3J6T
Cryo-EM structure of Dengue virus serotype 3 at 37 degrees C
Summary for 3J6T
| Entry DOI | 10.2210/pdb3j6t/pdb |
| Related | 3J6S 3J6U |
| EMDB information | 5933 5934 5935 |
| Descriptor | envelope protein, membrane protein (2 entities in total) |
| Functional Keywords | dengue virus, virus |
| Biological source | Dengue virus 3 More |
| Total number of polymer chains | 6 |
| Total formula weight | 186090.96 |
| Authors | Fibriansah, G.,Tan, J.L.,Smith, S.A.,de Alwis, R.,Ng, T.-S.,Kostyuchenko, V.A.,Kukkaro, P.,de Silva, A.M.,Crowe Jr., J.E.,Lok, S.-M. (deposition date: 2014-03-25, release date: 2015-03-04, Last modification date: 2024-02-21) |
| Primary citation | Fibriansah, G.,Tan, J.L.,Smith, S.A.,de Alwis, R.,Ng, T.S.,Kostyuchenko, V.A.,Jadi, R.S.,Kukkaro, P.,de Silva, A.M.,Crowe, J.E.,Lok, S.M. A highly potent human antibody neutralizes dengue virus serotype 3 by binding across three surface proteins. Nat Commun, 6:6341-6341, 2015 Cited by PubMed Abstract: Dengue virus (DENV) infects ~400 million people annually. There is no licensed vaccine or therapeutic drug. Only a small fraction of the total DENV-specific antibodies in a naturally occurring dengue infection consists of highly neutralizing antibodies. Here we show that the DENV-specific human monoclonal antibody 5J7 is exceptionally potent, neutralizing 50% of virus at nanogram-range antibody concentration. The 9 Å resolution cryo-electron microscopy structure of the Fab 5J7-DENV complex shows that a single Fab molecule binds across three envelope proteins and engages three functionally important domains, each from a different envelope protein. These domains are critical for receptor binding and fusion to the endosomal membrane. The ability to bind to multiple domains allows the antibody to fully coat the virus surface with only 60 copies of Fab, that is, half the amount compared with other potent antibodies. Our study reveals a highly efficient and unusual mechanism of molecular recognition by an antibody. PubMed: 25698059DOI: 10.1038/ncomms7341 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (7 Å) |
Structure validation
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