Binding of C-reactive protein to Aspergillus fumigatus fractions

Jensen, Tine D. Børglum; Schønheyder, Henrik Carl; Andersen, Paul; Stenderup, A

doi:10.1099/00222615-21-2-173

Cited by 23 publications

(8 citation statements)

References 11 publications

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“…85,95–98 CRP also binds, in a Ca 2+ -dependent manner, to certain parasites such as Plasmodium falciparum, Hymenopepis diminuta , and Leishmania donovani through either PCh or carbohydrates on their surfaces. 99–102 Binding of CRP to L. donovani induces their developmental transformation.…”

Section: Short Pentraxins: Crp and Sapmentioning

confidence: 99%

Pattern Recognition by Pentraxins

Agrawal

Singh

Bottazzi

et al. 2009

Advances in Experimental Medicine and Biology

139

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Pentraxins are a family of evolutionarily conserved pattern-recognition proteins that are made up of five identical subunits. Based on the primary structure of the subunit, the pentraxins are divided into two groups: short pentraxins and long pentraxins. C-reactive protein (CRP) and serum amyloid P-component (SAP) are the two short pentraxins. The prototype protein of the long pentraxin group is pentraxin 3 (PTX3). CRP and SAP are produced primarily in the liver while PTX3 is produced in a variety of tissues during inflammation. The main functions of short pentraxins are to recognize a variety of pathogenic agents and then to either eliminate them or neutralize their harmful effects by utilizing the complement pathways and macrophages in the host. CRP binds to modified low-density lipoproteins, bacterial polysaccharides, apoptotic cells, and nuclear materials. By virtue of these recognition functions, CRP participates in the resolution of cardiovascular, infectious, and autoimmune diseases. SAP recognizes carbohydrates, nuclear substances, and amyloid fibrils and thus participates in the resolution of infectious diseases, autoimmunity, and amyloidosis. PTX3 interacts with several ligands, including growth factors, extracellular matrix component and selected pathogens, playing a role in complement activation and facilitating pathogen recognition by phagocytes. In addition, data in gene-targeted mice show that PTX3 is essential in female fertility, participating in the assembly of the cumulus oophorus extra-cellular matrix. PTX3 is therefore a nonredundant component of the humoral arm of innate immunity as well as a tuner of inflammation. Thus, in conjunction with the other components of innate immunity, the pentraxins use their pattern-recognition property for the benefit of the host.

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Section: Short Pentraxins: Crp and Sapmentioning

confidence: 99%

Pattern Recognition by Pentraxins

Agrawal

Singh

Bottazzi

et al. 2009

Advances in Experimental Medicine and Biology

139

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“…The binding of ‘C‐reactive substances’ of A. fumigatus in a Ca 2+ dependent fashion to C‐reactive protein (CRP) was described in 1971 by Pepys and Longbottom. The molecules involved were never isolated and it was suggested by Jensen [ 32] that the C‐reactive substances of A. fumigatus are heterogeneous. Phospholipids may be involved in the binding of A. fumigatus to CRP [ 33].…”

Section: Adhesion To Host Tissuesmentioning

confidence: 99%

Putative virulence factors of Aspergillus fumigatus

Tomee

Kauffman

2000

Clin Experimental Allergy

142

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Various putative virulence factors of Aspergillus fumigatus have been studied over the past decades. A. fumigatus gliotoxin is a potent inhibitor of the mucociliary system. Several fungal metabolites interfere with phagocytosis and opsonization including toxins, 'conidial inhibitory factor', 'A. fumigatus diffusible product' and 'complement inhibitory factor'. A. fumigatus can bind specifically to different host tissues components, whereas toxins give a general and significant immunosuppressive effect on host defences. Circumstantial evidence links the production of elastinolytic proteases with the ability to cause disease. However, none of the reports demonstrates conclusively a decisive role for any of the virulence factors described thus far. It is conceivable that proteolytic enzyme activities such as those expressed by AFAlp are one of a number of factors, each with a minor effect, that combine to facilitate disease progression.

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“…In particular, CRP has been shown to bind a panoply of microbes, including fungi, yeasts, bacteria, and parasites, mostly through phosphorylcholine and carbohydrate structures, and promote phagocytosis, thus supporting resistance to infections [105]. Noticeably, high levels of CRP have been reported in IA patients [106,107], and this pentraxin has been described to recognize yet unknown components of the hyphal cell wall of A. fumigatus [108] and promote phagocytosis of germinating (more than dormant) conidia by human neutrophils in vitro [109]. Also, SAP has been shown to localize in areas of hyphal dissemination in the lung parenchyma of IPA patients [110] and attenuate some traits (i.e., airway resistance to methacholine, inflammation, and tissue remodeling) of the chronic allergic airway disease in A. fumigatus-sensitized mice, possibly via modulation of the M2 polarization of macrophages [111].…”

Section: The Role Of Pentraxins In Aspergillus Fumigatus Infectionsmentioning

confidence: 99%

The complement system in Aspergillus fumigatus infections and its crosstalk with pentraxins

et al. 2020

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Aspergillosis is a life-threatening infection mostly affecting immunocompromised individuals and primarily caused by the saprophytic fungus Aspergillus fumigatus. At the host-pathogen interface, both cellular and humoral components of the innate immune system are increasingly acknowledged as essential players in the recognition and disposal of this opportunistic mold. Fundamental hereof is the contribution of the complement system, which deploys all three activation pathways in the battle against A. fumigatus, and functionally cooperates with other soluble pattern recognition molecules, including pentraxins. In particular, preclinical and clinical observations point to the long pentraxin PTX3 as a nonredundant and complement-dependent effector with protective functions against A. fumigatus.Based on past and current literature, here we discuss how the complement participates in the immune response to this fungal pathogen, and illustrate its crosstalk with the pentraxins, with a focus on PTX3. Emphasis is placed on the molecular mechanisms underlying such processes, the genetic evidence from human epidemiology, and the translational potential of the currently available knowledge.Aspergillus fumigatus is an evolutionary ancient filamentous fungus (mold) that flourishes in soil and decomposing vegetation [1]. Traditionally regarded as asexual, the life cycle of this ubiquitous saprophyte actually comprises cryptic forms of sexual reproduction [2] and is hallmarked by several morphotypes with distinct metabolic, compositional, and structural traits [3]. The metabolically inactive and asexual airborne spores (known as dormant or resting conidia) are encased in a robust cell wall mostly made of complex polysaccharides [i.e., aand b-glucans, chitin, galactomannan (GM), and galactosaminogalactan (GAG)] in addition to lipids, proteins, and melanin pigments [i.e., dihydroxynaphthalene (DHN) melanin] [4]. Small in size (i.e., 2-3 µm across) and enveloped in a layer of hydrophobic rodlet-like proteins (i.e.

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Binding of C-reactive protein to Aspergillus fumigatus fractions

Cited by 23 publications

References 11 publications

Pattern Recognition by Pentraxins

Pattern Recognition by Pentraxins

Putative virulence factors of Aspergillus fumigatus

The complement system in Aspergillus fumigatus infections and its crosstalk with pentraxins

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