Crystal Structure of Neisserial Surface Protein A (NspA), a Conserved Outer Membrane Protein with Vaccine Potential Export

@article{citeulike:3938793, abstract = {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. 10.1074/jbc.M302803200}, author = {Vandeputte-Rutten, Lucy and Bos, Martine P. and Tommassen, Jan and Gros, Piet}, citeulike-article-id = {3938793}, citeulike-linkout-0 = {http://dx.doi.org/10.1074/jbc.M302803200}, citeulike-linkout-1 = {http://www.jbc.org/cgi/content/abstract/278/27/24825#REF40}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/12716881}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=12716881}, day = {27}, doi = {10.1074/jbc.M302803200}, journal = {J. Biol. Chem.}, keywords = {crystal, homolog, membrane, neisseria, neisserial, opa, outer, protein, structure}, month = {June}, number = {27}, pages = {24825--24830}, posted-at = {2009-01-25 18:28:10}, priority = {2}, title = {Crystal Structure of Neisserial Surface Protein A (NspA), a Conserved Outer Membrane Protein with Vaccine Potential}, url = {http://dx.doi.org/10.1074/jbc.M302803200}, volume = {278}, year = {2003} }

TY - JOUR ID - citeulike:3938793 L3 - citeulike-article-id:3938793 N2 - 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. 10.1074/jbc.M302803200 IS - 27 JF - J. Biol. Chem. EP - 24830 TI - Crystal Structure of Neisserial Surface Protein A (NspA), a Conserved Outer Membrane Protein with Vaccine Potential VL - 278 SP - 24825 KW - crystal KW - homolog KW - membrane KW - neisseria KW - neisserial KW - opa KW - outer KW - protein KW - structure AU - Vandeputte-Rutten, Lucy AU - Bos, Martine AU - Tommassen, Jan AU - Gros, Piet PY - 2003/06/27/ UR - http://dx.doi.org/10.1074/jbc.M302803200 ER -