Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Deciphering the acylation pattern of Yersinia enterocolitica lipid A.

PLoS pathogens - 1 Jan 2012

Reinés Mar, Llobet Enrique, Dahlström Käthe M, Pérez-Gutiérrez Camino, Llompart Catalina M, Torrecabota Nuria, Salminen Tiina A, Bengoechea José A

Abstract excerpt

Pathogenic bacteria may modify their surface to evade the host innate immune response. Yersinia enterocolitica modulates its lipopolysaccharide (LPS) lipid A structure, and the key regulatory signal is temperature. At 21°C, lipid A is hexa-acylated and may be modified with aminoarabinose or palmitate. At 37°C, Y. enterocolitica expresses a tetra-acylated lipid A consistent with the 3'-O-deacylation of the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Acylation
Share to Adhesins, Bacterial

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Arabinose

Share to Carboxylic Ester Hydrolases

Share to Lipid A

Share to Palmitic Acids

Share to Yersinia enterocolitica

Share to Yersinia Infections

Source

Open in PubMed Open full text

Identifiers

PMID: 23133372
DOI: 10.1371/journal.ppat.1002978
PMCID: PMC3486919

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Deciphering the acylation pattern of Yersinia enterocolitica lipid A.PMID 23133372Read ↗

Site-specific acylation changes in the lipid A of Escherichia coli lpxL mutants grown at high temperatures.Semantic proximity Read ↗

Characterization of late acyltransferase genes of Yersinia pestis and their role in temperature-dependent lipid A variation.Semantic proximity Read ↗

Early evolutionary loss of the lipid A modifying enzyme PagP resulting in innate immune evasion in Yersinia pestis.Semantic proximity Read ↗

Lipopolysaccharide O antigen status of Yersinia enterocolitica O:8 is essential for virulence and absence of O antigen affects the expression of other Yersinia virulence factors.Semantic proximity Read ↗

Human TLR4 and noncanonical inflammasome differ in their ability to respond to distinct lipid A variantsSemantic proximity Read ↗

LPS remodeling is an evolved survival strategy for bacteria.Semantic proximity Read ↗

Distinct biological activity of lipopolysaccharides with different lipid A acylation status from mutant strains of Yersinia pestis and some members of genus Psychrobacter.Semantic proximity Read ↗

Structural determination of <i>Rickettsia</i> lipid A without chemical extraction confirms shorter acyl chains in later-evolving Spotted Fever Group pathogensSemantic proximity Read ↗

Complexity of lipopolysaccharide modifications in Salmonella enterica: Its effects on endotoxin activity, membrane permeability, and resistance to antimicrobial peptidesSemantic proximity Read ↗

Structural snapshots along the reaction pathway of Yersinia pestis RipA, a putative butyryl-CoA transferase.Semantic proximity Read ↗

The LpxL acyltransferase is required for normal growth and penta-acylation of lipid A in Burkholderia cenocepacia.Semantic proximity Read ↗

An inner membrane enzyme in Salmonella and Escherichia coli that transfers 4-amino-4-deoxy-L-arabinose to lipid A: induction on polymyxin-resistant mutants and role of a novel lipid-linked donor.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.