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TitleHeterologous Prime-Boost with Immunologically Orthogonal Protein Nanoparticles for Peptide Immunofocusing.
Journal, issue, pagesbioRxiv, Year 2024
Publish dateFeb 26, 2024
AuthorsSonia Bhattacharya / Matthew C Jenkins / Parisa Keshavarz-Joud / Alisyn Retos Bourque / Keiyana White / Amina M Alvarez Barkane / Anton V Bryksin / Carolina Hernandez / Mykhailo Kopylov / M G Finn /
PubMed AbstractProtein nanoparticles are effective platforms for antigen presentation and targeting effector immune cells in vaccine development. Encapsulins are a class of protein-based microbial nanocompartments ...Protein nanoparticles are effective platforms for antigen presentation and targeting effector immune cells in vaccine development. Encapsulins are a class of protein-based microbial nanocompartments that self-assemble into icosahedral structures with external diameters ranging from 24 to 42 nm. Encapsulins from were designed to package bacterial RNA when produced in and were shown to have immunogenic and self-adjuvanting properties enhanced by this RNA. We genetically incorporated a 20-mer peptide derived from a mutant strain of the SARS-CoV-2 receptor binding domain (RBD) into the encapsulin protomeric coat protein for presentation on the exterior surface of the particle. This immunogen elicited conformationally-relevant humoral responses to the SARS-CoV-2 RBD. Immunological recognition was enhanced when the same peptide was presented in a heterologous prime/boost vaccination strategy using the engineered encapsulin and a previously reported variant of the PP7 virus-like particle, leading to the development of a selective antibody response against a SARS-CoV-2 RBD point mutant. While generating epitope-focused antibody responses is an interplay between inherent vaccine properties and B/T cells, here we demonstrate the use of orthogonal nanoparticles to fine-tune the control of epitope focusing.
External linksbioRxiv / PubMed:38464232 / PubMed Central
MethodsEM (single particle)
Resolution4.2 - 6.35 Å
Structure data

EMDB-43013: Myxococcus xanthus HEnc-K417N(A) protein shell with icosahedral T=1 symmetry
Method: EM (single particle) / Resolution: 4.91 Å

EMDB-43016: Myxococcus xanthus HEnc-K417N(A) protein shell with tetrahedral symmetry (12 pentamers, 4 hexamers)
Method: EM (single particle) / Resolution: 4.91 Å

EMDB-43037: Myxococcus xanthus HEnc-K417N(A) protein shell with D3 symmetry (12 pentamers, 3 hexamers)
Method: EM (single particle) / Resolution: 4.91 Å

EMDB-43038: Myxococcus xanthus HEnc-K417N(A) protein shell with D6 symmetry (12 pentamers, 8 hexamers)
Method: EM (single particle) / Resolution: 5.08 Å

EMDB-43039: Myxococcus xanthus HEnc-K417N(A) protein shell with C2 symmetry (12 pentamers, 9 hexamers)
Method: EM (single particle) / Resolution: 6.27 Å

EMDB-43040: Myxococcus xanthus HEnc-K417N(A) protein shell with D3 symmetry (12 pentamers, 11 hexamers)
Method: EM (single particle) / Resolution: 6.35 Å

EMDB-43041: Myxococcus xanthus HEnc-K417N(A) protein shell with D2 symmetry (12 pentamers, 12 hexamers)
Method: EM (single particle) / Resolution: 5.88 Å

EMDB-43042: Myxococcus xanthus HEnc-K417N(A) protein shell with D2 symmetry (12 pentamers, 14 hexamers)
Method: EM (single particle) / Resolution: 6.08 Å

EMDB-43043: Myxococcus xanthus HEnc-K417N(A) protein shell with D5 symmetry (12 pentamers, 15 hexamers)
Method: EM (single particle) / Resolution: 4.91 Å

EMDB-43113: Myxococcus xanthus EncA WT protein shell with icosahedral symmetry T=3
Method: EM (single particle) / Resolution: 4.2 Å

Source
  • Myxococcus xanthus (bacteria)

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