ArticleThe Journal of biological chemistry2014
Involvement of Neisseria meningitidis lipoprotein GNA2091 in the assembly of a subset of outer membrane proteins.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- NHBA antibodies elicited by 4CMenB vaccination are key for serum bactericidal activity against Neisseria gonorrhoeae.NPJ vaccines · 2024Article
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- Unveiling the role of BON domain-containing proteins in antibiotic resistance.Frontiers in microbiology · 2024Review
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- BonA frommBio · 2021Article
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- Label-Free Quantitative Proteomics Distinguishes General and Site-Specific Host Responses to Pseudomonas aeruginosa Infection at the Ocular Surface.Proteomics · 2020Article
- The Serogroup B Meningococcal Vaccine Bexsero Elicits Antibodies to Neisseria gonorrhoeae.Clinical infectious diseases : an official publication of the Infectious Diseases Society of America · 2019Article
- Article
- TheFrontiers in immunology · 2019Article
- YraP Contributes to Cell Envelope Integrity and Virulence of Salmonella enterica Serovar Typhimurium.Infection and immunity · 2018Article
- A unified model for BAM function that takes into account type Vc secretion and species differences in BAM composition.AIMS microbiology · 2018Article
- NlpD links cell wall remodeling and outer membrane invagination during cytokinesis in Escherichia coli.PLoS genetics · 2017Article
- The Hfq regulon ofFEBS open bio · 2017Article
- Impact of Moderate Temperature Changes on Neisseria meningitidis Adhesion Phenotypes and Proteome.Infection and immunity · 2016Article
- Expression of the Gene for Autotransporter AutB ofFrontiers in cellular and infection microbiology · 2016Article
- Article
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Authors and funding
4 authors.
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Abstract
GNA2091 of Neisseria meningitidis is a lipoprotein of unknown function that is included in the novel 4CMenB vaccine. Here, we investigated the biological function and the subcellular localization of the protein. We demonstrate that GNA2091 functions in the assembly of outer membrane proteins (OMPs) because its absence resulted in the accumulation of misassembled OMPs. Cell fractionation and protease accessibility experiments showed that the protein is localized at the periplasmic side of the outer membrane. Pulldown experiments revealed that it is not stably associated with the β-barrel assembly machinery, the previously identified complex for OMP assembly. Thus, GNA2091 constitutes a novel outer membrane-based lipoprotein required for OMP assembly. Furthermore, its location at the inner side of the outer membrane indicates that protective immunity elicited by this antigen cannot be due to bactericidal or opsonic activity of antibodies.
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