In Silico Determination and Validation of neisserial surface protein A (NspA) Structure and Ligand Binding Site

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. Evidence suggests that NspA protein is a useful antigen for inclusion in an effective vaccine, hence the identification of its structure is very important.The present study was designed to in silico resolving the major obstacles in the control or in prevention of the N. meningitidisdisease. We exploitedbioinformatic tools to better understanding and characterizing the NspA structure

کلیدواژه ها:

Neisserial surface protein A ، Neisseria meningitidis