M‐ficolin is expressed on monocytes and is a lectin binding to <i>N</i>‐acetyl‐					<scp>d</scp>‐glucosamine and mediates monocyte adhesion and phagocytosis of <i>Escherichia coli</i>

Teh, Cathleen; Le, Yevgeniya; Lee, S H; Lu, Jinhua

doi:10.1046/j.1365-2567.2000.00099.x

Cited by 143 publications

(134 citation statements)

References 25 publications

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“…This also means that the surfaces of some pathogens can induce the formation of the active conformation of the FBG domains and thereby increase the avidity for the surface. Indeed, the binding specificity for various bacteria differs among ficolins (9,20,22,29,32,45). Such surface-dependent conformational changes would facilitate the discrimination between self and non-self.…”

Section: Discussionmentioning

confidence: 99%

“…Since the corresponding residues of the ligandbinding site in H-ficolin differ from those in L-ficolin, Mficolin, and TL5A, its manner of ligand binding may differ. These differences would contribute to the range of pathogen recognition specificity (9,20,22,29,32,45).…”

Section: Discussionmentioning

confidence: 99%

“…Ficolins, as well as collectins, are one of the most important groups of pattern recognition molecules in the innate immunity systems (1-7) and have been identified in both vertebrates and invertebrates (6). Ficolins are comprised of a collagen-like domain at the N terminus and a fibrinogen-like domain (FBG), 3 which is the sugar-binding site, at the C terminus (8,9). Collectins, such as mannose-binding lectin (MBL), lung surfactant protein A, and surfactant protein D, also consist of an N-terminal collagen-like domain and a C-terminal carbohydrate-recognition domain (CRD) that binds to certain carbohydrates such as mannose and GlcNAc Ca 2ϩ dependently.…”

mentioning

confidence: 99%

“…M-ficolin (synonymous with ficolin-1 or Ficolin/ P35-related protein) has a primary sequence that is 80 and 48% identical to those of L-ficolin and H-ficolin, respectively (14,28). M-ficolin binds to GlcNAc, GalNAc, and sialic acid (9,22), and like L-ficolin, it recognizes acetyl groups (23). Unlike the serum ficolins, M-ficolin has been detected on the surfaces of peripheral blood monocytes and promonocytic U937 cells (9,23,27) and in secretory granules in the cytoplasm of neutrophils, monocytes, and type II alveolar epithelial cells in the lung (22).…”

mentioning

confidence: 99%

“…M-ficolin binds to GlcNAc, GalNAc, and sialic acid (9,22), and like L-ficolin, it recognizes acetyl groups (23). Unlike the serum ficolins, M-ficolin has been detected on the surfaces of peripheral blood monocytes and promonocytic U937 cells (9,23,27) and in secretory granules in the cytoplasm of neutrophils, monocytes, and type II alveolar epithelial cells in the lung (22). An antibody against the recombinant FBG domain of M-ficolin inhibits the phagocytosis of E. coli by U937 cell, suggesting that M-ficolin acts as a monocyte phagocytic receptor or adaptor for recognizing pathogens (9).…”

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Trivalent Recognition Unit of Innate Immunity System

Tanio

Kondo

Sugio

et al. 2007

Journal of Biological Chemistry

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Ficolins are a kind of pathogen-recognition molecule in the innate immune systems. To investigate the discrimination mechanism between self and non-self by ficolins, we determined the crystal structure of the human M-ficolin fibrinogen-like domain (FD1), which is the ligand-binding domain, at 1.9 Å resolution. Although the FD1 monomer shares a common fold with the fibrinogen ␥ fragment and tachylectin-5A, the Asp-282-Cys-283 peptide bond, which is the predicted ligand-binding site on the C-terminal P domain, is a normal trans bond, unlike the cases of the other two proteins. The trimeric formation of FD1 results in the separation of the three P domains, and the spatial arrangement of the three predicted ligand-binding sites on the trimer is very similar to that of the trimeric collectin, indicating that such an arrangement is generally required for pathogen-recognition. The ligand binding study of FD1 in solution indicated that the recombinant protein binds to N-acetyl-D-glucosamine and the peptide Gly-Pro-Arg-Pro and suggested that the ligand-binding region exhibits a conformational equilibrium involving cis-trans isomerization of the Asp-282-Cys-283 peptide bond. The crystal structure and the ligand binding study of FD1 provide an insight of the self-and non-self discrimination mechanism by ficolins.Surveillance systems of innate immunity are present in all multicellular organisms and play a crucial role in the first line of defense against pathogens. Ficolins, as well as collectins, are one of the most important groups of pattern recognition molecules in the innate immunity systems (1-7) and have been identified in both vertebrates and invertebrates (6). Ficolins are comprised of a collagen-like domain at the N terminus and a fibrinogen-like domain (FBG), 3 which is the sugar-binding site, at the C terminus (8, 9). Collectins, such as mannose-binding lectin (MBL), lung surfactant protein A, and surfactant protein D, also consist of an N-terminal collagen-like domain and a C-terminal carbohydrate-recognition domain (CRD) that binds to certain carbohydrates such as mannose and GlcNAc Ca 2ϩ dependently. The CRD on MBL, surfactant protein A, and surfactant protein D forms a trimeric structure through a triple ␣-helical coiled-coil at a short neck region between the collagen-like domain and the CRD (10 -12). Ficolins also form trimers (8,13,14), although the mechanism of trimerization is unclear. Both ficolins and collectins form trimer-based multimers that are N-terminally linked by disulfide bonds (15). Ficolins and MBL also interact with MBL-associated serine proteases, and their complexes activate the lectin complement pathway (6, 16 -23).Ficolins were originally discovered in porcine uterus membrane extracts as transforming growth factor-␤-binding proteins (24,25). In human, L-ficolin and H-ficolin in serum and M-ficolin in cells have been characterized (9, 14, 26 -29). Lficolin (synonymous with ficolin-2 or Ficolin/P35) binds to GlcNAc (29, 30) and GalNAc (8). The binding ability is inhibited by acetylated c...

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Trivalent Recognition Unit of Innate Immunity System

Tanio

Kondo

Sugio

et al. 2007

Journal of Biological Chemistry

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Innate Immune Mechanisms: Nonself Recognition

Quah¹,

Parish²

2010

Encyclopedia of Life Sciences

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The initial defence of the body against pathogens relies on the innate immune system. The innate immune system recognises unique molecular patterns expressed by pathogens, referred to as pathogen‐associated molecular patterns (PAMPs), through receptors known as pattern recognition molecules (PRMs). PRMs are a diverse range of cell‐bound and soluble proteins that sense extracellular and intracellular pathogens and induce a number of responses to help aid in their destruction including phagocytosis through opsonisation, cytokine production and activation of complement. In addition to pathogen sensing, host cells express proteins, the complement regulatory proteins, that protect them from attack by the alternative pathway of complement activation, whereas foreign organisms lack these protective proteins and are, therefore, susceptible to complement attack. Key Concepts: The innate immune system recognises pathogen‐associated molecular patterns (PAMPs) that are unique to pathogens. Cells of the innate immune system express a large range of pattern recognition molecules (PRM) that bind to PAMPs. Host cells express complement regulatory proteins that protect them from attack by innate mechanisms.

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Innate Immune Mechanisms: Nonself Recognition

Quah

Parish

2015

Encyclopedia of Life Sciences

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The initial defence of the body against pathogens relies on the innate immune system. The innate immune system recognises unique molecular patterns expressed by pathogens, referred to as pathogen‐associated molecular patterns ( PAMPs ), through receptors known as pattern recognition molecules ( PRMs ). PRMs are a diverse range of molecules and include secreted proteins, transmembrane proteins and cytosolic proteins. These molecules sense extracellular and intracellular pathogens and induce a number of responses to help aid in pathogen destruction including phagocytosis through opsonisation, cytokine production and activation of complement. In addition to pathogen sensing, host cells express proteins, the complement regulatory proteins that protect them from attack by the alternative pathway of complement activation, whereas foreign organisms lack these protective proteins and are, therefore, susceptible to complement attack. Key Concepts The innate immune system recognises pathogen‐associated molecular patterns (PAMPs) that are unique to pathogens. Cells of the innate immune system express a large range of pattern recognition molecules (PRM) that bind to PAMPs. PRMs are a diverse range of molecules and include secreted proteins, membrane‐associated proteins and cytosolic proteins. PRMs induce a number of host defence mechanisms upon recognition of PAMPs, including phagocytosis, cytokine production and complement activation. Host cells express complement regulatory proteins that protect them from attack by innate mechanisms.

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M‐ficolin is expressed on monocytes and is a lectin binding to N‐acetyl‐ d‐glucosamine and mediates monocyte adhesion and phagocytosis of Escherichia coli

Cited by 143 publications

References 25 publications

Trivalent Recognition Unit of Innate Immunity System

Trivalent Recognition Unit of Innate Immunity System

Innate Immune Mechanisms: Nonself Recognition

Innate Immune Mechanisms: Nonself Recognition

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