ArticleInfection and immunity2010
Identification and characterization of a glycosyltransferase involved in Acinetobacter baumannii lipopolysaccharide core biosynthesis.
Article in Infection and immunity, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers, 1 of them a synthesis that pooled it.
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Who cites it
71 citing papers in PubMed, 1 synthesis or guideline pooled it, 113 citations in OpenAlex.
- Intestinal microbiota signatures of clinical response and immune-related adverse events in melanoma patients treated with anti-PD-1.Nature medicine · 2022Pooled it
- Comparative pathogenomics and in silico analysis of energy metabolism in Acinetobacter baumannii ST195 and novel Turkish isolates encoding blaOXA-23, blaOXA-66, and blaOXA-852.International microbiology : the official journal of the Spanish Society for Microbiology · 2026Article
- Acinetobacter baumannii lipooligosaccharide core region promotes CD14-dependent TLR4 endocytosis and enhances pathogenicity through interferon-β production.PLoS pathogens · 2026Article
- A new component of the DNA damage response biofilm axis in Acinetobacter baumannii is a TetR-like DNA damage response regulator.FEMS microbiology letters · 2026Article
- A Novel Enterococcus Phage Endolysin Lys22 with a Wide Host Range Against Mixed Biofilm ofPathogens (Basel, Switzerland) · 2025Article
- Antibiotic-resistant Acinetobacter baumannii can be killed by a combination of bacteriophages and complement.Medical microbiology and immunology · 2025Article
- Acinetobacter phages use distinct strategies to breach the capsule barrier.PLoS pathogens · 2025Article
- Carbapenem-ResistantMicroorganisms · 2025Review
- Identification of EppR, a Second Repressor of Error-Prone DNA Polymerase Genes in Acinetobacter baumannii.Molecular microbiology · 2025Article
- AbOmpA in Acinetobacter baumannii: exploring virulence mechanisms of outer membrane-integrated and outer membrane vesicle-associated AbOmpA and developing anti-infective agents targeting AbOmpA.Journal of biomedical science · 2025Review
- Carbapenem-resistantiScience · 2024Review
- Emergence of multidrug-resistantEmerging microbes & infections · 2024Article
- Pan-Genome Plasticity and Virulence Factors: A Natural Treasure Trove forAntibiotics (Basel, Switzerland) · 2024Review
- Characterization ofmBio · 2024Article
- Acinetobacter baumannii as an oro-dental pathogen: a red alert!!Journal of applied oral science : revista FOB · 2024Review
- Outer Membrane Vesicles fromVaccines · 2023Review
- Exploring Roles of the Polysaccharide Capsule in Pathogenesis of HypervirulentAntibiotics (Basel, Switzerland) · 2023Article
- Systematic analyses identify modes of action of ten clinically relevant biocides and antibiotic antagonism in Acinetobacter baumannii.Nature microbiology · 2023Article
- Antimicrobial Resistance in Romania: Updates on Gram-Negative ESCAPE Pathogens in the Clinical, Veterinary, and Aquatic Sectors.International journal of molecular sciences · 2023Review
- Lipopolysaccharide structure modulates cationic biocide susceptibility and crystalline biofilm formation inFrontiers in microbiology · 2023Article
11 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Although Acinetobacter baumannii has emerged as a significant cause of nosocomial infections worldwide, there have been few investigations describing the factors important for A. baumannii persistence and pathogenesis. This paper describes the first reported identification of a glycosyltransferase, LpsB, involved in lipopolysaccharide (LPS) biosynthesis in A. baumannii. Mutational, structural, and complementation analyses indicated that LpsB is a core oligosaccharide glycosyl transferase. Using a genetic approach, lpsB was compared with the lpsB homologues of several A. baumannii strains. These analyses indicated that LpsB is highly conserved among A. baumannii isolates. Furthermore, we developed a monoclonal antibody, monoclonal antibody 13C11, which reacts to an LPS core epitope expressed by approximately one-third of the A. baumannii clinical isolates evaluated to date. Previous studies describing the heterogeneity of A. baumannii LPS were limited primarily to structural analyses; therefore, studies evaluating the correlation between these surface glycolipids and pathogenesis were warranted. Our data from an evaluation of LpsB mutant 307::TN17, which expresses a deeply truncated LPS glycoform consisting of only two 3-deoxy-d-manno-octulosonic acid residues and lipid A, suggest that A. baumannii LPS is important for resistance to normal human serum and confers a competitive advantage for survival in vivo. These results have important implications for the role of LPS in A. baumannii infections.
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