7P57
VSG2 mutant structure lacking the calcium binding pocket
Summary for 7P57
| Entry DOI | 10.2210/pdb7p57/pdb |
| Related | 1VSG 7P56 7P59 7P5A 7P5B 7P5D |
| Descriptor | Variant surface glycoprotein MITAT 1.2, alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
| Functional Keywords | variant surface glycoprotein, coat, trypanosoma brucei, african trypanosome, immune evasion, antigenic variation, calcium binding, calcium, membrane protein |
| Biological source | Trypanosoma brucei brucei |
| Total number of polymer chains | 1 |
| Total formula weight | 51720.07 |
| Authors | Gkeka, A.,Aresta-Branco, F.,Stebbins, C.E.,Papavasiliou, F.N. (deposition date: 2021-07-14, release date: 2022-07-27, Last modification date: 2024-11-13) |
| Primary citation | Gkeka, A.,Aresta-Branco, F.,Triller, G.,Vlachou, E.P.,van Straaten, M.,Lilic, M.,Olinares, P.D.B.,Perez, K.,Chait, B.T.,Blatnik, R.,Ruppert, T.,Verdi, J.P.,Stebbins, C.E.,Papavasiliou, F.N. Immunodominant surface epitopes power immune evasion in the African trypanosome. Cell Rep, 42:112262-112262, 2023 Cited by PubMed Abstract: The African trypanosome survives the immune response of its mammalian host by antigenic variation of its major surface antigen (the variant surface glycoprotein or VSG). Here we describe the antibody repertoires elicited by different VSGs. We show that the repertoires are highly restricted and are directed predominantly to distinct epitopes on the surface of the VSGs. They are also highly discriminatory; minor alterations within these exposed epitopes confer antigenically distinct properties to these VSGs and elicit different repertoires. We propose that the patterned and repetitive nature of the VSG coat focuses host immunity to a restricted set of immunodominant epitopes per VSG, eliciting a highly stereotyped response, minimizing cross-reactivity between different VSGs and facilitating prolonged immune evasion through epitope variation. PubMed: 36943866DOI: 10.1016/j.celrep.2023.112262 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.961 Å) |
Structure validation
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