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 cryst...

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Bibliographic Details
Published in:The Journal of biological chemistry 2003-07, Vol.278 (27), p.24825-24830
Main Authors: Vandeputte-Rutten, Lucy, Bos, Martine P, Tommassen, Jan, Gros, Piet
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Bacterial Outer Membrane Proteins - chemistry
Bacterial Vaccines - chemistry
Crystallography, X-Ray
Drug Design
Molecular Sequence Data
Neisseria meningitidis - chemistry
Protein Conformation
Sequence Alignment
Structure-Activity Relationship
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Summary: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-Å resolution. NspA forms an eight-stranded antiparallel β-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.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M302803200