Identification of an iron-regulated outer membrane protein of Neisseria meningitidis involved in the utilization of hemoglobin complexed to haptoglobin.
about
Shared and distinct mechanisms of iron acquisition by bacterial and fungal pathogens of humansA Neisseria meningitidis fbpABC mutant is incapable of using nonheme iron for growthCorynebacterium diphtheriae genes required for acquisition of iron from haemin and haemoglobin are homologous to ABC haemin transporters.Isolation of mutants of Vibrio anguillarum defective in haeme utilisation and cloning of huvA, a gene coding for an outer membrane protein involved in the use of haeme as iron source.Distribution of transferrin binding protein B gene (tbpB) variants among Neisseria species.Host iron binding proteins acting as niche indicators for Neisseria meningitidisTransport of intact porphyrin by HpuAB, the hemoglobin-haptoglobin utilization system of Neisseria meningitidis.Neisseria gonorrhoeae heme biosynthetic mutants utilize heme and hemoglobin as a heme source but fail to grow within epithelial cells.Pathogenic neisseriae can use hemoglobin, transferrin, and lactoferrin independently of the tonB locus.Genotypic and phenotypic modifications of Neisseria meningitidis after an accidental human passage.Transition metals at the host-pathogen interface: how Neisseria exploit human metalloproteins for acquiring iron and zinc.FbpC is not essential for iron acquisition in Neisseria gonorrhoeae.Molecular characterization of the hemin uptake locus (hmu) from Yersinia pestis and analysis of hmu mutants for hemin and hemoprotein utilization.Pyrophosphate-mediated iron acquisition from transferrin in Neisseria meningitidis does not require TonB activity.Binding and accumulation of hemin in Neisseria gonorrhoeae.A Legionella pneumophila gene that promotes hemin binding.A hemoglobin-binding outer membrane protein is involved in virulence expression by Haemophilus ducreyi in an animal model.Cloning of a DNA fragment encoding a heme-repressible hemoglobin-binding outer membrane protein from Haemophilus influenzae.Identification and purification of a hemoglobin-binding outer membrane protein from Neisseria gonorrhoeae.Evaluation of recombinant transferrin-binding protein B variants from Neisseria meningitidis for their ability to induce cross-reactive and bactericidal antibodies against a genetically diverse collection of serogroup B strains.Characterization of hemin binding activity of Streptococcus pneumoniae.A mutant form of the Neisseria gonorrhoeae pilus secretin protein PilQ allows increased entry of heme and antimicrobial compoundsA monoclonal antibody directed against the 97-kilodalton gonococcal hemin-binding protein inhibits hemin utilization by Neisseria gonorrhoeaeIron transport systems in Neisseria meningitidisInfluence of the combination and phase variation status of the haemoglobin receptors HmbR and HpuAB on meningococcal virulence.Iron and heme utilization in Porphyromonas gingivalis.Buried Treasure: Evolutionary Perspectives on Microbial Iron Piracy.Structural analysis of haemoglobin binding by HpuA from the Neisseriaceae family.Neisseria meningitidis tonB, exbB, and exbD genes: Ton-dependent utilization of protein-bound iron in Neisseriae.Kinetic analysis of ligand interaction with the gonococcal transferrin-iron acquisition systemBacterial heme-transport proteins and their heme-coordination modes.Sequestration and scavenging of iron in infection.Identification of a New Lipoprotein Export Signal in Gram-Negative Bacteria.HmbR outer membrane receptors of pathogenic Neisseria spp.: iron-regulated, hemoglobin-binding proteins with a high level of primary structure conservation.Heme Synthesis and Acquisition in Bacterial Pathogens.Neisserial surface lipoproteins: structure, function and biogenesis.HmbR, a hemoglobin-binding outer membrane protein of Neisseria meningitidis, undergoes phase variationConstruction and consequences of directed mutations affecting the hemin receptor in pathogenic Corynebacterium species.Phase variation of hemoglobin utilization in Neisseria gonorrhoeae.Identification and molecular analysis of lbpBA, which encodes the two-component meningococcal lactoferrin receptor.
P2860
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P2860
Identification of an iron-regulated outer membrane protein of Neisseria meningitidis involved in the utilization of hemoglobin complexed to haptoglobin.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Identification of an iron-regu ...... obin complexed to haptoglobin.
@ast
Identification of an iron-regu ...... obin complexed to haptoglobin.
@en
type
label
Identification of an iron-regu ...... obin complexed to haptoglobin.
@ast
Identification of an iron-regu ...... obin complexed to haptoglobin.
@en
prefLabel
Identification of an iron-regu ...... obin complexed to haptoglobin.
@ast
Identification of an iron-regu ...... obin complexed to haptoglobin.
@en
P2860
P1476
Identification of an iron-regu ...... obin complexed to haptoglobin.
@en
P2093
P2860
P304
P356
10.1128/JB.177.5.1299-1306.1995
P407
P577
1995-03-01T00:00:00Z