M-Ficolin Interacts with the Long Pentraxin PTX3: A Novel Case of Cross-Talk between Soluble Pattern-Recognition Molecules

Gout, Evelyne; Moriscot, Christine; Doni, Andrea; Dumestre-Pérard, Chantal; Lacroix, Monique; Pérard, Julien; Schoehn, Guy; Mantovani, Alberto; Arlaud, Gérard J.; Thielens, Nicole M.

doi:10.4049/jimmunol.1100180

Cited by 71 publications

(61 citation statements)

References 50 publications

(91 reference statements)

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“…Previously, we and others (29,30) have found that ficolin-1 interacts with PTX3. However, whether the ficolin-1-PTX3 interaction elicits biological effector functions has not been answered.…”

Section: Discussionmentioning

confidence: 99%

“…Recently, Gout et al (30) have suggested that the ficolin-1 binding site on PTX3 lies in the sialic acid moiety of the Cterminal pentraxin domain, based on SPR analysis. However, in contradiction to those findings, we report that ficolin-1 mainly (A, H), and also by double staining of annexin V and 7-aminoactinomycin D (7-AAD) (B, I).…”

Section: Discussionmentioning

confidence: 99%

“…It has been reported previously that the ficolin-1-PTX3 interaction might be dependent on the terminal sialic acid moiety of the PTX3 C-terminal pentraxin domain (30). To further clarify the effect of sialic acid moiety on the ficolin-1-PTX3 interaction, PTX3 was treated with C. perfringens type X neuraminidase, and the desialylation was analyzed by SDS-PAGE.…”

Section: Interaction Of Ficolin-1 and Ptx3 On Apoptotic Or Necrotic Cmentioning

confidence: 99%

“…We have previously shown that ficolin-1 may interact with PTX3 (29), and a potential binding unit on PTX3 was recently suggested to be sialylated glycosylation moieties at the C-terminal pentraxin domain of PTX3 (30). However, the potential physiological relevance of this interaction is at present unknown.…”

mentioning

confidence: 99%

“…Surface plasmon resonance (SPR) analysis of the PTX3-ficolin-1 interaction was performed using a BIAcore3000 instrument (GE Healthcare) and CM5 sensor chips (GE Healthcare) essentially as previously described (30), including immobilization of N-TD of PTX3 and full-length PTX3 by amine coupling at low pH (pH 3.5 and 2.5, respectively).…”

Section: Surface Plasmon Resonancementioning

confidence: 99%

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Ficolin-1–PTX3 Complex Formation Promotes Clearance of Altered Self-Cells and Modulates IL-8 Production

Jie

Doni

Romani

et al. 2013

The Journal of Immunology

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The long pentraxin 3 (PTX3) has been shown to be important in maintaining internal tissue homeostasis and in protecting against fungal Aspergillus fumigatus infection. However, the molecular mechanisms of how these functions are elicited are poorly delineated. Ficolin-1 is a soluble pattern recognition molecule that interacts with PTX3. We hypothesized that heterocomplexes between ficolin-1 and PTX3 might mediate the signals necessary for sequestration of altered self-cells and A. fumigatus. We were able to show that ficolin-1 interacts with PTX3 via its fibrinogen-like domain. The interaction was affected in a pH- and divalent cation–sensitive manner. The primary binding site for ficolin-1 on PTX3 was located in the N-terminal domain portion of PTX3. Ficolin-1 and PTX3 heterocomplex formation occurred on dying host cells, but not on A. fumigatus. The heterocomplex formation was a prerequisite for enhancement of phagocytosis by human monocyte–derived macrophages and downregulation of IL-8 production during phagocytosis. On A. fumigatus, PTX3 exposed the C-terminal portion of the molecule, probably resulting in steric hindrance of ficolin-1 interaction with PTX3. These results demonstrate that ficolin-1 and PTX3 heterocomplex formation acts as a noninflammatory “find me and eat me” signal to sequester altered-host cells. The fact that the ficolin-1–PTX3 complex formation did not occur on A. fumigatus shows that PTX3 uses different molecular effector mechanisms, depending on which domains it exposes during ligand interaction.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Interaction Of Ficolin-1 and Ptx3 On Apoptotic Or Necrotic Cmentioning

confidence: 99%

mentioning

confidence: 99%

Section: Surface Plasmon Resonancementioning

confidence: 99%

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Ficolin-1–PTX3 Complex Formation Promotes Clearance of Altered Self-Cells and Modulates IL-8 Production

Jie

Doni

Romani

et al. 2013

The Journal of Immunology

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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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Ficolins

Takahashi

Thiel

2013

Encyclopedia of Life Sciences

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Ficolins are innate immune pattern‐recognition molecules. The name of ficolin was derived from its basic structure, consisting of a collagen‐like domain and a fibrinogen‐like domain (FBG). The FBG preferably recognises acetylated compounds. Humans have three homologous proteins: H‐ficolin (or ficolin‐3), L‐ficolin (or ficolin‐2) and M‐ficolin (or ficolin‐1). Mice have ficolin‐A and ficolin‐B, which are homologous to L‐ficolin and M‐ficolin, respectively, whereas a murine homologue of H‐ficolin is absent. Ficolin genes are germinally present and, therefore, their proteins are expressed at healthy state and are circulating in blood or localised in organs, affording an instant host protection. Ficolins are homologous to collectins structurally and functionally but has a difference in target recognition. Ficolins, like collectins, play important roles in innate immunity as activators of the lectin pathway of the complement system. Key Concepts: Ficolins are molecules of innate immunity, which is the first line of host defence mechanism and is fully functional throughout the body and life regardless of health. Ficolins are similar to collectins in their structures and biologic functions with a major difference that target recognition is through fibrinogen‐like domain unlike carbohydrate recognition domain of collectins. Ficolins are pattern‐recognition molecules, which are able to identify invading pathogens and abnormal cells and tissues, in addition to normal cells, which are not recognised by collectins. Selected genetic mutations affect functions of ficolins and are associated with reduced host defence mechanisms. Some ficolins may be a disease modifier as deficiency itself may cause no problem, whereas it may have adverse effect depending on types of disease, infection or injury. Ficolins have structural and functional homology to collectins and may share and substitute functions in host defence.

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M-Ficolin Interacts with the Long Pentraxin PTX3: A Novel Case of Cross-Talk between Soluble Pattern-Recognition Molecules

Cited by 71 publications

References 50 publications

Ficolin-1–PTX3 Complex Formation Promotes Clearance of Altered Self-Cells and Modulates IL-8 Production

Ficolin-1–PTX3 Complex Formation Promotes Clearance of Altered Self-Cells and Modulates IL-8 Production

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

Ficolins

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