(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Eukaryota: NE > Opisthokonta: NE > Fungi: NE > Dikarya: NE > Ascomycota: NE > saccharomyceta: NE > Pezizomycotina: NE > leotiomyceta: NE > Eurotiomycetes: NE > Eurotiomycetidae: NE > Onygenales: NE > Arthrodermataceae: NE > Trichophyton: NE > Trichophyton rubrum: NE
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acide identity. You can retrieve all strain data
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) Trichophyton rubrum MR850: N, E.
Trichophyton rubrum CBS 288.86: N, E.
Trichophyton rubrum CBS 118892: N, E.
Trichophyton rubrum MR1448: N, E.
Trichophyton rubrum MR1459: N, E.
Trichophyton rubrum CBS 289.86: N, E.
Trichophyton rubrum D6: N, E.
Trichophyton rubrum CBS 202.88: N, E.
Trichophyton rubrum CBS 100081: N, E.
Trichophyton rubrum CBS 735.88: N, E.
Arthroderma benhamiae CBS 112371: N, E.
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MAAAKWLIASLAFASSGLAFTPEDFISAPRRGEAIPDPKGELAVFHVSKY NFDKKDRPSGWNLLNLKNGDINVLTTDSDVSEITWLGDGTKVVYINGTDS VKGGVGIWISDAKNFGNAYKAGSVNGAFSGLKLAKSGDKINFVGYGQSTT KGDLYNEAAAKEAVSSARIYDSLFVRHWDTYVGTQFNAVFSGTLTKSGDK YSFDGKLKNLVQPVKYAESPYPPFGGSGDYDLSSDGKTVAFMSKAPELPK ANLTTSYIFLVPHDGSRVAEPINKRNGPRTPQGIEGASSSPVFSPDGKRI AYLQMAAKNYESDRRVIHIAEVGTNKPVQRIASNWDRSPEAVKWSSDGRT LYVTAEDHATGKLFTLPADARDNHKPAVVKHDGSVSSFYFIGSSKSVLIS GNSLWSNALYQVATPDRPNRKLFYANEHDPELKGLGPNDIEPLWVDGART KIHSWIVKPTGFDKNKVYPLAFLIHGGPQGSWGDNWSTRWNPRVWADQGY VVVAPNPTGSTGFGQKLTDDITNDWGGAPYKDLVKIWEHVHDHIKYIDTD NGIAAGASFGGFMVNWIQGQDLGRKFKALVSHDGTFVGSSKIGTDELFFI EHDFNGTFFEARQNYDRWDCSKPELVAKWSTPQLVVHNDFDFRLSVAEGV GLFNVLQEKGVPSRFLNFPDETHWVTKPENSLVWHQQVLGWVNKWSGINK SNPKSIKLSDCPIEVVDHEAHSYFDY
The nature of secreted aminopeptidases in Trichophyton rubrum was investigated by using a reverse genetic approach. T. rubrum genomic and cDNA libraries were screened with Aspergillus spp. and Saccharomyces cerevisiae aminopeptidase genes as the probes. Two leucine aminopeptidases, ruLap1 and ruLap2, and two dipeptidyl-peptidases, ruDppIV and ruDppV, were characterized and compared to orthologues secreted by Aspergillus fumigatus using a recombinant protein from Pichia pastoris. RuLap1 is a 33 kDa nonglycosylated protein, while ruLap2 is a 58-65 kDa glycoprotein. The hydrolytic activity of ruLap1, ruLap2 and A. fumigatus orthologues showed various preferences for different aminoacyl-7-amido-4-methylcoumarin substrates, and various sensitivities to inhibitors and cations. ruDppIV and ruDppV showed similar activities to A. fumigatus orthologues. In addition to endopeptidases, the four aminopeptidases ruLap1, ruLap2, ruDppIV and ruDppV were produced by T. rubrum in a medium containing keratin as the sole nitrogen source. Synergism between endo- and exopeptidases is likely to be essential for dermatophyte virulence, since these fungi grow only in keratinized tissues.
Title: Cloning and characterization of Trichophyton rubrum genes encoding actin, Tri r2, and Tri r4 Gao J, Takashima A Ref: J Clin Microbiol, 42:3298, 2004 : PubMed
The three structural genes of Trichophyton rubrum encoding actin (3,429 bp) and two antigens, Tri r2 (2,950 bp) and Tri r4 (3,988 bp), were cloned and characterized. They contained six, four, and five exons, respectively. The T. rubrum actin protein sequence revealed extremely high homology to other fungal actins.
Title: Trichophyton antigens associated with IgE antibodies and delayed type hypersensitivity. Sequence homology to two families of serine proteinases Woodfolk JA, Wheatley LM, Piyasena RV, Benjamin DC, Platts-Mills TA Ref: Journal of Biological Chemistry, 273:29489, 1998 : PubMed
The dermatophyte fungus Trichophyton exhibits unique immunologic properties by its ability to cause both immediate and delayed type hypersensitivity. An 83-kDa Trichophyton tonsurans allergen (Tri t 4) was previously shown to elicit distinct T lymphocyte cytokine profiles in vitro. The homologous protein, Tri r 4, was cloned from a Trichophyton rubrum cDNA library, and the recombinant protein was expressed in Pichia pastoris. This 726-amino acid protein contained an arrangement of catalytic triad residues characteristic of the prolyl oligopeptidase family of serine proteinases (Ser-Asp-His). In addition, a novel Trichophyton allergen, encoding 412 amino acids, was identified by its human IgE antibody-binding activity. Sequence similarity searches showed that this allergen, designated Tri r 2, contained all of the conserved residues characteristic of the class D subtilase subfamily (41-58% overall sequence identity). Forty-two percent of subjects with immediate hypersensitivity skin test reactions to a Trichophyton extract exhibited IgE antibody binding to a recombinant glutathione S-transferase fusion protein containing the carboxyl-terminal 289 amino acids of Tri r 2. Furthermore, this antigen was capable of inducing delayed type hypersensitivity skin test reactions. Our results define two distinct antigens derived from the dermatophyte Trichophyton that serve as targets for diverse immune responses in humans.
