Serum Amyloid P Component and Systemic Fungal Infection: Does It Protect the Host or Is It a Trojan Horse?

Klotz, Stephen A.; Sobonya, Richard E.; Lipke, Peter N.; Garcia-Sherman, Melissa C.

doi:10.1093/ofid/ofw166

Cited by 21 publications

(18 citation statements)

References 20 publications

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“…One of these is serum amyloid component P (SAP). SAP can bind Candida albicans (Klotz et al, 2016 ) in the similar way Aβ binds to bacteria in its antimicrobial peptide capacity (Soscia et al, 2010 ; Kumar et al, 2016 ). This implies that amyloid-like proteins (Table 1 ) from foreign and host sources undergo physical protein-protein interactions with potential to cross-seed with Aβ, and increase the amyloid burden.…”

Section: Functional Amyloids From Prokaryotic Originsmentioning

confidence: 99%

“…C. albicans infection can be asymptomatic and is difficult to eradicate. The concept of trapping/incapacitating and killing bacteria in the brain by Aβ antimicrobial activity (Soscia et al, 2010 ; Kumar et al, 2016 ) perhaps equally applies to SAP mediated trapping of C. albicans systemically (Klotz et al, 2016 ). However, this affinity could also be due to the amyloid-like adhesion on the surface of C. albicans (Ramsook et al, 2010 ; Garcia et al, 2013 ).…”

Section: Senile Plaque a Miniature Biofilm Hypothesismentioning

confidence: 99%

“…However, this affinity could also be due to the amyloid-like adhesion on the surface of C. albicans (Ramsook et al, 2010 ; Garcia et al, 2013 ). If the senile plaques represent foci of miniature biofilms, then C. albicans may be responsible for adding to the Aβ burden by bringing its own Als (Ramsook et al, 2010 ; Garcia et al, 2013 ) and the insoluble SAP from its primary niche (Ramsook et al, 2010 ; Klotz et al, 2016 ). As human brain Aβ and bacterial LPS are resistant to degradation, their accumulation is to be expected.…”

Section: Senile Plaque a Miniature Biofilm Hypothesismentioning

confidence: 99%

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Periodontitis, Microbiomes and their Role in Alzheimer’s Disease

Pritchard

Crean

Olsen

et al. 2017

Front. Aging Neurosci.

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As far back as the eighteenth and early nineteenth centuries, microbial infections were responsible for vast numbers of deaths. The trend reversed with the introduction of antibiotics coinciding with longer life. Increased life expectancy however, accompanied the emergence of age related chronic inflammatory states including the sporadic form of Alzheimer’s disease (AD). Taken together, the true challenge of retaining health into later years of life now appears to lie in delaying and/or preventing the progression of chronic inflammatory diseases, through identifying and influencing modifiable risk factors. Diverse pathogens, including periodontal bacteria have been associated with AD brains. Amyloid-beta (Aβ) hallmark protein of AD may be a consequence of infection, called upon due to its antimicrobial properties. Up to this moment in time, a lack of understanding and knowledge of a microbiome associated with AD brain has ensured that the role pathogens may play in this neurodegenerative disease remains unresolved. The oral microbiome embraces a range of diverse bacterial phylotypes, which especially in vulnerable individuals, will excite and perpetuate a range of inflammatory conditions, to a wide range of extra-oral body tissues and organs specific to their developing pathophysiology, including the brain. This offers the tantalizing opportunity that by controlling the oral-specific microbiome; clinicians may treat or prevent a range of chronic inflammatory diseases orally. Evolution has equipped the human host to combat infection/disease by providing an immune system, but Porphyromonas gingivalis and selective spirochetes, have developed immune avoidance strategies threatening the host-microbe homeostasis. It is clear from longitudinal monitoring of patients that chronic periodontitis contributes to declining cognition. The aim here is to discuss the contribution from opportunistic pathogens of the periodontal microbiome, and highlight the challenges, the host faces, when dealing with unresolvable oral infections that may lead to clinical manifestations that are characteristic for AD.

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Section: Functional Amyloids From Prokaryotic Originsmentioning

confidence: 99%

Section: Senile Plaque a Miniature Biofilm Hypothesismentioning

confidence: 99%

Section: Senile Plaque a Miniature Biofilm Hypothesismentioning

confidence: 99%

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Periodontitis, Microbiomes and their Role in Alzheimer’s Disease

Pritchard

Crean

Olsen

et al. 2017

Front. Aging Neurosci.

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“…SAP binds to many microbes including parasites, bacteria, viruses, and fungi and this binding may be explained by the presence of functional amyloid on the surface of the microbes [ 12 ]. These SAP-coated microbes may dampen the immune response to infection [ 13 ].…”

Section: Discussionmentioning

confidence: 99%

“…No binding was detected for CRP or PTX3 to fungal surfaces. The presence of SAP on the fungi in the tissue may have an effect upon the host response to the infection [ 13 ].…”

Section: Discussionmentioning

confidence: 99%

Do Pentraxins Bind to Fungi in Invasive Human Gastrointestinal Candidiasis?

Golconda

Sobonya

Klotz

2018

JoF

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Tissue from 13 autopsy cases with invasive gastrointestinal candidiasis was studied for the binding of the pentraxins, C-reactive protein (CRP), pentraxin 3 (PTX3), and serum amyloid P component (SAP) to fungal surfaces. Invasive candidal infection was demonstrated using a hematoxylin and eosin stain and a Gomori methenamine silver stain (GMS). Immunohistochemistry was performed with CRP and PTX3 monoclonal antibodies and did not demonstrate CRP or PTX3 bound to fungi (0 of 13 cases), although CRP was extensively deposited on human tissue. A polyclonal antibody to SAP showed that SAP was bound to fungi in 12 of 13 cases. Although all three pentraxins have been reported to bind to fungi or bacteria, only SAP was bound to filamentous and yeast forms of Candida in human tissue, as detected by immunohistochemistry. SAP was abundantly present on fungi and may have affected the host innate immune response to the invading fungi.

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Human serum proteins bind to Sporothrix schenckii conidia with differential effects on phagocytosis

et al. 2020

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Serum is an important source of proteins that interact with pathogens. Once bound to the cell surface, serum proteins can stimulate the innate immune system. The phagocytosis of Sporothrix schenckii conidia by human macrophages is activated through human serum opsonisation. In this study, we have attempted to characterise human blood serum proteins that bind to the cell wall of S. schenckii conidia. We systematically observed the same four proteins independent of the plasma donor: albumin, serum amyloid protein (SAP), α-1 antitrypsin (AAT), and transferrin were identified with the help of tandem mass spectrometry. Phagocytosis depended on the concentration of the SAP or α-1 antitrypsin that was used to opsonise the conidia; however, transferrin or albumin did not have any effect on conidia internalisation. The presence of mannose did not affect macrophage phagocytosis of the conidia opsonised with SAP or α-1 antitrypsin, which suggests that these proteins are not recognised by the mannose receptor.

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Serum Amyloid P Component and Systemic Fungal Infection: Does It Protect the Host or Is It a Trojan Horse?

Cited by 21 publications

References 20 publications

Periodontitis, Microbiomes and their Role in Alzheimer’s Disease

Periodontitis, Microbiomes and their Role in Alzheimer’s Disease

Do Pentraxins Bind to Fungi in Invasive Human Gastrointestinal Candidiasis?

Human serum proteins bind to Sporothrix schenckii conidia with differential effects on phagocytosis

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