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LitCovid-PMC-OGER-BB

LitCovid-PubTator

LitCovid-PD-FMA-UBERON

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T197","span":{"begin":494,"end":504},"obj":"Body_part"},{"id":"T198","span":{"begin":509,"end":519},"obj":"Body_part"},{"id":"T199","span":{"begin":867,"end":874},"obj":"Body_part"},{"id":"T200","span":{"begin":903,"end":913},"obj":"Body_part"},{"id":"T201","span":{"begin":2550,"end":2557},"obj":"Body_part"},{"id":"T202","span":{"begin":2647,"end":2657},"obj":"Body_part"},{"id":"T203","span":{"begin":2832,"end":2843},"obj":"Body_part"},{"id":"T204","span":{"begin":3096,"end":3100},"obj":"Body_part"}],"attributes":[{"id":"A197","pred":"fma_id","subj":"T197","obj":"http://purl.org/sig/ont/fma/fma62293"},{"id":"A198","pred":"fma_id","subj":"T198","obj":"http://purl.org/sig/ont/fma/fma62293"},{"id":"A199","pred":"fma_id","subj":"T199","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A200","pred":"fma_id","subj":"T200","obj":"http://purl.org/sig/ont/fma/fma62860"},{"id":"A201","pred":"fma_id","subj":"T201","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A202","pred":"fma_id","subj":"T202","obj":"http://purl.org/sig/ont/fma/fma62293"},{"id":"A203","pred":"fma_id","subj":"T203","obj":"http://purl.org/sig/ont/fma/fma63169"},{"id":"A204","pred":"fma_id","subj":"T204","obj":"http://purl.org/sig/ont/fma/fma62100"}],"text":"Bacteria and Lactoferrin\nOne of the most well-known characteristics of LF is that it is antibacterial (19, 144–148), antiviral (99, 149–151), antifungal (152–154), anti-inflammatory (26), and anti-carcinogenic (155). Its ability to of limit iron availability to microbes is one of its crucial amicrobial properties. Bacteria have, however, developed various ways to sequester iron (156). Figure 4 shows how bacteria acquire iron through receptor-mediated recognition of transferrin, hemopexin, hemoglobin, or hemoglobin-haptoglobin complexes and also LF (30). As well as binding it directly from the environment, bacterial siderophores can obtain iron by removing it from transferrin, lactoferrin, or ferritin (32). These siderophore-iron complexes are then recognized by receptors on the bacterium (30). Host innate immune functions are supported by the circulating protein, siderocalin, also known as Neutrophil gelatinase-associated lipocalin (NGAL), lipocalin2 or Lcn2 as it inhibits siderophore-mediated iron acquisition and release (30).\nFigure 4 Ways by which bacteria acquire iron [adapted from (19, 30)]. Transferrin receptor, lactoferrin receptor, hemophore (Hp), hemophore receptor, and hemopexin. Siderophores remove iron from lactoferrin, ferritin and transferrin, and also from the environment. Stealth siderophores are modified in such a way as to prevent siderocalin binding. A primary bacterial defense against siderocalin involves the production of stealth siderophores. Modified from Rosa et al. and Skaar (19, 30). Diagram created with BioRender (https://biorender.com/). Although LF has various means to counteract bacteria as part of its immune function (131), it is also capable of being hijacked to benefit the activities of bacteria. Thus, bacteria can also exploit LF by removing its bound ferric iron (19, 30). This process involves (1) synthesis of high-affinity ferric ion chelators by bacteria, (2) iron acquisition through LF or transferrin binding, mediated by bacterial-specific surface bacterial receptors, (3) or iron acquisition through bacterial reductases, which are able to reduce ferric to ferrous ions (19, 144–148).\nSeveral Gram-negative pathogens including members of the genera Neisseria and Moraxella have evolved two-component systems that can extract iron from the host LF and transferrin (157). N. meningitidis is a principal cause of bacterial meningitis in children. While the majority of pathogenic bacteria employ siderophores to chelate and scavenge iron (158), Neisseria has evolved a series of protein transporters that directly hijack iron sequestered in host transferrin, lactoferrin, and hemoglobin (159). The system consists of a membrane-bound transporter that extracts and transports iron across the outer membrane (TbpA for transferrin and LbpA for lactoferrin), and a lipoprotein that delivers iron-loaded lactoferrin/transferrin to the transporter (TbpB for transferrin and LbpB for lactoferrin) (157). LbpB binds the N-lobe of lactoferrin, whereas TbpB binds the C-lobe of transferrin (157). However, more than 90% of LF in human milk is in the form of apolactoferrin (160), which competes with siderophilic bacteria for ferric iron, and disrupts the proliferation of these microbial and other pathogens. Similarly LF supplements may play an important role to counteract bacterial processes. LF is consequently a significant element of host defense (19), and its levels may vary in health and during disease. It is hence known to be a modulator of innate and adaptive immune responses (161)."}

LitCovid-PD-UBERON

{"project":"LitCovid-PD-UBERON","denotations":[{"id":"T36","span":{"begin":2985,"end":2989},"obj":"Body_part"},{"id":"T37","span":{"begin":3031,"end":3035},"obj":"Body_part"},{"id":"T38","span":{"begin":3096,"end":3100},"obj":"Body_part"}],"attributes":[{"id":"A36","pred":"uberon_id","subj":"T36","obj":"http://purl.obolibrary.org/obo/UBERON_3010752"},{"id":"A37","pred":"uberon_id","subj":"T37","obj":"http://purl.obolibrary.org/obo/UBERON_3010752"},{"id":"A38","pred":"uberon_id","subj":"T38","obj":"http://purl.obolibrary.org/obo/UBERON_0001913"}],"text":"Bacteria and Lactoferrin\nOne of the most well-known characteristics of LF is that it is antibacterial (19, 144–148), antiviral (99, 149–151), antifungal (152–154), anti-inflammatory (26), and anti-carcinogenic (155). Its ability to of limit iron availability to microbes is one of its crucial amicrobial properties. Bacteria have, however, developed various ways to sequester iron (156). Figure 4 shows how bacteria acquire iron through receptor-mediated recognition of transferrin, hemopexin, hemoglobin, or hemoglobin-haptoglobin complexes and also LF (30). As well as binding it directly from the environment, bacterial siderophores can obtain iron by removing it from transferrin, lactoferrin, or ferritin (32). These siderophore-iron complexes are then recognized by receptors on the bacterium (30). Host innate immune functions are supported by the circulating protein, siderocalin, also known as Neutrophil gelatinase-associated lipocalin (NGAL), lipocalin2 or Lcn2 as it inhibits siderophore-mediated iron acquisition and release (30).\nFigure 4 Ways by which bacteria acquire iron [adapted from (19, 30)]. Transferrin receptor, lactoferrin receptor, hemophore (Hp), hemophore receptor, and hemopexin. Siderophores remove iron from lactoferrin, ferritin and transferrin, and also from the environment. Stealth siderophores are modified in such a way as to prevent siderocalin binding. A primary bacterial defense against siderocalin involves the production of stealth siderophores. Modified from Rosa et al. and Skaar (19, 30). Diagram created with BioRender (https://biorender.com/). Although LF has various means to counteract bacteria as part of its immune function (131), it is also capable of being hijacked to benefit the activities of bacteria. Thus, bacteria can also exploit LF by removing its bound ferric iron (19, 30). This process involves (1) synthesis of high-affinity ferric ion chelators by bacteria, (2) iron acquisition through LF or transferrin binding, mediated by bacterial-specific surface bacterial receptors, (3) or iron acquisition through bacterial reductases, which are able to reduce ferric to ferrous ions (19, 144–148).\nSeveral Gram-negative pathogens including members of the genera Neisseria and Moraxella have evolved two-component systems that can extract iron from the host LF and transferrin (157). N. meningitidis is a principal cause of bacterial meningitis in children. While the majority of pathogenic bacteria employ siderophores to chelate and scavenge iron (158), Neisseria has evolved a series of protein transporters that directly hijack iron sequestered in host transferrin, lactoferrin, and hemoglobin (159). The system consists of a membrane-bound transporter that extracts and transports iron across the outer membrane (TbpA for transferrin and LbpA for lactoferrin), and a lipoprotein that delivers iron-loaded lactoferrin/transferrin to the transporter (TbpB for transferrin and LbpB for lactoferrin) (157). LbpB binds the N-lobe of lactoferrin, whereas TbpB binds the C-lobe of transferrin (157). However, more than 90% of LF in human milk is in the form of apolactoferrin (160), which competes with siderophilic bacteria for ferric iron, and disrupts the proliferation of these microbial and other pathogens. Similarly LF supplements may play an important role to counteract bacterial processes. LF is consequently a significant element of host defense (19), and its levels may vary in health and during disease. It is hence known to be a modulator of innate and adaptive immune responses (161)."}

LitCovid-PD-MONDO

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T31","span":{"begin":2384,"end":2404},"obj":"Disease"},{"id":"T32","span":{"begin":2394,"end":2404},"obj":"Disease"}],"attributes":[{"id":"A31","pred":"mondo_id","subj":"T31","obj":"http://purl.obolibrary.org/obo/MONDO_0006670"},{"id":"A32","pred":"mondo_id","subj":"T32","obj":"http://purl.obolibrary.org/obo/MONDO_0004796"},{"id":"A33","pred":"mondo_id","subj":"T32","obj":"http://purl.obolibrary.org/obo/MONDO_0021108"}],"text":"Bacteria and Lactoferrin\nOne of the most well-known characteristics of LF is that it is antibacterial (19, 144–148), antiviral (99, 149–151), antifungal (152–154), anti-inflammatory (26), and anti-carcinogenic (155). Its ability to of limit iron availability to microbes is one of its crucial amicrobial properties. Bacteria have, however, developed various ways to sequester iron (156). Figure 4 shows how bacteria acquire iron through receptor-mediated recognition of transferrin, hemopexin, hemoglobin, or hemoglobin-haptoglobin complexes and also LF (30). As well as binding it directly from the environment, bacterial siderophores can obtain iron by removing it from transferrin, lactoferrin, or ferritin (32). These siderophore-iron complexes are then recognized by receptors on the bacterium (30). Host innate immune functions are supported by the circulating protein, siderocalin, also known as Neutrophil gelatinase-associated lipocalin (NGAL), lipocalin2 or Lcn2 as it inhibits siderophore-mediated iron acquisition and release (30).\nFigure 4 Ways by which bacteria acquire iron [adapted from (19, 30)]. Transferrin receptor, lactoferrin receptor, hemophore (Hp), hemophore receptor, and hemopexin. Siderophores remove iron from lactoferrin, ferritin and transferrin, and also from the environment. Stealth siderophores are modified in such a way as to prevent siderocalin binding. A primary bacterial defense against siderocalin involves the production of stealth siderophores. Modified from Rosa et al. and Skaar (19, 30). Diagram created with BioRender (https://biorender.com/). Although LF has various means to counteract bacteria as part of its immune function (131), it is also capable of being hijacked to benefit the activities of bacteria. Thus, bacteria can also exploit LF by removing its bound ferric iron (19, 30). This process involves (1) synthesis of high-affinity ferric ion chelators by bacteria, (2) iron acquisition through LF or transferrin binding, mediated by bacterial-specific surface bacterial receptors, (3) or iron acquisition through bacterial reductases, which are able to reduce ferric to ferrous ions (19, 144–148).\nSeveral Gram-negative pathogens including members of the genera Neisseria and Moraxella have evolved two-component systems that can extract iron from the host LF and transferrin (157). N. meningitidis is a principal cause of bacterial meningitis in children. While the majority of pathogenic bacteria employ siderophores to chelate and scavenge iron (158), Neisseria has evolved a series of protein transporters that directly hijack iron sequestered in host transferrin, lactoferrin, and hemoglobin (159). The system consists of a membrane-bound transporter that extracts and transports iron across the outer membrane (TbpA for transferrin and LbpA for lactoferrin), and a lipoprotein that delivers iron-loaded lactoferrin/transferrin to the transporter (TbpB for transferrin and LbpB for lactoferrin) (157). LbpB binds the N-lobe of lactoferrin, whereas TbpB binds the C-lobe of transferrin (157). However, more than 90% of LF in human milk is in the form of apolactoferrin (160), which competes with siderophilic bacteria for ferric iron, and disrupts the proliferation of these microbial and other pathogens. Similarly LF supplements may play an important role to counteract bacterial processes. LF is consequently a significant element of host defense (19), and its levels may vary in health and during disease. It is hence known to be a modulator of innate and adaptive immune responses (161)."}

LitCovid-PD-CLO

LitCovid-PD-CHEBI

LitCovid-PD-GO-BP

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T37","span":{"begin":810,"end":823},"obj":"http://purl.obolibrary.org/obo/GO_0045087"},{"id":"T38","span":{"begin":1009,"end":1025},"obj":"http://purl.obolibrary.org/obo/GO_0044847"},{"id":"T39","span":{"begin":1865,"end":1874},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T40","span":{"begin":1930,"end":1946},"obj":"http://purl.obolibrary.org/obo/GO_0044847"},{"id":"T41","span":{"begin":2049,"end":2065},"obj":"http://purl.obolibrary.org/obo/GO_0044847"},{"id":"T42","span":{"begin":2550,"end":2570},"obj":"http://purl.obolibrary.org/obo/GO_0015031"},{"id":"T43","span":{"begin":2705,"end":2716},"obj":"http://purl.obolibrary.org/obo/GO_0006810"},{"id":"T44","span":{"begin":2735,"end":2745},"obj":"http://purl.obolibrary.org/obo/GO_0006810"},{"id":"T45","span":{"begin":2882,"end":2912},"obj":"http://purl.obolibrary.org/obo/GO_0033572"},{"id":"T46","span":{"begin":2901,"end":2912},"obj":"http://purl.obolibrary.org/obo/GO_0006810"},{"id":"T47","span":{"begin":3525,"end":3550},"obj":"http://purl.obolibrary.org/obo/GO_0002250"}],"text":"Bacteria and Lactoferrin\nOne of the most well-known characteristics of LF is that it is antibacterial (19, 144–148), antiviral (99, 149–151), antifungal (152–154), anti-inflammatory (26), and anti-carcinogenic (155). Its ability to of limit iron availability to microbes is one of its crucial amicrobial properties. Bacteria have, however, developed various ways to sequester iron (156). Figure 4 shows how bacteria acquire iron through receptor-mediated recognition of transferrin, hemopexin, hemoglobin, or hemoglobin-haptoglobin complexes and also LF (30). As well as binding it directly from the environment, bacterial siderophores can obtain iron by removing it from transferrin, lactoferrin, or ferritin (32). These siderophore-iron complexes are then recognized by receptors on the bacterium (30). Host innate immune functions are supported by the circulating protein, siderocalin, also known as Neutrophil gelatinase-associated lipocalin (NGAL), lipocalin2 or Lcn2 as it inhibits siderophore-mediated iron acquisition and release (30).\nFigure 4 Ways by which bacteria acquire iron [adapted from (19, 30)]. Transferrin receptor, lactoferrin receptor, hemophore (Hp), hemophore receptor, and hemopexin. Siderophores remove iron from lactoferrin, ferritin and transferrin, and also from the environment. Stealth siderophores are modified in such a way as to prevent siderocalin binding. A primary bacterial defense against siderocalin involves the production of stealth siderophores. Modified from Rosa et al. and Skaar (19, 30). Diagram created with BioRender (https://biorender.com/). Although LF has various means to counteract bacteria as part of its immune function (131), it is also capable of being hijacked to benefit the activities of bacteria. Thus, bacteria can also exploit LF by removing its bound ferric iron (19, 30). This process involves (1) synthesis of high-affinity ferric ion chelators by bacteria, (2) iron acquisition through LF or transferrin binding, mediated by bacterial-specific surface bacterial receptors, (3) or iron acquisition through bacterial reductases, which are able to reduce ferric to ferrous ions (19, 144–148).\nSeveral Gram-negative pathogens including members of the genera Neisseria and Moraxella have evolved two-component systems that can extract iron from the host LF and transferrin (157). N. meningitidis is a principal cause of bacterial meningitis in children. While the majority of pathogenic bacteria employ siderophores to chelate and scavenge iron (158), Neisseria has evolved a series of protein transporters that directly hijack iron sequestered in host transferrin, lactoferrin, and hemoglobin (159). The system consists of a membrane-bound transporter that extracts and transports iron across the outer membrane (TbpA for transferrin and LbpA for lactoferrin), and a lipoprotein that delivers iron-loaded lactoferrin/transferrin to the transporter (TbpB for transferrin and LbpB for lactoferrin) (157). LbpB binds the N-lobe of lactoferrin, whereas TbpB binds the C-lobe of transferrin (157). However, more than 90% of LF in human milk is in the form of apolactoferrin (160), which competes with siderophilic bacteria for ferric iron, and disrupts the proliferation of these microbial and other pathogens. Similarly LF supplements may play an important role to counteract bacterial processes. LF is consequently a significant element of host defense (19), and its levels may vary in health and during disease. It is hence known to be a modulator of innate and adaptive immune responses (161)."}

LitCovid-sentences

LitCovid-PD-HP

{"project":"LitCovid-PD-HP","denotations":[{"id":"T6","span":{"begin":2394,"end":2404},"obj":"Phenotype"}],"attributes":[{"id":"A6","pred":"hp_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/HP_0001287"}],"text":"Bacteria and Lactoferrin\nOne of the most well-known characteristics of LF is that it is antibacterial (19, 144–148), antiviral (99, 149–151), antifungal (152–154), anti-inflammatory (26), and anti-carcinogenic (155). Its ability to of limit iron availability to microbes is one of its crucial amicrobial properties. Bacteria have, however, developed various ways to sequester iron (156). Figure 4 shows how bacteria acquire iron through receptor-mediated recognition of transferrin, hemopexin, hemoglobin, or hemoglobin-haptoglobin complexes and also LF (30). As well as binding it directly from the environment, bacterial siderophores can obtain iron by removing it from transferrin, lactoferrin, or ferritin (32). These siderophore-iron complexes are then recognized by receptors on the bacterium (30). Host innate immune functions are supported by the circulating protein, siderocalin, also known as Neutrophil gelatinase-associated lipocalin (NGAL), lipocalin2 or Lcn2 as it inhibits siderophore-mediated iron acquisition and release (30).\nFigure 4 Ways by which bacteria acquire iron [adapted from (19, 30)]. Transferrin receptor, lactoferrin receptor, hemophore (Hp), hemophore receptor, and hemopexin. Siderophores remove iron from lactoferrin, ferritin and transferrin, and also from the environment. Stealth siderophores are modified in such a way as to prevent siderocalin binding. A primary bacterial defense against siderocalin involves the production of stealth siderophores. Modified from Rosa et al. and Skaar (19, 30). Diagram created with BioRender (https://biorender.com/). Although LF has various means to counteract bacteria as part of its immune function (131), it is also capable of being hijacked to benefit the activities of bacteria. Thus, bacteria can also exploit LF by removing its bound ferric iron (19, 30). This process involves (1) synthesis of high-affinity ferric ion chelators by bacteria, (2) iron acquisition through LF or transferrin binding, mediated by bacterial-specific surface bacterial receptors, (3) or iron acquisition through bacterial reductases, which are able to reduce ferric to ferrous ions (19, 144–148).\nSeveral Gram-negative pathogens including members of the genera Neisseria and Moraxella have evolved two-component systems that can extract iron from the host LF and transferrin (157). N. meningitidis is a principal cause of bacterial meningitis in children. While the majority of pathogenic bacteria employ siderophores to chelate and scavenge iron (158), Neisseria has evolved a series of protein transporters that directly hijack iron sequestered in host transferrin, lactoferrin, and hemoglobin (159). The system consists of a membrane-bound transporter that extracts and transports iron across the outer membrane (TbpA for transferrin and LbpA for lactoferrin), and a lipoprotein that delivers iron-loaded lactoferrin/transferrin to the transporter (TbpB for transferrin and LbpB for lactoferrin) (157). LbpB binds the N-lobe of lactoferrin, whereas TbpB binds the C-lobe of transferrin (157). However, more than 90% of LF in human milk is in the form of apolactoferrin (160), which competes with siderophilic bacteria for ferric iron, and disrupts the proliferation of these microbial and other pathogens. Similarly LF supplements may play an important role to counteract bacterial processes. LF is consequently a significant element of host defense (19), and its levels may vary in health and during disease. It is hence known to be a modulator of innate and adaptive immune responses (161)."}

MyTest

TEST0

2_test

PMC:7271924 / 15609-19166 JSONTXT

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PMC:7271924 / 15609-19166 JSON TXT