IlsA, a unique surface protein of Bacillus cereus required for iron acquisition from heme, hemoglobin and ferritin
about
Shared and distinct mechanisms of iron acquisition by bacterial and fungal pathogens of humansHaemophore functions revisitedA putative P-type ATPase required for virulence and resistance to haem toxicity in Listeria monocytogenesStructural Basis for Hemoglobin Capture by Staphylococcus aureus Cell-surface Protein, IsdHThe Near-iron Transporter (NEAT) Domains of the Anthrax Hemophore IsdX2 Require a Critical Glutamine to Extract Heme from MethemoglobinDifferential Function of Lip Residues in the Mechanism and Biology of an Anthrax HemophoreStructure of the Hemoglobin-IsdH Complex Reveals the Molecular Basis of Iron Capture byStaphylococcus aureusMolecular and evolutionary analysis of NEAr-iron Transporter (NEAT) domainsComparative Genomics of Iron-Transporting Systems in Bacillus cereus Strains and Impact of Iron Sources on Growth and Biofilm FormationBacterial swimmers that infiltrate and take over the biofilm matrix.The red flour beetle as a model for bacterial oral infections.IsdB-dependent hemoglobin binding is required for acquisition of heme by Staphylococcus aureus.A Bacillus anthracis S-layer homology protein that binds heme and mediates heme delivery to IsdCThe pore-forming protein Cry5B elicits the pathogenicity of Bacillus sp. against Caenorhabditis elegans.Iron acquisition in Bacillus cereus: the roles of IlsA and bacillibactin in exogenous ferritin iron mobilizationThe five near-iron transporter (NEAT) domain anthrax hemophore, IsdX2, scavenges heme from hemoglobin and transfers heme to the surface protein IsdC.Hal Is a Bacillus anthracis heme acquisition proteinThe insect Galleria mellonella as a powerful infection model to investigate bacterial pathogenesisDifferentiation of Bacillus anthracis, B. cereus, and B. thuringiensis on the basis of the csaB gene reflects host sourceSequestration and scavenging of iron in infection.The theft of host heme by Gram-positive pathogenic bacteria.Recent developments in understanding the iron acquisition strategies of gram positive pathogens.hsdS, Belonging to the Type I Restriction-Modification System, Contributes to the Streptococcus suis Serotype 2 Survival Ability in Phagocytes.Immunity of the greater wax moth Galleria mellonella.A novel metalloproteinase virulence factor is involved in Bacillus thuringiensis pathogenesis in nematodes and insects.DltX of Bacillus thuringiensis Is Essential for D-Alanylation of Teichoic Acids and Resistance to Antimicrobial Response in Insects.Collagen-like glycoprotein BclS is involved in the formation of filamentous structures of the Lysinibacillus sphaericus exosporium.Shr of group A streptococcus is a new type of composite NEAT protein involved in sequestering haem from methaemoglobinBalancing mcr-1 expression and bacterial survival is a delicate equilibrium between essential cellular defence mechanisms.Characterization of the second conserved domain in the heme uptake protein HtaA from Corynebacterium diphtheriae.Small RNA-mediated Cry toxin silencing allows Bacillus thuringiensis to evade Caenorhabditis elegans avoidance behavioral defenses.
P2860
Q21131297-7A6E8CE1-8253-4692-8B1C-FF34F88E3BDAQ26829609-97EF11CA-6463-47A4-9149-2008C30E2D58Q27309201-CD28CC8E-5093-43BB-9982-D2A0F7425470Q27673904-1A62969D-FA19-41A5-B449-754BEA4FD844Q27676069-17FD3A86-6B8A-4CCC-A2FF-2D0A9AB724C4Q27678024-CF503CF9-F2D5-40AB-88BD-4EC944E1AB47Q27681340-E206FC73-5E5D-4935-9DB3-9DD7FCA925B1Q28542534-CEF5419D-01D9-4EDB-8A6F-4E856FC5F4ACQ28601569-CD6248D9-01E9-493D-903C-F71B1196DEB4Q30524197-7C127B4D-5A1C-453F-B11C-D87573DB9687Q31118779-CFD9212B-8212-48A0-BAF4-03AA25287E44Q33687709-546B6AD2-4A18-4EE3-AE0A-A86C4EC6769CQ33964194-F6EEF271-A19E-4D5F-B710-913BE6FE634CQ34117229-7D5E8225-C0CF-4508-B453-9C55AE7E983EQ35097113-D3609E07-BF11-4DA0-AB82-FD5CD57117B5Q35311792-0265ED88-1A5E-4FF3-8573-CE4DC1559642Q36281042-3D747B75-6A15-407F-83FB-F86DB1AEC047Q36594846-EB1AE5E7-A6F4-48FB-AEE8-18CF4722F0F2Q36911213-D047E0B6-13FE-4C7A-8B16-F1089953C598Q37264669-D84C5D4C-F0D1-4F45-949F-886D50DD33E9Q37897143-47C5984A-DF92-4763-84AF-098CEC719CDBQ38415707-9D40CC6E-23C1-44B6-A952-150BDB311892Q38693998-51620928-2413-453B-9E93-7E716F64160DQ38723721-B3494CC6-A468-40DA-B4A0-A0B14C0FBA33Q40748607-2BC583FD-50F9-4F00-A730-19D800210F81Q41222006-4B238B24-5DE6-41BF-B7CA-A5D59BDAC57FQ42198405-5018E299-9138-48C4-A8BC-C1B6B4B7A121Q42398674-7F51EAA7-CC49-4119-A3A5-FF3AA28CB760Q47154422-7CA0E246-85DA-4AE4-828A-B6A42BA132AFQ48019657-D43508F1-9B7A-4BF1-B4DA-7AB770A8DB36Q50082693-D4188BAF-BDC8-431D-8646-8D9EA627E62D
P2860
IlsA, a unique surface protein of Bacillus cereus required for iron acquisition from heme, hemoglobin and ferritin
description
2009 nî lūn-bûn
@nan
2009 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
IlsA, a unique surface protein ...... heme, hemoglobin and ferritin
@ast
IlsA, a unique surface protein ...... heme, hemoglobin and ferritin
@en
IlsA, a unique surface protein ...... heme, hemoglobin and ferritin
@nl
type
label
IlsA, a unique surface protein ...... heme, hemoglobin and ferritin
@ast
IlsA, a unique surface protein ...... heme, hemoglobin and ferritin
@en
IlsA, a unique surface protein ...... heme, hemoglobin and ferritin
@nl
prefLabel
IlsA, a unique surface protein ...... heme, hemoglobin and ferritin
@ast
IlsA, a unique surface protein ...... heme, hemoglobin and ferritin
@en
IlsA, a unique surface protein ...... heme, hemoglobin and ferritin
@nl
P2093
P2860
P3181
P1433
P1476
IlsA, a unique surface protein ...... heme, hemoglobin and ferritin
@en
P2093
Christina Nielsen-LeRoux
Christophe Buisson
Didier Lereclus
Michel Gohar
Mireille Kallassy
Nadine Daou
P2860
P304
P3181
P356
10.1371/JOURNAL.PPAT.1000675
P407
P577
2009-11-26T00:00:00Z