Activation of toll-like receptor 2 (TLR2) and TLR4/MD2 by Neisseria is independent of capsule and lipooligosaccharide (LOS) sialylation but varies widely among LOS from different strains (Q35105676)

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English	Activation of toll-like receptor 2 (TLR2) and TLR4/MD2 by Neisseria is independent of capsule and lipooligosaccharide (LOS) sialylation but varies widely among LOS from different strains	scientific article

Statements

scholarly article

1 reference

Europe PubMed Central

6 August 2017

Activation of toll-like receptor 2 (TLR2) and TLR4/MD2 by Neisseria is independent of capsule and lipooligosaccharide (LOS) sialylation but varies widely among LOS from different strains (English)

1 reference

Europe PubMed Central

6 August 2017

toll-like receptor

0 references

object named as

Gary A Jarvis

2

1 reference

ORCID Public Data File 2021

author name string

Alison C Pridmore

1

1 reference

Europe PubMed Central

6 August 2017

Constance M John

3

1 reference

Europe PubMed Central

6 August 2017

Dominic L Jack

4

1 reference

Europe PubMed Central

6 August 2017

Steven K Dower

5

1 reference

Europe PubMed Central

6 August 2017

Robert C Read

6

1 reference

Europe PubMed Central

6 August 2017

language of work or name

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publication date

1 July 2003

1 reference

Europe PubMed Central

6 August 2017

Infection and Immunity

1 reference

Europe PubMed Central

6 August 2017

71

1 reference

Europe PubMed Central

6 August 2017

7

1 reference

Europe PubMed Central

6 August 2017

3901-3908

1 reference

Europe PubMed Central

6 August 2017

Structure and function of lipopolysaccharides.

1 reference

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Modification of the structure and activity of lipid A in Yersinia pestis lipopolysaccharide by growth temperature

1 reference

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Proinflammatory responses to lipo-oligosaccharide of Neisseria meningitidis immunotype strains in relation to virulence and disease

1 reference

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9 July 2018

Human Toll-like receptor 4 recognizes host-specific LPS modifications.

1 reference

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9 July 2018

Cutting edge: Immune stimulation by neisserial porins is toll-like receptor 2 and MyD88 dependent.

1 reference

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Influence of the length of the lipooligosaccharide alpha chain on its sialylation in Neisseria meningitidis

1 reference

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Recognition of double-stranded RNA and activation of NF-kappaB by Toll-like receptor 3

1 reference

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Interaction of Neisseria meningitidis with human dendritic cells

1 reference

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Modification of lipid A biosynthesis in Neisseria meningitidis lpxL mutants: influence on lipopolysaccharide structure, toxicity, and adjuvant activity

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Membrane-associated proteins of a lipopolysaccharide-deficient mutant of Neisseria meningitidis activate the inflammatory response through toll-like receptor 2.

1 reference

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A Toll-like receptor recognizes bacterial DNA

1 reference

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The repertoire for pattern recognition of pathogens by the innate immune system is defined by cooperation between toll-like receptors

1 reference

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A lipopolysaccharide-deficient mutant of Neisseria meningitidis elicits attenuated cytokine release by human macrophages and signals via toll-like receptor (TLR) 2 but not via TLR4/MD2.

1 reference

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The Toll receptor family and microbial recognition

1 reference

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Toll-like receptor 4 imparts ligand-specific recognition of bacterial lipopolysaccharide

1 reference

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Specific lipopolysaccharide found in cystic fibrosis airway Pseudomonas aeruginosa

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Differential roles of TLR2 and TLR4 in recognition of gram-negative and gram-positive bacterial cell wall components

1 reference

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Endothelial adhesion molecule expression and its inhibition by recombinant bactericidal/permeability-increasing protein are influenced by the capsulation and lipooligosaccharide structure of Neisseria meningitidis

1 reference

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Cell activation and apoptosis by bacterial lipoproteins through toll-like receptor-2

1 reference

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MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4

1 reference

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The (alpha2-->8)-linked polysialic acid capsule and lipooligosaccharide structure both contribute to the ability of serogroup B Neisseria meningitidis to resist the bactericidal activity of normal human serum

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Lipid A acylation and bacterial resistance against vertebrate antimicrobial peptides.

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A family of human receptors structurally related to Drosophila Toll

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Sialylation of Neisseria meningitidis lipooligosaccharide inhibits serum bactericidal activity by masking lacto-N-neotetraose

1 reference

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A human homologue of the Drosophila Toll protein signals activation of adaptive immunity

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Regulation of lipid A modifications by Salmonella typhimurium virulence genes phoP-phoQ.

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PhoP-PhoQ activates transcription of pmrAB, encoding a two-component regulatory system involved in Salmonella typhimurium antimicrobial peptide resistance

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The (alpha2-->8)-linked polysialic acid capsule of group B Neisseria meningitidis modifies multiple steps during interaction with human macrophages

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Modulation of cell surface sialic acid expression in Neisseria meningitidis via a transposable genetic element.

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Sialic acid of group B Neisseria meningitidis regulates alternative complement pathway activation

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Identifiers

10.1128/IAI.71.7.3901-3908.2003

1 reference

Europe PubMed Central

6 August 2017

1 reference

Europe PubMed Central

6 August 2017

1 reference

Europe PubMed Central

6 August 2017

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