7O4W
Crystal structure of diphtheria toxin mutant CRM197 with a disulphide bond replaced by a Cys-Acetone-Cys bridge
Summary for 7O4W
| Entry DOI | 10.2210/pdb7o4w/pdb |
| Descriptor | Diphtheria toxin, 1-hydroxypropan-2-one, 1,2-ETHANEDIOL, ... (6 entities in total) |
| Functional Keywords | diphtheria toxin, mutant, disulphide bridge, modified disulphide bridge, acetone., toxin |
| Biological source | Corynebacterium diphtheriae |
| Total number of polymer chains | 1 |
| Total formula weight | 59103.09 |
| Authors | Veggi, D.,Dello Iacono, L. (deposition date: 2021-04-07, release date: 2022-04-06, Last modification date: 2024-01-31) |
| Primary citation | Carboni, F.,Kitowski, A.,Sorieul, C.,Veggi, D.,Marques, M.C.,Oldrini, D.,Balducci, E.,Brogioni, B.,Del Bino, L.,Corrado, A.,Angiolini, F.,Dello Iacono, L.,Margarit, I.,Romano, M.R.,Bernardes, G.J.L.,Adamo, R. Retaining the structural integrity of disulfide bonds in diphtheria toxoid carrier protein is crucial for the effectiveness of glycoconjugate vaccine candidates. Chem Sci, 13:2440-2449, 2022 Cited by PubMed Abstract: The introduction of glycoconjugate vaccines marks an important point in the fight against various infectious diseases. The covalent conjugation of relevant polysaccharide antigens to immunogenic carrier proteins enables the induction of a long-lasting and robust IgG antibody response, which is not observed for pure polysaccharide vaccines. Although there has been remarkable progress in the development of glycoconjugate vaccines, many crucial parameters remain poorly understood. In particular, the influence of the conjugation site and strategy on the immunogenic properties of the final glycoconjugate vaccine is the focus of intense research. Here, we present a comparison of two cysteine selective conjugation strategies, elucidating the impact of both modifications on the structural integrity of the carrier protein, as well as on the immunogenic properties of the resulting glycoconjugate vaccine candidates. Our work suggests that conjugation chemistries impairing structurally relevant elements of the protein carrier, such as disulfide bonds, can have a dramatic effect on protein immunogenicity. PubMed: 35310500DOI: 10.1039/d1sc01928g PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.03002061079 Å) |
Structure validation
Download full validation report
