Cited by 35Endoplasmic Reticulum Stress and DiseaseFungal and yeast genetics researchAntifungal resistance and susceptibility

The fungal UPR: A regulatory hub for virulence traits in the mold pathogen Aspergillus fumigatus

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Krishnan, Karthik, Askew, David S·2014·Virulence

Abstract

Aspergillus fumigatus is an opportunistic pathogen that is responsible for a life-threatening fungal infection known as invasive aspergillosis. Current therapies for the treatment of this disease continue to be associated with a poor outcome, so there is a need for more information about aspects of the fungus-host interaction that could offer novel targets for drug intervention. One attractive possibility is the unfolded protein response (UPR), an intracellular signaling network that helps the fungus meet the demand for secretion in the host environment. The major function of the UPR is to mitigate ER stress by maintaining an equilibrium between the load of client proteins entering the endoplasmic reticulum (ER) and the protein folding capacity of the organelle. However, recent findings suggest that A. fumigatus, as well as several other pathogenic fungi, also rely upon this pathway for virulence. In this review, we provide an update on the A. fumigatus UPR, discuss emerging evidence that the UPR is situated at the nexus of a number of physiological functions that are vital for the virulence of this fungus, and suggest exciting possibilities for future therapeutic targeting of this pathway for the treatment of aspergillosis.

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  • The secretion capacity of Aspergillus species must be regulated to avoid the accumulation of toxic unfolded proteins when the organism encounters adverse environmental conditions.

    “their secretion capacity, which is vital for the fungus, must be regulated to avoid the accumulation of toxic unfolded proteins when the organism encounters adverse environmental conditions (602).”

    From Aspergillus fumigatus and Aspergillosis in 2019 (2019) · cites this paper as [602]

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Authors
Krishnan, K., & Askew, D. S.
Affiliations
University of Cincinnati (US)
Corresponding author
Askew, David S
Venue
Virulence
Published
2013-10-18
Volume
5
Issue
2
Pages
334-340
ISSN
  • 2150-5594 (ISSN-L)
  • 2150-5608
OpenAlex
W2022496663
Cited by
35
References
60
Citations by year
2026: 1 · 2025: 2 · 2024: 4 · 2023: 5 · 2022: 1 · 2021: 2 · 2020: 5 · 2019: 3 · 2017: 1 · 2016: 3 · 2015: 4 · 2014: 4
FWCI
0.42
Type
journal article
Language
en
Open access
Licence
cc-by-nc
Locations
  • Virulence (publishedVersion, cc-by-nc)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by-nc)
  • PubMed Central (publishedVersion, cc-by-nc)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health (UL1TR000077)
  • National Institute of Allergy and Infectious Diseases (R01AI072297)
  • National Center for Advancing Translational Sciences
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
  • Health Sciences › Medicine › Infectious Diseases › Antifungal resistance and susceptibility
Keywords
unfolded protein response, Aspergillus fumigatus, invasive aspergillosis, endoplasmic reticulum stress, fungal virulence, host-pathogen interaction, antifungal drug targets, protein secretion, endoplasmic reticulum protein folding
MeSH terms
Aspergillus fumigatus, Humans, Stress, Physiological, Virulence, Host-Pathogen Interactions, Unfolded Protein Response

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