Publication Abstract from PubMed
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.
Crystal structure of Neisserial surface protein A (NspA), a conserved outer membrane protein with vaccine potential.,Vandeputte-Rutten L, Bos MP, Tommassen J, Gros P J Biol Chem. 2003 Jul 4;278(27):24825-30. Epub 2003 Apr 26. PMID:12716881[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
