PMC:7271924 / 17768-19166 JSON TXT

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LitCovid-PMC-OGER-BB

LitCovid-PubTator

LitCovid-PD-FMA-UBERON

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T201","span":{"begin":391,"end":398},"obj":"Body_part"},{"id":"T202","span":{"begin":488,"end":498},"obj":"Body_part"},{"id":"T203","span":{"begin":673,"end":684},"obj":"Body_part"},{"id":"T204","span":{"begin":937,"end":941},"obj":"Body_part"}],"attributes":[{"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":"Several 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":826,"end":830},"obj":"Body_part"},{"id":"T37","span":{"begin":872,"end":876},"obj":"Body_part"},{"id":"T38","span":{"begin":937,"end":941},"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":"Several 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":225,"end":245},"obj":"Disease"},{"id":"T32","span":{"begin":235,"end":245},"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":"Several 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

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T234","span":{"begin":204,"end":205},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T235","span":{"begin":292,"end":300},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_2"},{"id":"T236","span":{"begin":367,"end":370},"obj":"http://purl.obolibrary.org/obo/CLO_0051582"},{"id":"T237","span":{"begin":379,"end":380},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T238","span":{"begin":529,"end":530},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T239","span":{"begin":531,"end":539},"obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"T240","span":{"begin":609,"end":617},"obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"T241","span":{"begin":671,"end":672},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T242","span":{"begin":931,"end":936},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9606"},{"id":"T243","span":{"begin":1015,"end":1023},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_2"},{"id":"T244","span":{"begin":1218,"end":1219},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T245","span":{"begin":1340,"end":1341},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"}],"text":"Several 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-CHEBI

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T224","span":{"begin":140,"end":144},"obj":"Chemical"},{"id":"T225","span":{"begin":159,"end":161},"obj":"Chemical"},{"id":"T226","span":{"begin":308,"end":320},"obj":"Chemical"},{"id":"T227","span":{"begin":345,"end":349},"obj":"Chemical"},{"id":"T228","span":{"begin":391,"end":398},"obj":"Chemical"},{"id":"T229","span":{"begin":433,"end":437},"obj":"Chemical"},{"id":"T230","span":{"begin":488,"end":498},"obj":"Chemical"},{"id":"T231","span":{"begin":587,"end":591},"obj":"Chemical"},{"id":"T232","span":{"begin":673,"end":684},"obj":"Chemical"},{"id":"T233","span":{"begin":699,"end":703},"obj":"Chemical"},{"id":"T234","span":{"begin":925,"end":927},"obj":"Chemical"},{"id":"T235","span":{"begin":1028,"end":1039},"obj":"Chemical"},{"id":"T236","span":{"begin":1035,"end":1039},"obj":"Chemical"},{"id":"T237","span":{"begin":1122,"end":1124},"obj":"Chemical"},{"id":"T238","span":{"begin":1199,"end":1201},"obj":"Chemical"}],"attributes":[{"id":"A224","pred":"chebi_id","subj":"T224","obj":"http://purl.obolibrary.org/obo/CHEBI_18248"},{"id":"A225","pred":"chebi_id","subj":"T225","obj":"http://purl.obolibrary.org/obo/CHEBI_73585"},{"id":"A226","pred":"chebi_id","subj":"T226","obj":"http://purl.obolibrary.org/obo/CHEBI_26672"},{"id":"A227","pred":"chebi_id","subj":"T227","obj":"http://purl.obolibrary.org/obo/CHEBI_18248"},{"id":"A228","pred":"chebi_id","subj":"T228","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A229","pred":"chebi_id","subj":"T229","obj":"http://purl.obolibrary.org/obo/CHEBI_18248"},{"id":"A230","pred":"chebi_id","subj":"T230","obj":"http://purl.obolibrary.org/obo/CHEBI_35143"},{"id":"A231","pred":"chebi_id","subj":"T231","obj":"http://purl.obolibrary.org/obo/CHEBI_18248"},{"id":"A232","pred":"chebi_id","subj":"T232","obj":"http://purl.obolibrary.org/obo/CHEBI_6495"},{"id":"A233","pred":"chebi_id","subj":"T233","obj":"http://purl.obolibrary.org/obo/CHEBI_18248"},{"id":"A234","pred":"chebi_id","subj":"T234","obj":"http://purl.obolibrary.org/obo/CHEBI_73585"},{"id":"A235","pred":"chebi_id","subj":"T235","obj":"http://purl.obolibrary.org/obo/CHEBI_29034"},{"id":"A236","pred":"chebi_id","subj":"T236","obj":"http://purl.obolibrary.org/obo/CHEBI_18248"},{"id":"A237","pred":"chebi_id","subj":"T237","obj":"http://purl.obolibrary.org/obo/CHEBI_73585"},{"id":"A238","pred":"chebi_id","subj":"T238","obj":"http://purl.obolibrary.org/obo/CHEBI_73585"}],"text":"Several 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-GO-BP

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T42","span":{"begin":391,"end":411},"obj":"http://purl.obolibrary.org/obo/GO_0015031"},{"id":"T43","span":{"begin":546,"end":557},"obj":"http://purl.obolibrary.org/obo/GO_0006810"},{"id":"T44","span":{"begin":576,"end":586},"obj":"http://purl.obolibrary.org/obo/GO_0006810"},{"id":"T45","span":{"begin":723,"end":753},"obj":"http://purl.obolibrary.org/obo/GO_0033572"},{"id":"T46","span":{"begin":742,"end":753},"obj":"http://purl.obolibrary.org/obo/GO_0006810"},{"id":"T47","span":{"begin":1366,"end":1391},"obj":"http://purl.obolibrary.org/obo/GO_0002250"}],"text":"Several 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

{"project":"LitCovid-sentences","denotations":[{"id":"T144","span":{"begin":0,"end":184},"obj":"Sentence"},{"id":"T145","span":{"begin":185,"end":258},"obj":"Sentence"},{"id":"T146","span":{"begin":259,"end":505},"obj":"Sentence"},{"id":"T147","span":{"begin":506,"end":808},"obj":"Sentence"},{"id":"T148","span":{"begin":809,"end":898},"obj":"Sentence"},{"id":"T149","span":{"begin":899,"end":1111},"obj":"Sentence"},{"id":"T150","span":{"begin":1112,"end":1198},"obj":"Sentence"},{"id":"T151","span":{"begin":1199,"end":1315},"obj":"Sentence"},{"id":"T152","span":{"begin":1316,"end":1398},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Several 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-HP

{"project":"LitCovid-PD-HP","denotations":[{"id":"T6","span":{"begin":235,"end":245},"obj":"Phenotype"}],"attributes":[{"id":"A6","pred":"hp_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/HP_0001287"}],"text":"Several 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

{"project":"MyTest","denotations":[{"id":"32574271-25286931-34514697","span":{"begin":179,"end":182},"obj":"25286931"},{"id":"32574271-18675317-34514698","span":{"begin":351,"end":354},"obj":"18675317"},{"id":"32574271-10383753-34514699","span":{"begin":500,"end":503},"obj":"10383753"},{"id":"32574271-25286931-34514700","span":{"begin":803,"end":806},"obj":"25286931"},{"id":"32574271-25286931-34514701","span":{"begin":893,"end":896},"obj":"25286931"},{"id":"32574271-7359228-34514702","span":{"begin":976,"end":979},"obj":"7359228"},{"id":"32574271-28914813-34514703","span":{"begin":1257,"end":1259},"obj":"28914813"},{"id":"32574271-27234406-34514704","span":{"begin":1393,"end":1396},"obj":"27234406"}],"namespaces":[{"prefix":"_base","uri":"https://www.uniprot.org/uniprot/testbase"},{"prefix":"UniProtKB","uri":"https://www.uniprot.org/uniprot/"},{"prefix":"uniprot","uri":"https://www.uniprot.org/uniprotkb/"}],"text":"Several 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)."}

TEST0

{"project":"TEST0","denotations":[{"id":"32574271-179-186-2882289","span":{"begin":179,"end":182},"obj":"[\"25286931\"]"},{"id":"32574271-92-99-2882290","span":{"begin":351,"end":354},"obj":"[\"18675317\"]"},{"id":"32574271-235-242-2882291","span":{"begin":500,"end":503},"obj":"[\"10383753\"]"},{"id":"32574271-231-238-2882292","span":{"begin":803,"end":806},"obj":"[\"25286931\"]"},{"id":"32574271-84-91-2882293","span":{"begin":893,"end":896},"obj":"[\"25286931\"]"},{"id":"32574271-77-84-2882294","span":{"begin":976,"end":979},"obj":"[\"7359228\"]"},{"id":"32574271-58-64-2882295","span":{"begin":1257,"end":1259},"obj":"[\"28914813\"]"},{"id":"32574271-77-84-2882296","span":{"begin":1393,"end":1396},"obj":"[\"27234406\"]"}],"text":"Several 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)."}

2_test

{"project":"2_test","denotations":[{"id":"32574271-25286931-34514697","span":{"begin":179,"end":182},"obj":"25286931"},{"id":"32574271-18675317-34514698","span":{"begin":351,"end":354},"obj":"18675317"},{"id":"32574271-10383753-34514699","span":{"begin":500,"end":503},"obj":"10383753"},{"id":"32574271-25286931-34514700","span":{"begin":803,"end":806},"obj":"25286931"},{"id":"32574271-25286931-34514701","span":{"begin":893,"end":896},"obj":"25286931"},{"id":"32574271-7359228-34514702","span":{"begin":976,"end":979},"obj":"7359228"},{"id":"32574271-28914813-34514703","span":{"begin":1257,"end":1259},"obj":"28914813"},{"id":"32574271-27234406-34514704","span":{"begin":1393,"end":1396},"obj":"27234406"}],"text":"Several 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)."}

PMC:7271924 / 17768-19166 JSONTXT

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PMC:7271924 / 17768-19166 JSON TXT