Similar to other filamentous ascomycetes, one putative GPCR grouping to this class was identified in each of the three Trichoderma species. Whereas the respective proteins of both T. atroviride and T. reesei exhibit the typical structure with 7 transmembrane domains

and the long C-terminal tail, the T. virens homologue (Trive179509) only exhibits 6 transmembrane regions. PTH11-Related proteins of Trichoderma The PTH11 receptor was first identified in M. grisea, where it is required for host surface recognition and pathogenicity [37]. PTH11 has an extracellular amino-terminal CFEM domain followed by seven transmembrane regions and PTH11-related proteins are restricted to fungi belonging to the subphylum Pezizomycotina [14]. In both the mycoparasitic Trichoderma species as well as T. reesei[38, 39], the number PI3K inhibitors in clinical trials of identified PTH11-like proteins was higher than in the selleck inhibitor saprophyte N. crassa (25 members) but lower than in the plant pathogens M. grisea (61 members) and F. graminearum (106 members) [2, 14]. Similar {Selleck Anti-infection Compound Library|Selleck Antiinfection Compound Library|Selleck Anti-infection Compound Library|Selleck Antiinfection Compound Library|Selleckchem Anti-infection Compound Library|Selleckchem Antiinfection Compound Library|Selleckchem Anti-infection Compound Library|Selleckchem Antiinfection Compound Library|Anti-infection Compound Library|Antiinfection Compound Library|Anti-infection Compound Library|Antiinfection Compound Library|Anti-infection Compound Library|Antiinfection Compound Library|Anti-infection Compound Library|Antiinfection Compound Library|Anti-infection Compound Library|Antiinfection Compound Library|Anti-infection Compound Library|Antiinfection Compound Library|Anti-infection Compound Library|Antiinfection Compound Library|Anti-infection Compound Library|Antiinfection Compound Library|Anti-infection Compound Library|Antiinfection Compound Library|buy Anti-infection Compound Library|Anti-infection Compound Library ic50|Anti-infection Compound Library price|Anti-infection Compound Library cost|Anti-infection Compound Library solubility dmso|Anti-infection Compound Library purchase|Anti-infection Compound Library manufacturer|Anti-infection Compound Library research buy|Anti-infection Compound Library order|Anti-infection Compound Library mouse|Anti-infection Compound Library chemical structure|Anti-infection Compound Library mw|Anti-infection Compound Library molecular weight|Anti-infection Compound Library datasheet|Anti-infection Compound Library supplier|Anti-infection Compound Library in vitro|Anti-infection Compound Library cell line|Anti-infection Compound Library concentration|Anti-infection Compound Library nmr|Anti-infection Compound Library in vivo|Anti-infection Compound Library clinical trial|Anti-infection Compound Library cell assay|Anti-infection Compound Library screening|Anti-infection Compound Library high throughput|buy Antiinfection Compound Library|Antiinfection Compound Library ic50|Antiinfection Compound Library price|Antiinfection Compound Library cost|Antiinfection Compound Library solubility dmso|Antiinfection Compound Library purchase|Antiinfection Compound Library manufacturer|Antiinfection Compound Library research buy|Antiinfection Compound Library order|Antiinfection Compound Library chemical structure|Antiinfection Compound Library datasheet|Antiinfection Compound Library supplier|Antiinfection Compound Library in vitro|Antiinfection Compound Library cell line|Antiinfection Compound Library concentration|Antiinfection Compound Library clinical trial|Antiinfection Compound Library cell assay|Antiinfection Compound Library screening|Antiinfection Compound Library high throughput|Anti-infection Compound high throughput screening| to the above mentioned fungi, only a subset of the identified Trichoderma proteins contained the fungal-specific cysteine-rich CFEM (pfam05730) domain (Figure 5, Additional file 2), which is characteristically present in the extracellular region of some membrane proteins with

proposed roles in fungal pathogenicity. Compared to T. atroviride (38 members) and T. reesei (35 members), we found a marked expansion of PTH11-related proteins in T. virens (52 members). Figure 5 Neighbor-joining tree of PTH11-related proteins identified in the genomes of the three Trichoderma species. The clade containing proteins with a CFEM domain is marked with a black line. Nodes supported with bootstrap values above 70% (1000 repetitions) are indicated with a black dot, nodes with bootstrap values between 50 -70% are indicated with a grey dot, bootstrap values

less than 50% were removed. Additional putative GPCRs of Trichoderma which are beyond the existing classification system of fungal GPCRs (class XIII) Recently, a putative GPCR of Phytophtora sojae (GPR11) controlling zoospore development and virulence of P. sojae to soybean has been described HA-1077 [35]. Performing a BLASTP search with GPR11 as a query against the proteomes of T. atroviride, T. virens, T. reesei, and those of N. crassa, M. grisea, and A. fumigatus revealed respective orthologues in all fungi tested. Whereas in T. atroviride three proteins were identified (Table 1), T. reesei and T. virens as well as the other ascomycetes possess two members each. All putative Trichoderma GPCRs identified this way have a DUF300 domain (domain of unknown function, pfam03619). Such a domain is also present in e.g. the class A GPCRs Cand9 and Cand10 of Arabidopsis thaliana[61] and P. sojae GPR11.