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.

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.

Related Concept Videos

Formation of Lipopolysaccharides01:19

Formation of Lipopolysaccharides

Lipopolysaccharides (LPS) are crucial components of the outer membrane of Gram-negative bacteria, serving both structural and functional roles. It contributes to membrane stability and protects bacteria from host immune responses. LPS is composed of three major regions—lipid A, a core oligosaccharide, and an O antigen. The biosynthesis and assembly of LPS involve a highly coordinated set of enzymatic reactions and transport mechanisms. Additionally, LPS is recognized as an endotoxin, triggering...
Peptidoglycan Synthesis01:28

Peptidoglycan Synthesis

Structure of PeptidoglycanPeptidoglycan is a vital structural component of the bacterial cell wall, providing mechanical strength and shape to the cell. It consists of repeating units of two sugars—N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM)—linked by β-1,4 glycosidic bonds. These sugar chains are cross-linked by short peptide chains, forming a mesh-like polymer that surrounds the bacterial plasma membrane.Cytoplasmic Phase – Precursor SynthesisPeptidoglycan biosynthesis begins in...
GPI Anchoring of Proteins in the ER Membrane01:29

GPI Anchoring of Proteins in the ER Membrane

GPI-anchoring is a post-translational, reversible protein modification that is ubiquitous in eukaryotes. Such proteins are primarily present on the exoplasmic leaflet of the plasma membrane.
GPI-anchor structure
A sequence of 11 enzymatic reactions results in the synthesis of the complete GPI anchor consisting of a hydrophobic and a hydrophilic portion. The hydrophobic portion comprises phosphatidylinositol, while the hydrophilic part comprises polar groups like phosphoethanolamine,...
Bacterial Meningitis II: Pathophysiology01:26

Bacterial Meningitis II: Pathophysiology

Bacterial meningitis typically begins when pathogens such as Neisseria meningitidis and Streptococcus pneumoniae colonize the nasopharynx and invade the bloodstream. This process is facilitated by bacterial virulence factors, such as polysaccharide capsules, which resist phagocytosis and complement-mediated killing. Less commonly, bacteria reach the central nervous system via contiguous spread from infections like otitis media or sinusitis, through congenital or acquired dural defects, or...