicolor, and also their functional analysis in M. grisea. The exhaustive search for tetraspanins in fungal genomes reveals that higher fungi (Basidiomycetes and ascomycetes) contain three families of tetraspanins (Pls1, Tsp2 and Tsp3) with different distribution amongst phyla. Pls1 is found in ascomycetes and Basidiomycetes, whereas Tsp2 is restricted to Basidiomycetes and Tsp3 to ascomycetes. A unique copy of each of PLS1 and TSP3 was found in ascomycetes in contrast to TSP2, which has several paralogs in the Basidiomycetes, Coprinus cinereus and Laccaria bicolor. A tetraspanin-like family (Tpl1) was also identified in ascomycetes. Transcriptional analyses in various tissues of L. bicolor and M. grisea showed that PLS1 and TSP2 are expressed in all tissues in L. bicolor and that TSP3 and TPL1 are overexpressed in the sexual fruiting bodies (perithecia) and mycelia of M. grisea, suggesting that these genes are not pseudogenes. Phenotypic analysis of gene replacementmutants Δtsp3 and Δtpl1 of M. grisea revealed a reduction of the pathogenicity only on rice, in contrast to Δpls1 mutants, which are completely non-pathogenic on barley and rice. A new tetraspanin family (Tsp3) and a tetraspanin-like protein family (Tpl1) have been identified in fungi. Functional analysis by gene replacement showed that these proteins, as well as Pls1, are involved in the infection process of the plant pathogenic fungus M. grisea. The next challenge will be to decipher the role(s) of tetraspanins in a range of symbiotic, saprophytic and human pathogenic fungi.
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The major pathways of carbohydrate metabolism in the ectomycorrhizal basidiomycete Laccaria bicolor S238N
New Phytologist, 2008Co-Authors: Aurélie Deveau, Annegret Kohler, Pascale Frey-klett, Francis MartinAbstract:• The primary carbohydrate metabolism of an ectomycorrhizal fungus and its transcriptional regulation has never been characterized at the genome scale although it plays a fundamental role in the functioning of the symbiosis. In this study, the genome sequence of the ectomycorrhizal basidiomycete Laccaria bicolor S238N-H82 was explored to construct a comprehensive genome-wide inventory of pathways involved in primary carbohydrate metabolism. • Several genes and gene families were annotated, including those of the glycolysis, pentose phosphate pathway, tricarboxylic acid cycle, and trehalose and mannitol metabolism. The transcriptional regulation of these pathways was studied using whole-genome expression oligoarrays and quantitative polymerase chain reaction in free-living mycelium, ectomycorrhizas and fruiting bodies. • Pathways of carbohydrate biosynthesis and catabolism are identical in L. bicolor compared with other sequenced saprotrophic Basidiomycetes. • Ectomycorrhiza and fruiting body development induced the regulation of a restricted set of transcripts of the glycolytic, mannitol and trehalose metabolisms.
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Fungi have three tetraspanin families with distinct functions
BMC Genomics, 2008Co-Authors: Karine Lambou, Catherine Sirven, Crystel Barbisan, Adrienne Sexton, Francis Martin, Melanie Marguerettaz, Annegret Kohler, Didier Tharreau, Ellen Kellner, Barbara HowlettAbstract:Background: Tetraspanins are small membrane proteins that belong to a superfamily encompassing 33 members in human and mouse. These proteins act as organizers of membrane-signalling complexes. So far only two tetraspanin families have been identified in fungi. These are Pls1, which is required for pathogenicity of the plant pathogenic ascomycetes, Magnaporthe grisea, Botrytis cinerea and Colletotrichum lindemuthianum, and Tsp2, whose function is unknown. In this report, we describe a third family of tetraspanins (Tsp3) and a new family of tetraspanin-like proteins (Tpl1) in fungi. We also describe expression of some of these genes in M. grisea and a basidiomycete, Laccaria bicolor, and also their functional analysis in M. grisea. Results: The exhaustive search for tetraspanins in fungal genomes reveals that higher fungi (Basidiomycetes and ascomycetes) contain three families of tetraspanins (Pls1, Tsp2 and Tsp3) with different distribution amongst phyla. Pls1 is found in ascomycetes and Basidiomycetes, whereas Tsp2 is restricted to Basidiomycetes and Tsp3 to ascomycetes. A unique copy of each of PLS1 and TSP3 was found in ascomycetes in contrast to TSP2, which has several paralogs in the Basidiomycetes, Coprinus cinereus and Laccaria bicolor. A tetraspanin-like family (Tpl1) was also identified in ascomycetes. Transcriptional analyses in various tissues of L. bicolor and M. grisea showed that PLS1 and TSP2 are expressed in all tissues in L. bicolor and that TSP3 and TPL1 are overexpressed in the sexual fruiting bodies (perithecia) and mycelia of M. grisea, suggesting that these genes are not pseudogenes. Phenotypic analysis of gene replacementmutants Δtsp3 and Δtpl1 of M. grisea revealed a reduction of the pathogenicity only on rice, in contrast to Δpls1 mutants, which are completely non-pathogenic on barley and rice. Conclusion: A new tetraspanin family (Tsp3) and a tetraspanin-like protein family (Tpl1) have been identified in fungi. Functional analysis by gene replacement showed that these proteins, as well as Pls1, are involved in the infection process of the plant pathogenic fungus M. grisea. The next challenge will be to decipher the role(s) of tetraspanins in a range of symbiotic, saprophytic and human pathogenic fungi.
Annegret Kohler - One of the best experts on this subject based on the ideXlab platform.
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Fatty acid metabolism in the ectomycorrhizal fungus Laccaria bicolor
New Phytologist, 2009Co-Authors: Marlis Reich, Francis Martin, Annegret Kohler, Cornelia Göbel, Marc Buee, Ivo Feussner, Andrea PolleAbstract:Here, the genome sequence of the ectomycorrhizal basidiomycete Laccaria bicolor was explored with the aim of constructing a genome-wide inventory of genes involved in fatty acid metabolism. Sixty-three genes of the major pathways were annotated and validated by the detection of the corresponding transcripts. Seventy-one per cent belonged to multigene families of up to five members. In the mycelium of L. bicolor, 19 different fatty acids were detected, including at low concentrations palmitvaccenic acid (16:1(11Z)), which is known to be a marker for arbuscular mycorrhizal fungi. The pathways of fatty acid biosynthesis and degradation in L. bicolor were reconstructed using lipid composition, gene annotation and transcriptional analysis. Annotation results indicated that saturated fatty acids were degraded in mitochondria, whereas degradation of modified fatty acids was confined to peroxisomes. Fatty acid synthase (FAS) was the second largest protein annotated in L. bicolor. Phylogenetic analysis indicated that L. bicolor, Ustilago maydis and Coprinopsis cinerea have a vertebrate-like type I FAS encoded as a single protein, whereas in other Basidiomycetes, including the human pathogenic basidiomycete Cryptococcus neoformans, and in most ascomycetes FAS is composed of the two structurally distinct subunits α and β.
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Fungi have three tetraspanin families with distinct functions
BMC Genomics, 2008Co-Authors: Karine Lambou, Catherine Sirven, Ellen M. Kellner, Crystel Barbisan, Adrienne Sexton, Francis Martin, Melanie Marguerettaz, Annegret Kohler, Didier Tharreau, Barbara J. HowlettAbstract:Tetraspanins are small membrane proteins that belong to a superfamily encompassing 33 members in human and mouse. These proteins act as organizers of membrane-signalling complexes. So far only two tetraspanin families have been identified in fungi. These are Pls1, which is required for pathogenicity of the plant pathogenic ascomycetes, Magnaporthe grisea, Botrytis cinerea and Colletotrichum lindemuthianum, and Tsp2, whose function is unknown. In this report, we describe a third family of tetraspanins (Tsp3) and a new family of tetraspanin-like proteins (Tpl1) in fungi. We also describe expression of some of these genes in M. grisea and a basidiomycete, Laccaria bicolor, and also their functional analysis in M. grisea. The exhaustive search for tetraspanins in fungal genomes reveals that higher fungi (Basidiomycetes and ascomycetes) contain three families of tetraspanins (Pls1, Tsp2 and Tsp3) with different distribution amongst phyla. Pls1 is found in ascomycetes and Basidiomycetes, whereas Tsp2 is restricted to Basidiomycetes and Tsp3 to ascomycetes. A unique copy of each of PLS1 and TSP3 was found in ascomycetes in contrast to TSP2, which has several paralogs in the Basidiomycetes, Coprinus cinereus and Laccaria bicolor. A tetraspanin-like family (Tpl1) was also identified in ascomycetes. Transcriptional analyses in various tissues of L. bicolor and M. grisea showed that PLS1 and TSP2 are expressed in all tissues in L. bicolor and that TSP3 and TPL1 are overexpressed in the sexual fruiting bodies (perithecia) and mycelia of M. grisea, suggesting that these genes are not pseudogenes. Phenotypic analysis of gene replacementmutants Δtsp3 and Δtpl1 of M. grisea revealed a reduction of the pathogenicity only on rice, in contrast to Δpls1 mutants, which are completely non-pathogenic on barley and rice. A new tetraspanin family (Tsp3) and a tetraspanin-like protein family (Tpl1) have been identified in fungi. Functional analysis by gene replacement showed that these proteins, as well as Pls1, are involved in the infection process of the plant pathogenic fungus M. grisea. The next challenge will be to decipher the role(s) of tetraspanins in a range of symbiotic, saprophytic and human pathogenic fungi.
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The major pathways of carbohydrate metabolism in the ectomycorrhizal basidiomycete Laccaria bicolor S238N
New Phytologist, 2008Co-Authors: Aurélie Deveau, Annegret Kohler, Pascale Frey-klett, Francis MartinAbstract:• The primary carbohydrate metabolism of an ectomycorrhizal fungus and its transcriptional regulation has never been characterized at the genome scale although it plays a fundamental role in the functioning of the symbiosis. In this study, the genome sequence of the ectomycorrhizal basidiomycete Laccaria bicolor S238N-H82 was explored to construct a comprehensive genome-wide inventory of pathways involved in primary carbohydrate metabolism. • Several genes and gene families were annotated, including those of the glycolysis, pentose phosphate pathway, tricarboxylic acid cycle, and trehalose and mannitol metabolism. The transcriptional regulation of these pathways was studied using whole-genome expression oligoarrays and quantitative polymerase chain reaction in free-living mycelium, ectomycorrhizas and fruiting bodies. • Pathways of carbohydrate biosynthesis and catabolism are identical in L. bicolor compared with other sequenced saprotrophic Basidiomycetes. • Ectomycorrhiza and fruiting body development induced the regulation of a restricted set of transcripts of the glycolytic, mannitol and trehalose metabolisms.
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Fungi have three tetraspanin families with distinct functions
BMC Genomics, 2008Co-Authors: Karine Lambou, Catherine Sirven, Crystel Barbisan, Adrienne Sexton, Francis Martin, Melanie Marguerettaz, Annegret Kohler, Didier Tharreau, Ellen Kellner, Barbara HowlettAbstract:Background: Tetraspanins are small membrane proteins that belong to a superfamily encompassing 33 members in human and mouse. These proteins act as organizers of membrane-signalling complexes. So far only two tetraspanin families have been identified in fungi. These are Pls1, which is required for pathogenicity of the plant pathogenic ascomycetes, Magnaporthe grisea, Botrytis cinerea and Colletotrichum lindemuthianum, and Tsp2, whose function is unknown. In this report, we describe a third family of tetraspanins (Tsp3) and a new family of tetraspanin-like proteins (Tpl1) in fungi. We also describe expression of some of these genes in M. grisea and a basidiomycete, Laccaria bicolor, and also their functional analysis in M. grisea. Results: The exhaustive search for tetraspanins in fungal genomes reveals that higher fungi (Basidiomycetes and ascomycetes) contain three families of tetraspanins (Pls1, Tsp2 and Tsp3) with different distribution amongst phyla. Pls1 is found in ascomycetes and Basidiomycetes, whereas Tsp2 is restricted to Basidiomycetes and Tsp3 to ascomycetes. A unique copy of each of PLS1 and TSP3 was found in ascomycetes in contrast to TSP2, which has several paralogs in the Basidiomycetes, Coprinus cinereus and Laccaria bicolor. A tetraspanin-like family (Tpl1) was also identified in ascomycetes. Transcriptional analyses in various tissues of L. bicolor and M. grisea showed that PLS1 and TSP2 are expressed in all tissues in L. bicolor and that TSP3 and TPL1 are overexpressed in the sexual fruiting bodies (perithecia) and mycelia of M. grisea, suggesting that these genes are not pseudogenes. Phenotypic analysis of gene replacementmutants Δtsp3 and Δtpl1 of M. grisea revealed a reduction of the pathogenicity only on rice, in contrast to Δpls1 mutants, which are completely non-pathogenic on barley and rice. Conclusion: A new tetraspanin family (Tsp3) and a tetraspanin-like protein family (Tpl1) have been identified in fungi. Functional analysis by gene replacement showed that these proteins, as well as Pls1, are involved in the infection process of the plant pathogenic fungus M. grisea. The next challenge will be to decipher the role(s) of tetraspanins in a range of symbiotic, saprophytic and human pathogenic fungi.
Ángel T. Martínez - One of the best experts on this subject based on the ideXlab platform.
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Biodeinking of flexographic inks by fungal laccases using synthetic and natural mediators
Biochemical Engineering Journal, 2012Co-Authors: Úrsula Fillat, Ángel T. Martínez, Alicia Prieto, Susana Camarero, María Jesús MartínezAbstract:Abstract The use of new printing technologies based on flexographic inks hampers ink elimination during paper recycling, making necessary the development of alternative methods. Decolorization of four flexographic inks has been evaluated by using fungal laccases, three of them from Basidiomycetes ( Trametes villosa , Coriolopsis rigida , and Pycnoporus coccineus ), and one from the ascomycete Myceliophthora thermophila in the presence of synthetic and natural mediators. The results obtained showed a higher capacity of the three basidiomycete laccases to decolorize flexographic inks as compared with M. thermophila laccase, a low redox potential laccase. Basidiomycete laccases decolorized inks without mediators at long reaction times, although the presence of natural or synthetic mediators (above all HBT) accelerated the process. On the other hand, M. thermophila laccase was unable to decolorize the inks assayed. The addition of syringyl-type mediators led to medium levels of decolorization except for R48 ink, which was almost completely decolorized. Most decolorization was obtained during the first hours of treatment, when all the basidiomycete laccases were fully active in the presence of mediators. As opposed to other basidiomycete laccases, which become inactive in the presence of HBT after 24 h, the enzyme of P. coccineus was not deactivated by this mediator even after 48 h. A complete loss of M. thermophila laccase activity was observed at short times with acetosyringone and methyl syringate, the only two mediators able to promote ink decolorization with this enzyme.
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identification of a novel series of alkylitaconic acids in wood cultures of ceriporiopsis subvermispora by gas chromatography mass spectrometry
Rapid Communications in Mass Spectrometry, 2002Co-Authors: José C. Del Río, Ana Gutiérrez, María Jesús Martínez, Ángel T. MartínezAbstract:A novel series of long-chain unsaturated dicarboxylic acids consisting of a long aliphatic chain attached to the C-3 position of itaconic acid has been identified by gas chromatography/mass spectrometry during in vitro decay of eucalypt wood by the white-rot basidiomycete Ceriporiopsis subvermispora. The major compounds were identified as tetradecyl-, 7-hexadecenyl- and hexadecylitaconic acids by their mass fragmentation patterns. Other members of the same compound series, identified as dodecanyl-, tridecanyl-, tetradecenyl-, pentadecanyl-, octadecenyl- and octadecanylitaconic acids, were present in very minor amounts or traces. Whereas hexadecenylitaconic acid has already been reported in cultures of C. subvermispora, to our knowledge this is the first report of the presence of the other alkylitaconic acids in fungal cultures. These new alkylitaconic-type metabolites may constitute a source for peroxidizable lipids involved in lignin degradation during wood decay by C. subvermispora and other white-rot Basidiomycetes.
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Identification of a novel series of alkylitaconic acids in wood cultures of Ceriporiopsis subvermispora by gas chromatography/mass spectrometry.
Rapid Communications in Mass Spectrometry, 2001Co-Authors: José C. Del Río, Ana Gutiérrez, María Jesús Martínez, Ángel T. MartínezAbstract:A novel series of long-chain unsaturated dicarboxylic acids consisting of a long aliphatic chain attached to the C-3 position of itaconic acid has been identified by gas chromatography/mass spectrometry during in vitro decay of eucalypt wood by the white-rot basidiomycete Ceriporiopsis subvermispora. The major compounds were identified as tetradecyl-, 7-hexadecenyl- and hexadecylitaconic acids by their mass fragmentation patterns. Other members of the same compound series, identified as dodecanyl-, tridecanyl-, tetradecenyl-, pentadecanyl-, octadecenyl- and octadecanylitaconic acids, were present in very minor amounts or traces. Whereas hexadecenylitaconic acid has already been reported in cultures of C. subvermispora, to our knowledge this is the first report of the presence of the other alkylitaconic acids in fungal cultures. These new alkylitaconic-type metabolites may constitute a source for peroxidizable lipids involved in lignin degradation during wood decay by C. subvermispora and other white-rot Basidiomycetes.
Barbara Howlett - One of the best experts on this subject based on the ideXlab platform.
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Fungi have three tetraspanin families with distinct functions
BMC Genomics, 2008Co-Authors: Karine Lambou, Catherine Sirven, Crystel Barbisan, Adrienne Sexton, Francis Martin, Melanie Marguerettaz, Annegret Kohler, Didier Tharreau, Ellen Kellner, Barbara HowlettAbstract:Background: Tetraspanins are small membrane proteins that belong to a superfamily encompassing 33 members in human and mouse. These proteins act as organizers of membrane-signalling complexes. So far only two tetraspanin families have been identified in fungi. These are Pls1, which is required for pathogenicity of the plant pathogenic ascomycetes, Magnaporthe grisea, Botrytis cinerea and Colletotrichum lindemuthianum, and Tsp2, whose function is unknown. In this report, we describe a third family of tetraspanins (Tsp3) and a new family of tetraspanin-like proteins (Tpl1) in fungi. We also describe expression of some of these genes in M. grisea and a basidiomycete, Laccaria bicolor, and also their functional analysis in M. grisea. Results: The exhaustive search for tetraspanins in fungal genomes reveals that higher fungi (Basidiomycetes and ascomycetes) contain three families of tetraspanins (Pls1, Tsp2 and Tsp3) with different distribution amongst phyla. Pls1 is found in ascomycetes and Basidiomycetes, whereas Tsp2 is restricted to Basidiomycetes and Tsp3 to ascomycetes. A unique copy of each of PLS1 and TSP3 was found in ascomycetes in contrast to TSP2, which has several paralogs in the Basidiomycetes, Coprinus cinereus and Laccaria bicolor. A tetraspanin-like family (Tpl1) was also identified in ascomycetes. Transcriptional analyses in various tissues of L. bicolor and M. grisea showed that PLS1 and TSP2 are expressed in all tissues in L. bicolor and that TSP3 and TPL1 are overexpressed in the sexual fruiting bodies (perithecia) and mycelia of M. grisea, suggesting that these genes are not pseudogenes. Phenotypic analysis of gene replacementmutants Δtsp3 and Δtpl1 of M. grisea revealed a reduction of the pathogenicity only on rice, in contrast to Δpls1 mutants, which are completely non-pathogenic on barley and rice. Conclusion: A new tetraspanin family (Tsp3) and a tetraspanin-like protein family (Tpl1) have been identified in fungi. Functional analysis by gene replacement showed that these proteins, as well as Pls1, are involved in the infection process of the plant pathogenic fungus M. grisea. The next challenge will be to decipher the role(s) of tetraspanins in a range of symbiotic, saprophytic and human pathogenic fungi.
Karine Lambou - One of the best experts on this subject based on the ideXlab platform.
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Fungi have three tetraspanin families with distinct functions
BMC Genomics, 2008Co-Authors: Karine Lambou, Catherine Sirven, Ellen M. Kellner, Crystel Barbisan, Adrienne Sexton, Francis Martin, Melanie Marguerettaz, Annegret Kohler, Didier Tharreau, Barbara J. HowlettAbstract:Tetraspanins are small membrane proteins that belong to a superfamily encompassing 33 members in human and mouse. These proteins act as organizers of membrane-signalling complexes. So far only two tetraspanin families have been identified in fungi. These are Pls1, which is required for pathogenicity of the plant pathogenic ascomycetes, Magnaporthe grisea, Botrytis cinerea and Colletotrichum lindemuthianum, and Tsp2, whose function is unknown. In this report, we describe a third family of tetraspanins (Tsp3) and a new family of tetraspanin-like proteins (Tpl1) in fungi. We also describe expression of some of these genes in M. grisea and a basidiomycete, Laccaria bicolor, and also their functional analysis in M. grisea. The exhaustive search for tetraspanins in fungal genomes reveals that higher fungi (Basidiomycetes and ascomycetes) contain three families of tetraspanins (Pls1, Tsp2 and Tsp3) with different distribution amongst phyla. Pls1 is found in ascomycetes and Basidiomycetes, whereas Tsp2 is restricted to Basidiomycetes and Tsp3 to ascomycetes. A unique copy of each of PLS1 and TSP3 was found in ascomycetes in contrast to TSP2, which has several paralogs in the Basidiomycetes, Coprinus cinereus and Laccaria bicolor. A tetraspanin-like family (Tpl1) was also identified in ascomycetes. Transcriptional analyses in various tissues of L. bicolor and M. grisea showed that PLS1 and TSP2 are expressed in all tissues in L. bicolor and that TSP3 and TPL1 are overexpressed in the sexual fruiting bodies (perithecia) and mycelia of M. grisea, suggesting that these genes are not pseudogenes. Phenotypic analysis of gene replacementmutants Δtsp3 and Δtpl1 of M. grisea revealed a reduction of the pathogenicity only on rice, in contrast to Δpls1 mutants, which are completely non-pathogenic on barley and rice. A new tetraspanin family (Tsp3) and a tetraspanin-like protein family (Tpl1) have been identified in fungi. Functional analysis by gene replacement showed that these proteins, as well as Pls1, are involved in the infection process of the plant pathogenic fungus M. grisea. The next challenge will be to decipher the role(s) of tetraspanins in a range of symbiotic, saprophytic and human pathogenic fungi.
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Fungi have three tetraspanin families with distinct functions
BMC Genomics, 2008Co-Authors: Karine Lambou, Catherine Sirven, Crystel Barbisan, Adrienne Sexton, Francis Martin, Melanie Marguerettaz, Annegret Kohler, Didier Tharreau, Ellen Kellner, Barbara HowlettAbstract:Background: Tetraspanins are small membrane proteins that belong to a superfamily encompassing 33 members in human and mouse. These proteins act as organizers of membrane-signalling complexes. So far only two tetraspanin families have been identified in fungi. These are Pls1, which is required for pathogenicity of the plant pathogenic ascomycetes, Magnaporthe grisea, Botrytis cinerea and Colletotrichum lindemuthianum, and Tsp2, whose function is unknown. In this report, we describe a third family of tetraspanins (Tsp3) and a new family of tetraspanin-like proteins (Tpl1) in fungi. We also describe expression of some of these genes in M. grisea and a basidiomycete, Laccaria bicolor, and also their functional analysis in M. grisea. Results: The exhaustive search for tetraspanins in fungal genomes reveals that higher fungi (Basidiomycetes and ascomycetes) contain three families of tetraspanins (Pls1, Tsp2 and Tsp3) with different distribution amongst phyla. Pls1 is found in ascomycetes and Basidiomycetes, whereas Tsp2 is restricted to Basidiomycetes and Tsp3 to ascomycetes. A unique copy of each of PLS1 and TSP3 was found in ascomycetes in contrast to TSP2, which has several paralogs in the Basidiomycetes, Coprinus cinereus and Laccaria bicolor. A tetraspanin-like family (Tpl1) was also identified in ascomycetes. Transcriptional analyses in various tissues of L. bicolor and M. grisea showed that PLS1 and TSP2 are expressed in all tissues in L. bicolor and that TSP3 and TPL1 are overexpressed in the sexual fruiting bodies (perithecia) and mycelia of M. grisea, suggesting that these genes are not pseudogenes. Phenotypic analysis of gene replacementmutants Δtsp3 and Δtpl1 of M. grisea revealed a reduction of the pathogenicity only on rice, in contrast to Δpls1 mutants, which are completely non-pathogenic on barley and rice. Conclusion: A new tetraspanin family (Tsp3) and a tetraspanin-like protein family (Tpl1) have been identified in fungi. Functional analysis by gene replacement showed that these proteins, as well as Pls1, are involved in the infection process of the plant pathogenic fungus M. grisea. The next challenge will be to decipher the role(s) of tetraspanins in a range of symbiotic, saprophytic and human pathogenic fungi.