In:
Environmental Microbiology, Wiley, Vol. 23, No. 3 ( 2021-03), p. 1594-1607
Abstract:
Secreted proteins are key players in fungal physiology and cell protection against external stressing agents and antifungals. Oak stress‐induced protein 1 (OSIP1) is a fungal‐specific protein with unknown function. By using Podospora anserina and Phanerochaete chrysosporium as models, we combined both in vivo functional approaches and biophysical characterization of OSIP1 recombinant protein. The P. anserina OSIP1 Δ mutant showed an increased sensitivity to the antifungal caspofungin compared to the wild type. This correlated with the production of a weakened extracellular exopolysaccharide/protein matrix (ECM). Since the recombinant OSIP1 from P. chrysosporium self‐assembled as fibers and was capable of gelation, it is likely that OSIP1 is linked to ECM formation that acts as a physical barrier preventing drug toxicity. Moreover, compared to the wild type, the OSIP1 Δ mutant was more sensitive to oak extractives including chaotropic phenols and benzenes. It exhibited a strongly modified secretome pattern and an increased production of proteins associated to the cell‐wall integrity signalling pathway, when grown on oak sawdust. This demonstrates that OSIP1 has also an important role in fungal resistance to extractive‐induced stress.
Type of Medium:
Online Resource
ISSN:
1462-2912
,
1462-2920
DOI:
10.1111/1462-2920.15381
Language:
English
Publisher:
Wiley
Publication Date:
2021
detail.hit.zdb_id:
2020213-1
SSG:
12
