Brucella-Salmonella lipopolysaccharide chimeras are less permeable to hydrophobic probes and more sensitive to cationic peptides and EDTA than are their native Brucella sp. counterparts.
about
Capsule polysaccharide mediates bacterial resistance to antimicrobial peptidesBinding of protegrin-1 to Pseudomonas aeruginosa and Burkholderia cepacia.Analyzing the molecular mechanism of lipoprotein localization in BrucellaEffect of omp10 or omp19 deletion on Brucella abortus outer membrane properties and virulence in mice.The two-component system BvrR/BvrS essential for Brucella abortus virulence regulates the expression of outer membrane proteins with counterparts in members of the RhizobiaceaeBrucella abortus uses a stealthy strategy to avoid activation of the innate immune system during the onset of infection.Identification and isolation of Brucella suis virulence genes involved in resistance to the human innate immune system.The differential interaction of Brucella and ochrobactrum with innate immunity reveals traits related to the evolution of stealthy pathogensVirulent Brucella abortus prevents lysosome fusion and is distributed within autophagosome-like compartments.Regulation of the mitogen-activated protein kinases by Brucella spp. expressing a smooth and rough phenotype: relationship to pathogen invasiveness.Brucella abortus ornithine lipids are dispensable outer membrane components devoid of a marked pathogen-associated molecular pattern.The outer membrane of Brucella ovis shows increased permeability to hydrophobic probes and is more susceptible to cationic peptides than are the outer membranes of mutant rough Brucella abortus strains.The lipopolysaccharide core of Brucella abortus acts as a shield against innate immunity recognitionRole of the Brucella suis lipopolysaccharide O antigen in phagosomal genesis and in inhibition of phagosome-lysosome fusion in murine macrophages.Role of the Omp25/Omp31 family in outer membrane properties and virulence of Brucella ovisBrucella canis is an intracellular pathogen that induces a lower proinflammatory response than smooth zoonotic counterpartsDefensin susceptibility and colonization in the mouse model of AJ100, a polymyxin B-resistant, Brucella abortus RB51 isolate.N-Formyl-Perosamine Surface Homopolysaccharides Hinder the Recognition of Brucella abortus by Mouse Neutrophils.An evolutionary strategy for a stealthy intracellular Brucella pathogen.Brucella evasion of adaptive immunity.Brucella, nitrogen and virulence.Brucella central carbon metabolism: an update.In vitro Brucella suis infection prevents the programmed cell death of human monocytic cellsLipopolysaccharides of Brucella abortus and Brucella melitensis induce nitric oxide synthesis in rat peritoneal macrophages.Brucella abortus and its closest phylogenetic relative, Ochrobactrum spp., differ in outer membrane permeability and cationic peptide resistance.Pathogenic Yersinia enterocolitica strains increase the outer membrane permeability in response to environmental stimuli by modulating lipopolysaccharide fluidity and lipid A structure.Bactericidal and antiendotoxic properties of short cationic peptides derived from a snake venom Lys49 phospholipase A2.Different responses of macrophages to smooth and rough Brucella spp.: relationship to virulenceTemperature-regulated efflux pump/potassium antiporter system mediates resistance to cationic antimicrobial peptides in Yersinia.Lysine and novel hydroxylysine lipids in soil bacteria: amino acid membrane lipid response to temperature and pH in Pseudopedobacter saltansIdentification of Brucella abortus virulence proteins that modulate the host immune response.Novel mono-, di-, and trimethylornithine membrane lipids in northern wetland planctomycetes.Interaction of Brucella suis and Brucella abortus rough strains with human dendritic cells.The lipopolysaccharide of Brucella abortus BvrS/BvrR mutants contains lipid A modifications and has higher affinity for bactericidal cationic peptides.Characterization of a cationic surfactant-resistant mutant isolated spontaneously from Escherichia coli.Elucidation and identification of amino acid containing membrane lipids using liquid chromatography/high-resolution mass spectrometry.A two-component regulatory system playing a critical role in plant pathogens and endosymbionts is present in Brucella abortus and controls cell invasion and virulence.GTPases of the Rho subfamily are required for Brucella abortus internalization in nonprofessional phagocytes: direct activation of Cdc42.
P2860
Q24559990-92AEF9A5-87FC-4153-9BF9-67032AE85CC7Q24807172-6F72EFFE-E89E-4907-A229-E104FE96CBCCQ27003985-F640ABBB-C2D7-442B-9EFF-67C992437403Q30723599-42AC8054-7E7F-4DA3-8392-994E45C867FCQ30846698-7506E2BB-F740-4411-A984-CD473356D92CQ33291121-95C0FA09-CCE9-4227-9117-FE9F8AD60D39Q33294684-976EB99E-5D14-403D-B711-7B9740ADB845Q33468439-11F04A41-AEC8-458E-ADC2-D1EC22A4418BQ33754151-8A7A136A-6157-45E1-B282-224C3DD7A4FCQ33769058-FB277BBA-4515-4E4B-8AE4-4DF6F2E61112Q33797961-5E47178A-7FB4-4D72-9BFD-EA97E2A8D160Q34002596-4AB56553-C107-4521-88B1-D8BA56A75659Q34270392-253491DD-AD8A-4A22-8A49-4BF92D9C867AQ34714844-2E7BE2B3-A4C4-4F5F-BA5B-4D25C6553B84Q35949897-B62A7FBC-B9D3-4C9E-BCE5-53DFA4A1C01FQ36281386-08D5083F-26A7-4C69-8883-7795A28D9DF2Q36444823-0217E151-B1B8-4E01-B91A-5F6563490299Q37002295-67FE6C85-8A24-47C0-A8E5-A4ADD038C392Q37846874-D5984C05-47AE-482E-8CB0-E06B498CA83DQ38078458-0D432CD4-715E-442D-AA70-17BCD375F292Q38282517-ADF6D309-B4C4-454E-B119-C47DE0F54857Q38892749-C6B28506-1660-45F9-8154-72E7B8CE941BQ39513799-82716510-FC15-4D29-93E7-D73D9F0BED24Q39514877-42869B83-BEAE-499C-AB34-D8CF86128C06Q39516006-4C23E12B-3923-4CE1-BA88-1E8369EDBA8DQ39741818-F168EA5E-3A81-4A1D-8885-71EA9FF5DE12Q40442273-A65EBD01-E2F1-4666-A4E1-3B8D16460B0AQ40574714-4A38CA30-91F2-43B9-AF1E-88FA84C9B192Q41478684-FBA2443C-0796-41C4-80BC-A53A41237ACDQ41633335-BB57215C-D384-4B28-B73C-9BBCBA477E4CQ42410797-37F89971-0B99-4A13-9075-6FA5E71585A0Q42747814-F3FE2A10-15D8-49A4-B360-F6292AD0AEF7Q42909728-4889CC06-5379-4D52-9945-6B3CEE948D52Q42949034-A4313BCC-F345-472F-A6B8-39A645522C7BQ43889483-FA0DAD6C-D0E7-407B-A758-8251CC596FBEQ46535116-76850268-C950-44CE-82FD-3748E1547C02Q47694537-FF14896F-B2EC-405F-967D-B9E9EA41EB90Q50112973-8A90E150-077A-4582-827C-10BFD7C74622
P2860
Brucella-Salmonella lipopolysaccharide chimeras are less permeable to hydrophobic probes and more sensitive to cationic peptides and EDTA than are their native Brucella sp. counterparts.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
Brucella-Salmonella lipopolysa ...... ive Brucella sp. counterparts.
@ast
Brucella-Salmonella lipopolysa ...... ive Brucella sp. counterparts.
@en
type
label
Brucella-Salmonella lipopolysa ...... ive Brucella sp. counterparts.
@ast
Brucella-Salmonella lipopolysa ...... ive Brucella sp. counterparts.
@en
prefLabel
Brucella-Salmonella lipopolysa ...... ive Brucella sp. counterparts.
@ast
Brucella-Salmonella lipopolysa ...... ive Brucella sp. counterparts.
@en
P2093
P2860
P1476
Brucella-Salmonella lipopolysa ...... ive Brucella sp. counterparts.
@en
P2093
Pizarro-Cerdá J
Weintraub A
P2860
P304
P356
10.1128/JB.178.20.5867-5876.1996
P407
P577
1996-10-01T00:00:00Z