ArticleCurrent microbiology2016
Identification of Two Genes Encoding for the Late Acyltransferases of Lipid A in Klebsiella pneumoniae.
Article in Current microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 10 citations in OpenAlex.
- Proline-Hinged α-Helical Peptides Sensitize Gram-Positive Antibiotics, Expanding Their Physicochemical Properties to Be Used as Gram-Negative Antibiotics.Journal of medicinal chemistry · 2024Article
- Heterogeneity of Lipopolysaccharide as Source of Variability in Bioassays and LPS-Binding Proteins as Remedy.International journal of molecular sciences · 2023Review
- Lipid A structural diversity among members of the genusFrontiers in microbiology · 2023Article
- Variation, Modification and Engineering of Lipid A in Endotoxin of Gram-Negative Bacteria.International journal of molecular sciences · 2021Review
- Analogues of a Cyclic Antimicrobial Peptide with a Flexible Linker Show Promising Activity againstAntibiotics (Basel, Switzerland) · 2020Article
- Identification and Characterization of Two Klebsiella pneumoniaeInfection and immunity · 2017Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lipid A, the hydrophobic anchor of lipopolysaccharide, is an essential component in the outer membrane of most gram-negative bacteria. It is recognized by the TLR4/MD2 receptor of the innate immune system, which triggers an inflammatory response accompanied by massive overproduction of cytokines and leads to gram-negative septic shock. Human pathogen Klebsiella pneumoniae, which may synthesize two lipid A species, differs by the length of the secondary acyl chain. In this study, we identified two genes encoding the putative late acyltransferases of lipid A biosynthesis pathway in K. pneumoniae. Based on the sequence alignment, proteins YP_002239312.1 encoded by KPK3489 and YP_002239899.1 encoded by KPK4096 are homologous to E. coli LpxL, which were designated as LpxL1 and LpxL2, respectively. Functions of the two acyltransferases were confirmed by overexpressing the genes in E. coli, isolating lipid A and analyzing their structures using an ESI/MS. Like E. coli LpxL, K. pneumoniae LpxL1 transfers a C12:0 secondary acyl chain to the 2'-position of lipid A, while K. pneumoniae LpxL2 transfers a C14:0 secondary acyl chain to the 2'-position primary acyl chain of lipid A. These two acyltransferases might play important roles in the biosynthesis of lipid A and the innate immune system recognition in K. pneumoniae.
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Registered trials
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