ArticleInfection and immunity2001
Modification of lipid A biosynthesis in Neisseria meningitidis lpxL mutants: influence on lipopolysaccharide structure, toxicity, and adjuvant activity.
Article in Infection and immunity, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 121 papers.
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Who cites it
121 citing papers in PubMed, 213 citations in OpenAlex.
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- Optimization of methods for isolation and purification of outer membrane vesicles (OMVs) from Neisseria lactamica.Applied microbiology and biotechnology · 2025Article
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- Engineered bacterial outer membrane vesicles: a versatile bacteria-based weapon against gastrointestinal tumors.Theranostics · 2024Review
- Characterisation and Immunogenicity ofFrontiers in immunology · 2024Article
- Bacterial Membrane Vesicles: Physiological Roles, Infection Immunology, and Applications.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Review
- The Two Faces of Bacterial Membrane Vesicles: Pathophysiological Roles and Therapeutic Opportunities.Antibiotics (Basel, Switzerland) · 2023Review
- Emerging role of bacterial outer membrane vesicle in gastrointestinal tract.Gut pathogens · 2023Review
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- Bacterial outer-membrane vesicles promote Vγ9Vδ2 T cell oncolytic activity.Frontiers in immunology · 2023Article
- Position-Specific Secondary Acylation Determines Detection of Lipid A by Murine TLR4 and Caspase-11.Infection and immunity · 2022Article
61 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
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two genes homologous to lpxL and lpxM from Escherichia coli and other gram-negative bacteria, which are involved in lipid A acyloxyacylation, were identified in Neisseria meningitidis strain H44/76 and insertionally inactivated. Analysis by tandem mass spectrometry showed that one of the resulting mutants, termed lpxL1, makes lipopolysaccharide (LPS) with penta- instead of hexa-acylated lipid A, in which the secondary lauroyl chain is specifically missing from the nonreducing end of the GlcN disaccharide. Insertional inactivation of the other (lpxL2) gene was not possible in wild-type strain H44/76 expressing full-length immunotype L3 lipopolysaccharide (LPS) but could be readily achieved in a galE mutant expressing a truncated oligosaccharide chain. Structural analysis of lpxL2 mutant lipid A showed a major tetra-acylated species lacking both secondary lauroyl chains and a minor penta-acylated species. The lpxL1 mutant LPS has retained adjuvant activity similar to wild-type meningococcal LPS when used for immunization of mice in combination with LPS-deficient outer membrane complexes from N. meningitidis but has reduced toxicity as measured in a tumor necrosis factor alpha induction assay with whole bacteria. In contrast, both adjuvant activity and toxicity of the lpxL2 mutant LPS are strongly reduced. As the combination of reduced toxicity and retained adjuvant activity has not been reported before for either lpxL or lpxM mutants from other bacterial species, our results demonstrate that modification of meningococcal lipid A biosynthesis can lead to novel LPS species more suitable for inclusion in human vaccines.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.