High osmolarity glycerol response PtcB phosphatase is important for Aspergillus fumigatus virulence. Issue 1 (11th February 2015)
- Record Type:
- Journal Article
- Title:
- High osmolarity glycerol response PtcB phosphatase is important for Aspergillus fumigatus virulence. Issue 1 (11th February 2015)
- Main Title:
- High osmolarity glycerol response PtcB phosphatase is important for Aspergillus fumigatus virulence
- Authors:
- Winkelströter, Lizziane K.
Bom, Vinícius Leite Pedro
de Castro, Patrícia Alves
Ramalho, Leandra Naira Zambelli
Goldman, Maria Helena S.
Brown, Neil Andrew
Rajendran, Ranjith
Ramage, Gordon
Bovier, Elodie
dos Reis, Thaila Fernanda
Savoldi, Marcela
Hagiwara, Daisuke
Goldman, Gustavo H. - Abstract:
- Summary: A spergillus fumigatus is a fungal pathogen that is capable of adapting to different host niches and to avoid host defenses. An enhanced understanding of how, and which, A . fumigatus signal transduction pathways are engaged in the regulation of these processes is essential for the development of improved disease control strategies. Protein phosphatases are central to numerous signal transduction pathways. To comprehend the functions of protein phosphatases in A . fumigatus, 32 phosphatase catalytic subunit encoding genes were identified. We have recognized PtcB as one of the phosphatases involved in the high osmolarity glycerol response (HOG) pathway. The ΔptcB mutant has both increased phosphorylation of the p38 MAPK (SakA) and expression of osmo‐dependent genes. The ΔptcB strain was more sensitive to cell wall damaging agents, had increased chitin and β ‐1, 3‐glucan, and impaired biofilm formation. The ΔptcB strain was avirulent in a murine model of invasive pulmonary aspergillosis. These results stress the importance of the HOG pathway in the regulation of pathogenicity determinants and virulence in A . fumigatus . Abstract : Aspergillus fumigatus is a fungal pathogen that is capable of adapting to different host niches and avoiding host defenses. We have recognized PtcB as a protein phosphatase involved in the HOG (High Osmolarity Glycerol response) pathway. The ΔptcB mutant has both increased phosphorylation of the p38 MAPK (SakA) and expression ofSummary: A spergillus fumigatus is a fungal pathogen that is capable of adapting to different host niches and to avoid host defenses. An enhanced understanding of how, and which, A . fumigatus signal transduction pathways are engaged in the regulation of these processes is essential for the development of improved disease control strategies. Protein phosphatases are central to numerous signal transduction pathways. To comprehend the functions of protein phosphatases in A . fumigatus, 32 phosphatase catalytic subunit encoding genes were identified. We have recognized PtcB as one of the phosphatases involved in the high osmolarity glycerol response (HOG) pathway. The ΔptcB mutant has both increased phosphorylation of the p38 MAPK (SakA) and expression of osmo‐dependent genes. The ΔptcB strain was more sensitive to cell wall damaging agents, had increased chitin and β ‐1, 3‐glucan, and impaired biofilm formation. The ΔptcB strain was avirulent in a murine model of invasive pulmonary aspergillosis. These results stress the importance of the HOG pathway in the regulation of pathogenicity determinants and virulence in A . fumigatus . Abstract : Aspergillus fumigatus is a fungal pathogen that is capable of adapting to different host niches and avoiding host defenses. We have recognized PtcB as a protein phosphatase involved in the HOG (High Osmolarity Glycerol response) pathway. The ΔptcB mutant has both increased phosphorylation of the p38 MAPK (SakA) and expression of osmo‐dependent genes. The ΔptcB strain was avirulent in a murine model of invasive pulmonary aspergillosis, stressing the importance of the HOG pathway in the regulation of pathogenicity and virulence. … (more)
- Is Part Of:
- Molecular microbiology. Volume 96:Issue 1(2015)
- Journal:
- Molecular microbiology
- Issue:
- Volume 96:Issue 1(2015)
- Issue Display:
- Volume 96, Issue 1 (2015)
- Year:
- 2015
- Volume:
- 96
- Issue:
- 1
- Issue Sort Value:
- 2015-0096-0001-0000
- Page Start:
- 42
- Page End:
- 54
- Publication Date:
- 2015-02-11
- Subjects:
- Molecular microbiology -- Periodicals
572.829 - Journal URLs:
- http://www.blackwell-synergy.com/servlet/useragent?func=showIssues&code=mmi&close=2003#C2003 ↗
http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1365-2958 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/mmi.12919 ↗
- Languages:
- English
- ISSNs:
- 0950-382X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5900.817960
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 4545.xml