Neisserial lipooligosaccharide is a target for complement component C4b. Inner core phosphoethanolamine residues define C4b linkage specificity.
about
The meningococcal vaccine candidate neisserial surface protein A (NspA) binds to factor H and enhances meningococcal resistance to complementlpt6, a gene required for addition of phosphoethanolamine to inner-core lipopolysaccharide of Neisseria meningitidis and Haemophilus influenzaeGenetic and functional analyses of PptA, a phospho-form transferase targeting type IV pili in Neisseria gonorrhoeaeCytosolic proteins contribute to surface plasminogen recruitment of Neisseria meningitidisTransmigration of polymorphnuclear neutrophils and monocytes through the human blood-cerebrospinal fluid barrier after bacterial infection in vitro.The MisR/MisS two-component regulatory system influences inner core structure and immunotype of lipooligosaccharide in Neisseria meningitidis.O-Acetylation of the terminal N-acetylglucosamine of the lipooligosaccharide inner core in Neisseria meningitidis. Influence on inner core structure and assembly.Profiles of structural heterogeneity in native lipooligosaccharides of Neisseria and cytokine inductionRole of complement in host defense against pneumococcal otitis mediaHost iron binding proteins acting as niche indicators for Neisseria meningitidisIdentification of cptA, a PmrA-regulated locus required for phosphoethanolamine modification of the Salmonella enterica serovar typhimurium lipopolysaccharide coreThe transcriptional repressor FarR is not involved in meningococcal fatty acid resistance mediated by the FarAB efflux pump and dependent on lipopolysaccharide structure.Sequence-based predictions of lipooligosaccharide diversity in the Neisseriaceae and their implication in pathogenicity.Lipooligosaccharide Structure is an Important Determinant in the Resistance of Neisseria Gonorrhoeae to Antimicrobial Agents of Innate Host DefenseThe oligosaccharide of gonococcal lipooligosaccharide contains several epitopes that are recognized by human antibodies.Inhibition of the classical pathway of complement by meningococcal capsular polysaccharidesEnhanced factor H binding to sialylated Gonococci is restricted to the sialylated lacto-N-neotetraose lipooligosaccharide species: implications for serum resistance and evidence for a bifunctional lipooligosaccharide sialyltransferase in GonococciPolar invasion and translocation of Neisseria meningitidis and Streptococcus suis in a novel human model of the blood-cerebrospinal fluid barrier.Biochemical analysis of Lpt3, a protein responsible for phosphoethanolamine addition to lipooligosaccharide of pathogenic Neisseria.Lipooligosaccharide structure contributes to multiple steps in the virulence of Neisseria meningitidis.Opc expression, LPS immunotype switch and pilin conversion contribute to serum resistance of unencapsulated meningococci.Meningococcal group W-135 and Y capsular polysaccharides paradoxically enhance activation of the alternative pathway of complement.Novel blocking human IgG directed against the pentapeptide repeat motifs of Neisseria meningitidis Lip/H.8 and Laz lipoproteinsHuman lipooligosaccharide IGG that prevents endemic meningococcal disease recognizes an internal lacto-N-neotetraose structure.Role of complement in defense of the middle ear revealed by restoring the virulence of nontypeable Haemophilus influenzae siaB mutants.Bacteremia in an immunocompromised patient caused by a commensal Neisseria meningitidis strain harboring the capsule null locus (cnl).Lipooligosaccharide Structures of Invasive and Carrier Isolates of Neisseria meningitidis Are Correlated with Pathogenicity and CarriageThe molecular mechanisms used by Neisseria gonorrhoeae to initiate infection differ between men and women.The relative roles of factor H binding protein, neisserial surface protein A, and lipooligosaccharide sialylation in regulation of the alternative pathway of complement on meningococciHeptose I glycan substitutions on Neisseria gonorrhoeae lipooligosaccharide influence C4b-binding protein binding and serum resistanceMisR/MisS two-component regulon in Neisseria meningitidis.Defining targets for complement components C4b and C3b on the pathogenic neisseriaeCloning, expression, purification and crystallization of an endotoxin-biosynthesis enzyme from Neisseria meningitidis.The meningococcal vaccine candidate GNA1870 binds the complement regulatory protein factor H and enhances serum resistanceA comparison of the endotoxin biosynthesis and protein oxidation pathways in the biogenesis of the outer membrane of Escherichia coli and Neisseria meningitidis.Phosphoethanolamine residues on the lipid A moiety of Neisseria gonorrhoeae lipooligosaccharide modulate binding of complement inhibitors and resistance to complement killing.The periplasmic disulfide oxidoreductase DsbA contributes to Haemophilus influenzae pathogenesis.Effect of host lactate on gonococci and meningococci: new concepts on the role of metabolites in pathogenicity.Phosphoethanolamine substitution of lipid A and resistance of Neisseria gonorrhoeae to cationic antimicrobial peptides and complement-mediated killing by normal human serumPeptidoglycan fragment release from Neisseria meningitidis
P2860
Q28474974-632C430C-0060-4061-8A3A-A2C1E1A21D64Q28484981-B01E1296-59B9-412E-B1FD-96FE13C441ACQ28492779-3A877ECB-4E4C-414B-914B-37AAD3B25B59Q28903782-968E44F5-EE34-42AF-9FF0-FEBEC5067FD3Q30540058-E84C30E8-DFD2-4484-913F-01D5C1B76C60Q31069986-CE0AC401-9871-4DC9-ABE2-73C54CE4FF3DQ33243022-4FBC033E-4B9B-4E71-9426-AD8811725125Q33373636-158E67CD-A402-41C6-A873-D098CDDBFCE7Q33399371-EBF237DC-C29E-48F7-92C0-0C6EE3E970AEQ33427822-9DF055B9-5B66-4E47-AB16-93F8FD0F05EAQ33788470-105B5E1C-EBD4-4C85-AAD7-94C615EA0676Q33847702-27F185D0-EAE9-4244-907D-AFA11848FE08Q33886334-A9E10FBF-CBDF-4A36-AB6E-F7094AC92BACQ33957867-DFE450EA-A31B-4472-A5DB-3DAC162D864EQ33963027-E1846E0E-1AEA-43DC-BDC1-1B65468666A9Q33992223-FD6EC2CB-2001-4795-9955-540ADBF7658BQ34111593-E93B4804-EB42-4996-8CF1-ECB50FE03107Q34131008-C1E7D0CA-392C-42C1-A653-DA24868D980EQ34303363-0A5123A8-C414-4B9E-8CBB-6530090AB56FQ34334420-3740F17C-040E-4472-812F-3C663241068AQ34428168-83EA5A2B-A6D0-4D46-8587-17644CA7D4D4Q34624357-9CC0380A-2DFA-40A1-9B1E-25103F134CF3Q35075181-BA36A1AB-806F-4C3C-931C-C0205FB9D2C0Q35626087-105ABDA9-980D-440C-9A0A-22F073C542FCQ35689035-1381E594-EB98-4B21-9A7C-6F3F865B0BEAQ35714421-5E394DFF-17AE-4343-BC2B-E426264DA582Q35865898-F3D9BACF-2365-48F5-A553-BBD080CAB626Q35920654-A06CAD40-B670-47B5-827B-1CA57B34A9B2Q35936064-AA575D57-298D-4632-8034-657697D6DCEEQ35949845-354BDAED-7735-4447-AF09-AF0272179FE3Q36421536-112651D4-56F2-498F-8D1B-22EF68FF3AE0Q36422066-82F2BF0F-1AD0-4998-8F81-4B95E7B2BB2FQ36433619-311D3484-1C4D-48AB-A10B-603728EA2D60Q36470692-36C9DB4E-3464-4BE4-A254-FF0749C12E8AQ36479175-4A4D6DA6-BCD0-4BAB-90DB-E6F83302395AQ36506184-C2E1F4A6-94DE-4477-9BA8-10244C38CEF5Q36539649-C67300E0-D386-4300-B26C-167DE19F3EC0Q36847072-168E4670-FBDD-4B95-AF57-73A0FFB76397Q37099451-A2DA88BB-38A8-40CC-99E5-CD68083C420DQ37123794-595258D7-D55F-452C-81C1-A16A06DE3AC1
P2860
Neisserial lipooligosaccharide is a target for complement component C4b. Inner core phosphoethanolamine residues define C4b linkage specificity.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
2003年论文
@zh
2003年论文
@zh-cn
name
Neisserial lipooligosaccharide ...... efine C4b linkage specificity.
@en
type
label
Neisserial lipooligosaccharide ...... efine C4b linkage specificity.
@en
prefLabel
Neisserial lipooligosaccharide ...... efine C4b linkage specificity.
@en
P2093
P2860
P356
P1476
Neisserial lipooligosaccharide ...... define C4b linkage specificity
@en
P2093
Andrew D Cox
E Richard Moxon
J Claire Wright
James C Richards
Jianjun Li
Joyce S Plested
Peter A Rice
Ryan Boden
Sanjay Ram
Seppo Meri
P2860
P304
50853-50862
P356
10.1074/JBC.M308364200
P407
P577
2003-10-02T00:00:00Z