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Updated: Jun 5, 2026

Enrichment of Bacterial Lipoproteins and Preparation of N-terminal Lipopeptides for Structural Determination by Mass Spectrometry
Published on: May 21, 2018
1H, 13C and 15N assignment of the GNA1946 outer membrane lipoprotein from Neisseria meningitidis
A Neumoin1, A Leonchiks, P Petit
1Bijvoet Center for Biomolecular Research, Science Faculty, Utrecht University, Padualaan 8, 3584 CH, Utrecht, The Netherlands.
Abstract:
GNA1946 (Genome-derived Neisseria Antigen 1946) is a highly conserved exposed outer membrane lipoprotein from Neisseria meningitidis bacteria of 287 amino acid length (31 kDa). Although the structure of NMB1946 has been solved recently by X-Ray crystallography, understanding the behaviour of GNA1946 in aqueuos solution is highly relevant for the discovery of the antigenic determinants of the protein that will possibly lead to a more efficient vaccine development against virulent serogroup B strain of N. meningitidis. Here we report almost complete (1)H, (13)C and (15)N resonance assignments of GNA1946 (residues 10-287) in aqueous buffer solution.
Insights
Researchers have assigned nuclear magnetic resonance signals for Genome-derived Neisseria Antigen 1946 (GNA1946), a key protein from Neisseria meningitidis. This structural data in solution aids in developing new vaccines against bacterial meningitis.
Area of Science:
- Structural biology
- Protein chemistry
- Vaccine development
Background:
- Neisseria meningitidis serogroup B causes severe meningitis.
- GNA1946 is a conserved outer membrane lipoprotein antigen of N. meningitidis.
- Understanding GNA1946's solution behavior is crucial for vaccine design.
Purpose of the Study:
- To provide complete resonance assignments for GNA1946 in aqueous solution.
- To facilitate the identification of antigenic determinants on GNA1946.
- To support the development of a meningococcal serogroup B vaccine.
Main Methods:
- Nuclear Magnetic Resonance (NMR) spectroscopy.
- Collected (1)H, (13)C, and (15)N resonance assignments.
- Studied GNA1946 (residues 10-287) in aqueous buffer.
Main Results:
- Achieved near-complete (1)H, (13)C, and (15)N resonance assignments for GNA1946.
- Provided foundational data on GNA1946 structure and dynamics in solution.
- Enabled further investigation into GNA1946's antigenic properties.
Conclusions:
- NMR assignments provide critical insights into GNA1946's solution structure.
- This data is essential for epitope mapping and rational vaccine design.
- Facilitates progress towards an effective N. meningitidis serogroup B vaccine.
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