New Features of Invasive Candidiasis in Humans: Amyloid Formation by Fungi and Deposition of Serum Amyloid P Component by the Host
Open accessAbstract
BACKGROUND: Invasive candidiasis occurs in the gastrointestinal tract, especially in neutropenic patients. We were interested in determining whether invasive fungi formed amyloid in humans as they are known to do in vitro. We also sought to characterize the consequence(s) of such amyloid formation. METHODS: Tissue from 25 autopsy patients with invasive candidiasis of the gastrointestinal tract was stained with amyloidophilic dyes and for the presence of serum amyloid P component (SAP). Confirmation of the interaction of SAP and Candida was demonstrated using Candida albicans and mutants for amyloid formation. RESULTS: Amyloid was present on the cellular surface of fungi invading gut tissue. Moreover, SAP bound to the fungal cell walls, confirming the presence of amyloid. In vitro observations showed SAP bound avidly to fungi when amyloid formed in fungal cell walls. An unexpected result was the lack of host neutrophils in response to the invading fungi, not only in neutropenic patients but also in patients with normal or increased white blood counts. CONCLUSIONS: We report the first demonstration of functional fungal amyloid in human tissue and the binding of SAP to invading fungi. It is postulated that fungal amyloid, SAP, or a complex of the proteins may inhibit the neutrophil response.
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CPHPC efficiently binds to SAP, leading to the dissociation of SAP from bound amyloids and subsequent depletion of SAP levels in the body.
“This compound efficiently binds to SAP, leading to the dissociation of SAP from bound amyloids and subsequent depletion of SAP levels in the body24,62–68.”
From Serum amyloid P secreted by bone marrow adipocytes drives skeletal amyloidosis (2025) · cites this paper as [66]
The Results and Discussion report SAP binding to fungal amyloid, but do not address CPHPC. Searches for CPHPC, SAP dissociation and SAP depletion found no passage describing the compound’s claimed effects. (LLM, conf=0.76)
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- Authors
- Gilchrist, K. B., Garcia, M. C., Sobonya, R., Lipke, P. N., & Klotz, S. A.
- Affiliations
- University of Arizona (US)
- City University of New York (US)
- Corresponding author
- Gilchrist, K. B.
- Venue
- Journal of Infectious Diseases
- Publisher
- Oxford University Press (OUP)
- Published
- 2012-07-16
- Volume
- 206
- Issue
- 9
- Pages
- 1473-1478
- ISSN
- 0022-1899 (ISSN-L)
- 1537-6613
- PMC
- PMC3570177
- OpenAlex
- W2123179985
- Cited by
- 41
- References
- 36
- Citations by year
- 2025: 5 · 2024: 1 · 2023: 1 · 2022: 3 · 2021: 2 · 2020: 5 · 2019: 2 · 2018: 2 · 2017: 3 · 2016: 4 · 2015: 3 · 2014: 6 · 2013: 4
- FWCI
- 2.88
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- The Journal of Infectious Diseases (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM098616, SC1GM083756)
- Topics
- Health Sciences › Medicine › Infectious Diseases › Antifungal resistance and susceptibility
- Health Sciences › Medicine › Epidemiology › Fungal Infections and Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Keywords
- invasive candidiasis, serum amyloid P component, Candida albicans, gastrointestinal infections, neutropenia, host-fungus interactions, fungal cell wall, neutrophil response, autopsy tissue
- MeSH terms
- Serum Amyloid P-Component, Candida albicans, Gastrointestinal Diseases, Histocytochemistry, Humans, Microscopy, Staining and Labeling, Plaque, Amyloid, Candidiasis, Invasive
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