Putative Membrane Receptors Contribute to Activation and Efficient Signaling of Mitogen-Activated Protein Kinase Cascades during Adaptation of Aspergillus fumigatus to Different Stressors and Carbon Sources
Silva, LP; Frawley, D; Assis, LJD; et al.Tierney, C; Fleming, AB; Bayram, O; Goldman, GH
Date: 16 September 2020
Journal
mSphere
Publisher
American Society for Microbiology
Publisher DOI
Abstract
The high-osmolarity glycerol (HOG) response pathway is a multifunctional signal transduction pathway that specifically transmits ambient osmotic signals. Saccharomyces cerevisiae Hog1p has two upstream signaling branches, the sensor histidine kinase Sln1p and the receptor Sho1p. The Sho1p branch includes two
other proteins, the Msb2p ...
The high-osmolarity glycerol (HOG) response pathway is a multifunctional signal transduction pathway that specifically transmits ambient osmotic signals. Saccharomyces cerevisiae Hog1p has two upstream signaling branches, the sensor histidine kinase Sln1p and the receptor Sho1p. The Sho1p branch includes two
other proteins, the Msb2p mucin and Opy2p. Aspergillus fumigatus is the leading
cause of pulmonary fungal diseases. Here, we investigated the roles played by A. fumigatus SlnASln1p, ShoASho1p, MsbAMsb2p, and OpyAOpy2p putative homologues during the activation of the mitogen-activated protein kinase (MAPK) HOG pathway.
The shoA, msbA, and opyA singly and doubly null mutants are important for the cell
wall integrity (CWI) pathway, oxidative stress, and virulence as assessed by a Galleria
mellonella model. Genetic interactions of ShoA, MsbA, and OpyA are also important
for proper activation of the SakAHog1p and MpkASlt2 cascade and the response to osmotic and cell wall stresses. Comparative label-free quantitative proteomics analysis
of the singly null mutants with the wild-type strain upon caspofungin exposure indicates that the absence of ShoA, MsbA, and OpyA affects the osmotic stress response, carbohydrate metabolism, and protein degradation. The putative receptor
mutants showed altered trehalose and glycogen accumulation, suggesting a role for
ShoA, MsbA, and OpyA in sugar storage. Protein kinase A activity was also decreased in these mutants. We also observed genetic interactions between SlnA,
ShoA, MsbA, and OpyA, suggesting that both branches are important for activation
of the HOG/CWI pathways. Our results help in the understanding of the activation
and modulation of the HOG and CWI pathways in this important fungal pathogen.
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