Crystal structure of Neisserial surface protein A (NspA), a conserved outer membrane protein with vaccine potential.
The neisserial surface protein A (NspA) from Neisseria meningitidis is a promising vaccine candidate because it is highly conserved among meningococcal strains and induces bactericidal antibodies. NspA is a homolog of the Opa proteins, which mediate adhesion to host cells. Here, we present the crystal structure of NspA, determined to 2.55-A resolution. NspA forms an eight-stranded antiparallel beta-barrel. The four loops at the extracellular side of the NspA molecule form a long cleft, which contains mainly hydrophobic residues and harbors a detergent molecule, suggesting that the protein might function in the binding of hydrophobic ligands, such as lipids. In addition, the structure provides a starting point for structure-based vaccine design.
Vandeputte-Rutten
Lucy
L
Department of Crystal and Structural Chemistry, Bijvoet Center for Biomolecular Research, Utrecht, The Netherlands.
Bos
Martine P
MP
Tommassen
Jan
J
Gros
Piet
P
D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry*; D001428:Bacterial Vaccines / Q000737:chemistry*; D018360:Crystallography, X-Ray; D015195:Drug Design; D008969:Molecular Sequence Data; D009345:Neisseria meningitidis / Q000737:chemistry*; D011487:Protein Conformation; D016415:Sequence Alignment; D013329:Structure-Activity Relationship
D001425:Bacterial Outer Membrane Proteins; D001428:Bacterial Vaccines; C105506:NspA protein, Neisseria