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4ETQ

Vaccinia virus D8L IMV envelope protein in complex with Fab of murine IgG2a LA5

Summary for 4ETQ
Entry DOI10.2210/pdb4etq/pdb
Related4E9O 4EBQ
Descriptoranti-vaccinia D8L antigen murine monoclonal IgG2a antibody LA5, heavy chain, anti-vaccinia D8L antigen murine monoclonal IgG2a antibody LA5, light chain, IMV membrane protein, ... (8 entities in total)
Functional Keywordsvariable domain, constant domain, igg2a, igg domain, cdr, hypervariable region, neutralizing antibody, beta sheet, carbonic anhydrase fold, loose knot, chondroitin-sulfate binding site, delta 262, immune system-viral protein complex, immune system/viral protein
Biological sourceMus musculus
More
Total number of polymer chains6
Total formula weight157827.42
Authors
Matho, M.H.,Zajonc, D.M. (deposition date: 2012-04-24, release date: 2012-06-06, Last modification date: 2024-11-20)
Primary citationMatho, M.H.,Maybeno, M.,Benhnia, M.R.,Becker, D.,Meng, X.,Xiang, Y.,Crotty, S.,Peters, B.,Zajonc, D.M.
Structural and Biochemical Characterization of the Vaccinia Virus Envelope Protein D8 and Its Recognition by the Antibody LA5.
J.Virol., 86:8050-8058, 2012
Cited by
PubMed Abstract: Smallpox vaccine is considered a gold standard of vaccines, as it is the only one that has led to the complete eradication of an infectious disease from the human population. B cell responses are critical for the protective immunity induced by the vaccine, yet their targeted epitopes recognized in humans remain poorly described. Here we describe the biochemical and structural characterization of one of the immunodominant vaccinia virus (VACV) antigens, D8, and its binding to the monoclonal antibody LA5, which is capable of neutralizing VACV in the presence of complement. The full-length D8 ectodomain was found to form a tetramer. We determined the crystal structure of the LA5 Fab-monomeric D8 complex at a resolution of 2.1 Å, as well as the unliganded structures of D8 and LA5-Fab at resolutions of 1.42 Å and 1.6 Å, respectively. D8 features a carbonic anhydrase (CAH) fold that has evolved to bind to the glycosaminoglycan (GAG) chondroitin sulfate (CS) on host cells. The central positively charged crevice of D8 was predicted to be the CS binding site by automated docking experiments. Furthermore, sequence alignment of various poxvirus D8 orthologs revealed that this crevice is structurally conserved. The D8 epitope is formed by 23 discontinuous residues that are spread across 80% of the D8 protein sequence. Interestingly, LA5 binds with a high-affinity lock-and-key mechanism above this crevice with an unusually large antibody-antigen interface, burying 2,434 Å(2) of protein surface.
PubMed: 22623786
DOI: 10.1128/JVI.00836-12
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

238895

數據於2025-07-16公開中

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