PREFUSION STABILIZED EBV GB MUTATIONS AND USES THEREOF
We have generated a 3D model of the glycoprotein B (gB) of Epstein-Barr virus (EBV) to design candidate stabilizing mutations that increase the stability of the prefusion state essential for an effective EBV gB based vaccine. Provided herein are engineered polypeptides derived from the EBV gB, which include an altered EBV gB ectodomain that has modifications relative to the native EBV gB ectodomain that stabilize a prefusion conformation of the polypeptides. In various aspects, the modifications are amino acid substitutions to generate pairs of cysteine amino acid residues, preferably positioned to connect different domains of the polypeptide or different copies of the polypeptide in a trimeric or multimeric conformation via formation of disulfide bonds during protein expression. In additional aspects, the modifications and/or the engineered polypeptides do not contain pairs of cysteine amino acid residues that may form disulfide bonds in a postfusion conformation..
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Patent| Erscheinungsjahr: |
2024 |
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| Erschienen: |
2024 |
| Enthalten in: |
Europäisches Patentamt - (2024) vom: 04. Jan. Zur Gesamtaufnahme - year:2024 |
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| Sprache: |
Englisch |
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| Beteiligte Personen: |
PRICE JASON [VerfasserIn] |
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| Links: |
Volltext [kostenfrei] |
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| Themen: |
Sonstige Themen: |
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| Anmerkungen: |
Source: www.epo.org (no modifications made), First posted: 2024-01-04, Last update posted on www.tib.eu: 2024-02-06, Last updated: 2024-02-09 |
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| Patentnummer: |
WO2024006930 |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
EPA019010796 |
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| 520 | |a We have generated a 3D model of the glycoprotein B (gB) of Epstein-Barr virus (EBV) to design candidate stabilizing mutations that increase the stability of the prefusion state essential for an effective EBV gB based vaccine. Provided herein are engineered polypeptides derived from the EBV gB, which include an altered EBV gB ectodomain that has modifications relative to the native EBV gB ectodomain that stabilize a prefusion conformation of the polypeptides. In various aspects, the modifications are amino acid substitutions to generate pairs of cysteine amino acid residues, preferably positioned to connect different domains of the polypeptide or different copies of the polypeptide in a trimeric or multimeric conformation via formation of disulfide bonds during protein expression. In additional aspects, the modifications and/or the engineered polypeptides do not contain pairs of cysteine amino acid residues that may form disulfide bonds in a postfusion conformation. | ||
| 650 | 4 | |a A61K: Preparations for medical, dental, or toilet purposes (devices or methods specially adapted for bringing pharmaceutical products into particular physical or administering forms a61j0003000000;chemical aspects of, or use of materials for deodorisation of air, for disinfection or sterilisation, or for bandages, dressings, absorbent pads or surgical articles a61l; soap compositions c11d) | |
| 650 | 4 | |a C07K: Peptides (peptides containing β-lactam rings c07d;cyclic dipeptides not having in their molecule any other peptide link than those which form their ring, e.g. piperazine-2,5-diones, c07d;ergot alkaloids of the cyclic peptide type c07d0519020000; single cell proteins, enzymes c12n;genetic engineering processes for obtaining peptides c12n0015000000) | |
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