ArticleThe Journal of biological chemistry2011
The LptD chaperone LptE is not directly involved in lipopolysaccharide transport in Neisseria meningitidis.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 42 citations in OpenAlex.
- Advances in Helicobacter pylori lipopolysaccharide structure and function.FEMS microbiology reviews · 2025Review
- Targeting LPS biosynthesis and transport in gram-negative bacteria in the era of multi-drug resistance.Biochimica et biophysica acta. Molecular cell research · 2023Review
- Article
- Genome-wide association studies reveal the role of polymorphisms affecting factor H binding protein expression in host invasion by Neisseria meningitidis.PLoS pathogens · 2021Article
- Intermembrane transport: Glycerophospholipid homeostasis of the Gram-negative cell envelope.Proceedings of the National Academy of Sciences of the United States of America · 2019Review
- Quantitative Proteomics of the 2016 WHOMolecular & cellular proteomics : MCP · 2019Article
- Structural Basis for the Lipopolysaccharide Export Activity of the Bacterial Lipopolysaccharide Transport System.International journal of molecular sciences · 2018Review
- Proteomics, Bioinformatics and Structure-Function Antigen Mining For Gonorrhea Vaccines.Frontiers in immunology · 2018Review
- Pseudomonas aeruginosa LptE is crucial for LptD assembly, cell envelope integrity, antibiotic resistance and virulence.Virulence · 2018Article
- The lipopolysaccharide transport (Lpt) machinery: A nonconventional transporter for lipopolysaccharide assembly at the outer membrane of Gram-negative bacteria.The Journal of biological chemistry · 2017Review
- A deeper mining on the protein composition of VA-MENGOC-BC®: An OMV-based vaccine against N. meningitidis serogroup B and C.Human vaccines & immunotherapeutics · 2017Review
- LptD is a promising vaccine antigen and potential immunotherapeutic target for protection against Vibrio species infection.Scientific reports · 2016Article
- Lipopolysaccharide transport and assembly at the outer membrane: the PEZ model.Nature reviews. Microbiology · 2016Review
- Article
- Antimicrobial peptide resistance in Neisseria meningitidis.Biochimica et biophysica acta · 2015Review
- Lipopolysaccharide transport to the cell surface: periplasmic transport and assembly into the outer membrane.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015Review
- Lipopolysaccharide is inserted into the outer membrane through an intramembrane hole, a lumen gate, and the lateral opening of LptD.Structure (London, England : 1993) · 2015Article
- Article
- LptE binds to and alters the physical state of LPS to catalyze its assembly at the cell surface.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Involvement of Neisseria meningitidis lipoprotein GNA2091 in the assembly of a subset of outer membrane proteins.The Journal of biological chemistry · 2014Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The biosynthesis of lipopolysaccharide (LPS) in gram-negative bacteria is well understood, in contrast to the transport to its destination, the outer leaflet of the outer membrane. In Escherichia coli, synthesis and transport of LPS are essential processes. Neisseria meningitidis, conversely, can survive without LPS and tolerates inactivation of genes involved in LPS synthesis and transport. Here, we analyzed whether the LptA, LptB, LptC, LptE, LptF, and LptG proteins, recently implicated in LPS transport in E. coli, function similarly in N. meningitidis. None of the analyzed proteins was essential in N. meningitidis, consistent with their expected roles in LPS transport and additionally demonstrating that they are not required for an essential process such as phospholipid transport. As expected, the absence of most of the Lpt proteins resulted in a severe defect in LPS transport. However, the absence of LptE did not disturb transport of LPS to the cell surface. LptE was found to be associated with LptD, and its absence affected total levels of LptD, suggesting a chaperone-like role for LptE in LptD biogenesis. The absence of a direct role of LptE in LPS transport was substantiated by bioinformatic analyses showing a low conservation of LptE in LPS-producing bacteria. Apparently, the role of LptE in N. meningitidis deviates from that in E. coli, suggesting that the Lpt system does not function in a completely conserved manner in all gram-negative bacteria.
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