In Silico Determination and Validation of neisserial surface protein A (NspA) Structure and Ligand Binding Site
Publish place: دومین کنفرانس بین المللی علوم و مهندسی
Publish Year: 1394
نوع سند: مقاله کنفرانسی
زبان: English
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شناسه ملی سند علمی:
ICESCON02_229
تاریخ نمایه سازی: 16 شهریور 1395
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-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
Keywords:
Neisserial surface protein A , Neisseria meningitidis
Authors
Rozhia Zangeneh
Departeman of biology, Science and Art University, Yazd, Iran
Fateme Sefid
Department of Biology, shahed University ,Tehran-Qom Express Way
Shiva Zangeneh
Departeman of biological science, Shahid beheshti University, Tehran, Iran
Sama Amirisamani
Departeman of biology, Science and Art University, Yazd, Iran
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