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Systematic Global Analysis of Genes Encoding Protein Phosphatases in Aspergillus fumigatus.

Winkelströter LK, Dolan SK, Fernanda Dos Reis T, Bom VL, Alves de Castro P, Hagiwara D, Alowni R, Jones GW, Doyle S, Brown NA, Goldman GH - G3 (Bethesda) (2015)

Bottom Line: We identified 32 phosphatase catalytic subunit-encoding genes in A. fumigatus, of which we were able to construct 24 viable deletion mutants.We were also able to identify 11 phosphatases involved in iron assimilation, six that are related to gliotoxin resistance, and three implicated in gliotoxin production.These results present the creation of a fundamental resource for the study of signaling in A. fumigatus and its implications in the regulation of pathogenicity determinants and virulence in this important pathogen.

View Article: PubMed Central - PubMed

Affiliation: Faculdade de Ciências Farmacêuticas de Ribeirão Preto, Universidade de São Paulo, 13083-970 Ribeirão Preto, Brazil.

No MeSH data available.


Related in: MedlinePlus

Ferricrocin (FC) production in the wild-type and phosphatase  mutants that have increased growth during iron excess. The bars represent the integration areas of the FC peaks identified from culture supernatants analyzed by RP-HPLC (reverse-phase high-performance liquid chromatography). The asterisks indicate statistical analysis using unpaired t-test (*P < 0.05 and **P < 0.01 when compared to the wild-type strain).
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fig8: Ferricrocin (FC) production in the wild-type and phosphatase mutants that have increased growth during iron excess. The bars represent the integration areas of the FC peaks identified from culture supernatants analyzed by RP-HPLC (reverse-phase high-performance liquid chromatography). The asterisks indicate statistical analysis using unpaired t-test (*P < 0.05 and **P < 0.01 when compared to the wild-type strain).

Mentions: Growth of the 24 mutants was compared to the wild-type strain in the following conditions: (1) different temperatures (30°, 37°, and 44°); (2) in media of different nutritional states [complete media (YAG), minimal media (MM), and fetal bovine serum (FBS)]; (3) during calcium starvation [ethylene glycol tetraacetic acid (EGTA)]; (4) for sensitivity to manganese chloride (MnCl2); (5) sodium dodecyl sulfate (SDS); (6) oxidative stress (t-butyl peroxide, menadione, and paraquat); (7) osmotic stress (NaCl and sorbitol); (8) cell wall–damaging agents [Congo Red (CR) and Calcofluor White (CFW)]; (9) unfolded protein response (UPR) [dithiotreitol (DTT)]; (10) GEL inhibition; (11) iron assimilation; and (12) gliotoxin production/sensitivity (Table 2, Figure 2, Figure 3, Figure 4, Figure 5, Figure 6, Figure 7, Figure 8, Figure 9, Figure 10). No dramatic differences in growth for the phosphatase mutants were observed in comparison to the wild-type strain (Table 2 and Figure S3), except for the ΔptcF and ΔptcG mutants that had reduced growth at 44° (Table 2 and Figure S3). In addition, the ΔppzA, ΔnemA, and ΔdspD mutants had reduced conidiation at 44° (Table 2 and Figure S3).


Systematic Global Analysis of Genes Encoding Protein Phosphatases in Aspergillus fumigatus.

Winkelströter LK, Dolan SK, Fernanda Dos Reis T, Bom VL, Alves de Castro P, Hagiwara D, Alowni R, Jones GW, Doyle S, Brown NA, Goldman GH - G3 (Bethesda) (2015)

Ferricrocin (FC) production in the wild-type and phosphatase  mutants that have increased growth during iron excess. The bars represent the integration areas of the FC peaks identified from culture supernatants analyzed by RP-HPLC (reverse-phase high-performance liquid chromatography). The asterisks indicate statistical analysis using unpaired t-test (*P < 0.05 and **P < 0.01 when compared to the wild-type strain).
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4502386&req=5

fig8: Ferricrocin (FC) production in the wild-type and phosphatase mutants that have increased growth during iron excess. The bars represent the integration areas of the FC peaks identified from culture supernatants analyzed by RP-HPLC (reverse-phase high-performance liquid chromatography). The asterisks indicate statistical analysis using unpaired t-test (*P < 0.05 and **P < 0.01 when compared to the wild-type strain).
Mentions: Growth of the 24 mutants was compared to the wild-type strain in the following conditions: (1) different temperatures (30°, 37°, and 44°); (2) in media of different nutritional states [complete media (YAG), minimal media (MM), and fetal bovine serum (FBS)]; (3) during calcium starvation [ethylene glycol tetraacetic acid (EGTA)]; (4) for sensitivity to manganese chloride (MnCl2); (5) sodium dodecyl sulfate (SDS); (6) oxidative stress (t-butyl peroxide, menadione, and paraquat); (7) osmotic stress (NaCl and sorbitol); (8) cell wall–damaging agents [Congo Red (CR) and Calcofluor White (CFW)]; (9) unfolded protein response (UPR) [dithiotreitol (DTT)]; (10) GEL inhibition; (11) iron assimilation; and (12) gliotoxin production/sensitivity (Table 2, Figure 2, Figure 3, Figure 4, Figure 5, Figure 6, Figure 7, Figure 8, Figure 9, Figure 10). No dramatic differences in growth for the phosphatase mutants were observed in comparison to the wild-type strain (Table 2 and Figure S3), except for the ΔptcF and ΔptcG mutants that had reduced growth at 44° (Table 2 and Figure S3). In addition, the ΔppzA, ΔnemA, and ΔdspD mutants had reduced conidiation at 44° (Table 2 and Figure S3).

Bottom Line: We identified 32 phosphatase catalytic subunit-encoding genes in A. fumigatus, of which we were able to construct 24 viable deletion mutants.We were also able to identify 11 phosphatases involved in iron assimilation, six that are related to gliotoxin resistance, and three implicated in gliotoxin production.These results present the creation of a fundamental resource for the study of signaling in A. fumigatus and its implications in the regulation of pathogenicity determinants and virulence in this important pathogen.

View Article: PubMed Central - PubMed

Affiliation: Faculdade de Ciências Farmacêuticas de Ribeirão Preto, Universidade de São Paulo, 13083-970 Ribeirão Preto, Brazil.

No MeSH data available.


Related in: MedlinePlus