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7P56

Variant Surface Glycoprotein 2 (VSG2, MiTat1.2, VSG221) Bound to Calcium

Summary for 7P56
Entry DOI10.2210/pdb7p56/pdb
Related7P57 7P59 7P5A 7P5B 7P5D
DescriptorVariant surface glycoprotein MITAT 1.2, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
Functional Keywordsvariant surface glycoprotein, vsg coat, trypanosoma brucei, immune evasion, african trypanosome, calcium, metal binding, membrane protein
Biological sourceTrypanosoma brucei brucei
Total number of polymer chains2
Total formula weight103620.24
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: 2024-02-07)
Primary citationGkeka, 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: 36943866
DOI: 10.1016/j.celrep.2023.112262
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.735 Å)
Structure validation

226707

數據於2024-10-30公開中

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