Antifungal Activity of Mammalian Serum Amyloid A1 against
            <i>Candida albicans</i>

Gong, Jiao; Wu, Jun; Ikeh, Mélanie; Li, Tao; Jian, Bing; Nobile, Clarissa J.; Huang, Guanghua

doi:10.1128/aac.01975-19

Cited by 9 publications

(15 citation statements)

References 28 publications

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“…On the other hand, upon fungal infection, the host has a number of defense strategies, including secreting AMPs, "nutritional immunity," and producing antibodies through adaptive immunity to clear invading fungal pathogens (15). Mammalian SAA1 is a major acute-phase protein that has antimicrobial activity against both bacteria and fungi (5,7). In the present study, we set out to investigate the antifungal mechanism of human SAA1 against C. albicans.…”

Section: Discussionmentioning

confidence: 99%

“…We previously found that rhSAA1 binds to the cell surface of C. albicans and disrupts membrane integrity (7). Interestingly, unlike most membrane-disrupting AMPs, human SAA1 is hydrophilic and negatively charged (16), and native SAA1 often exists as a hexamer.…”

Section: Discussionmentioning

confidence: 99%

“…Als3 is a species-specific adhesin only found in C. albicans and its closely related species Candida dubliniensis. Perhaps due to the lack of an ortholog of Als3 in Candida glabrata, Candida parapsilosis, and S. cerevisiae, rhSAA1 exhibited no killing effect on cells of these fungi (7). Interestingly, Als3 contains a conservative amyloid-forming region (AFR; 325 to 331 amino acids [aa]) that is required for the formation of amyloid fibers and its aggregative function (11).…”

Section: Discussionmentioning

confidence: 99%

“…Recombinant expression and purification of human SAA1 in E. coli. The methods of recombinant expression and purification of human SAA1 in Escherichia coli were performed as described previously (7). Briefly, the expression plasmid pET28-hSAA1 was transformed into E. coli strain Rosetta (DE3).…”

Section: Methodsmentioning

confidence: 99%

“…Mouse intestinal epithelial and hepatic SAAs can act as modulators in the control of bacterial growth (5). In a recent study, we demonstrated that recombinant human and mouse SAA1 proteins (rhSAA1 and rmSAA1, respectively) exhibit potent antifungal activities against C. albicans (7). rhSAA1 targets the cell surface of C. albicans cells and impairs the integrity of the fungal cell membrane.…”

mentioning

confidence: 99%

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The Als3 Cell Wall Adhesin Plays a Critical Role in Human Serum Amyloid A1-Induced Cell Death and Aggregation in Candida albicans

Gong

Jian

Guan

et al. 2020

Antimicrob Agents Chemother

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Antimicrobial peptides and proteins play critical roles in the host defense against invading pathogens. We recently discovered that recombinantly expressed human and mouse serum amyloid A1 (rhSAA1 and rmSAA1, respectively) proteins have potent antifungal activities against the major human fungal pathogen Candida albicans. At high concentrations, rhSAA1 disrupts C. albicans membrane integrity and induces rapid fungal cell death. In the present study, we find that rhSAA1 promotes cell aggregation and targets the C. albicans cell wall adhesin Als3. Inactivation of ALS3 in C. albicans leads to a striking decrease in cell aggregation and cell death upon rhSAA1 treatment, suggesting that Als3 plays a critical role in SAA1 sensing. We further demonstrate that deletion of the transcriptional regulators controlling the expression of ALS3, such as AHR1, BCR1, and EFG1, in C. albicans results in similar effects to that of the als3/als3 mutant upon rhSAA1 treatment. Global gene expression profiling indicates that rhSAA1 has a discernible impact on the expression of cell wall- and metabolism-related genes, suggesting that rhSAA1 treatment could lead to a nutrient starvation effect on C. albicans cells.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

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The Als3 Cell Wall Adhesin Plays a Critical Role in Human Serum Amyloid A1-Induced Cell Death and Aggregation in Candida albicans

Gong

Jian

Guan

et al. 2020

Antimicrob Agents Chemother

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Structural and functional swapping of amyloidogenic and antimicrobial peptides: Redefining the role of amyloidogenic propensity in disease and host defense

Yadav

2021

Journal of Peptide Science

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Peptides constitute an essential component of all organisms' protein homeostasis ranging from bacteria, plants, and animals. They have organically been evolved to perform a wide range of essential functions, including their role as neurotransmitters, antimicrobial peptides (AMPs), and hormones. AMPs are short peptides synthesized by almost all organisms, implicated in guarding the host from various microbial infections. Their inherent ability to differentiate the target microbes from the host confers them excellent prospects in fighting against microbial infections and affirming their robust therapeutic potential against numerous drug-resistant microbes. Amyloidogenic peptides (AMYs) represent another class of short peptides armed with inherent aggregation propensity and form fibrillar aggregates rich in cross β-sheet structure. They are often involved in various degenerative diseases, including Alzheimer's disease (AD), Parkinson's disease (PD), and type-2 diabetes. Although these two distinct classes of peptides (i.e., AMPs and AMYs) appear to be functionally divergent, recent studies suggest that they possess a significant degree of structural and functional reciprocity. Consistent with this, many AMPs display amphiphilic nature, and hence, they can facilitate membrane remodeling processes, such as pore formation and fusion, similar to AMYs. The mounting evidence suggests the inherent ability of AMPs to self-assemble to form amyloid-like structures. On the other hand, the demonstration of antimicrobial properties of AMYs in their monomeric conformation provides a hint about the existence of an evolutionary linkage between these two classes of peptides. The congregation of specific amino acids to form aggregation-prone regions in a protein/peptide might have served as an evolutionary reservoir from which AMPs and AMYs were consecutively evolved. The current article reviews the fundamental features of the AMPs, AMYs, and their inter-relatedness and emerging paradigm for their inter-conversion.

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Enteric fungi protect against intestinal ischemia–reperfusion injury via inhibiting the SAA1-GSDMD pathway

Chen,

Han,

Guan

et al. 2024

Journal of Advanced Research

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Antifungal Activity of Mammalian Serum Amyloid A1 against Candida albicans

Cited by 9 publications

References 28 publications

The Als3 Cell Wall Adhesin Plays a Critical Role in Human Serum Amyloid A1-Induced Cell Death and Aggregation in Candida albicans

The Als3 Cell Wall Adhesin Plays a Critical Role in Human Serum Amyloid A1-Induced Cell Death and Aggregation in Candida albicans

Structural and functional swapping of amyloidogenic and antimicrobial peptides: Redefining the role of amyloidogenic propensity in disease and host defense

Enteric fungi protect against intestinal ischemia–reperfusion injury via inhibiting the SAA1-GSDMD pathway

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