5T5F
Neisseria meningitidis factor H binding protein in complex with monoclonal antibody JAR5
5T5F の概要
エントリーDOI | 10.2210/pdb5t5f/pdb |
分子名称 | Factor H binding protein variant B24, Monoclonal antibody Jar5 heavy chain, Monoclonal antibody Jar5 light chain, ... (4 entities in total) |
機能のキーワード | fhbp, jar5, epitope mapping, monoclonal antibody, cooperativity, neisseria meningitidis, protein binding |
由来する生物種 | Neisseria meningitidis 詳細 |
タンパク質・核酸の鎖数 | 3 |
化学式量合計 | 73908.72 |
構造登録者 | |
主引用文献 | Malito, E.,Lo Surdo, P.,Veggi, D.,Santini, L.,Stefek, H.,Brunelli, B.,Luzzi, E.,Bottomley, M.J.,Beernink, P.T.,Scarselli, M. Neisseria meningitidis factor H-binding protein bound to monoclonal antibody JAR5: implications for antibody synergy. Biochem. J., 473:4699-4713, 2016 Cited by PubMed Abstract: Factor H-binding protein (fHbp) is an important antigen of Neisseria meningitidis that is capable of eliciting a robust protective immune response in humans. Previous studies on the interactions of fHbp with antibodies revealed that some anti-fHbp monoclonal antibodies that are unable to trigger complement-mediated bacterial killing in vitro are highly co-operative and become bactericidal if used in combination. Several factors have been shown to influence such co-operativity, including IgG subclass and antigen density. To investigate the structural basis of the anti-fHbp antibody synergy, we determined the crystal structure of the complex between fHbp and the Fab (fragment antigen-binding) fragment of JAR5, a specific anti-fHbp murine monoclonal antibody known to be highly co-operative with other monoclonal antibodies. We show that JAR5 is highly synergic with monoclonal antibody (mAb) 12C1, whose structure in complex with fHbp has been previously solved. Structural analyses of the epitopes recognized by JAR5 and 12C1, and computational modeling of full-length IgG mAbs of JAR5 and 12C1 bound to the same fHbp molecule, provide insights into the spatial orientation of Fc (fragment crystallizable) regions and into the possible implications for the susceptibility of meningococci to complement-mediated killing. PubMed: 27784765DOI: 10.1042/BCJ20160806 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.98 Å) |
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