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Antigen- and scaffold-specific antibody responses to protein nanoparticle immunogens.
Kraft, John C; Pham, Minh N; Shehata, Laila; Brinkkemper, Mitch; Boyoglu-Barnum, Seyhan; Sprouse, Kaitlin R; Walls, Alexandra C; Cheng, Suna; Murphy, Mike; Pettie, Deleah; Ahlrichs, Maggie; Sydeman, Claire; Johnson, Max; Blackstone, Alyssa; Ellis, Daniel; Ravichandran, Rashmi; Fiala, Brooke; Wrenn, Samuel; Miranda, Marcos; Sliepen, Kwinten; Brouwer, Philip J M; Antanasijevic, Aleksandar; Veesler, David; Ward, Andrew B; Kanekiyo, Masaru; Pepper, Marion; Sanders, Rogier W; King, Neil P.
  • Kraft JC; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA; Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
  • Pham MN; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA; Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
  • Shehata L; Department of Immunology, University of Washington, Seattle, WA 98195, USA.
  • Brinkkemper M; Department of Medical Microbiology, Amsterdam UMC, University of Amsterdam, Amsterdam Infection and Immunity Institute, 1105 AZ Amsterdam, the Netherlands.
  • Boyoglu-Barnum S; Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
  • Sprouse KR; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.
  • Walls AC; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA; Howard Hughes Medical Institute, Seattle, WA 98195, USA.
  • Cheng S; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA; Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
  • Murphy M; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA; Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
  • Pettie D; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA; Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
  • Ahlrichs M; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA; Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
  • Sydeman C; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA; Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
  • Johnson M; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA; Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
  • Blackstone A; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA; Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
  • Ellis D; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA; Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
  • Ravichandran R; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA; Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
  • Fiala B; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA; Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
  • Wrenn S; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA; Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
  • Miranda M; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA; Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
  • Sliepen K; Department of Medical Microbiology, Amsterdam UMC, University of Amsterdam, Amsterdam Infection and Immunity Institute, 1105 AZ Amsterdam, the Netherlands.
  • Brouwer PJM; Department of Medical Microbiology, Amsterdam UMC, University of Amsterdam, Amsterdam Infection and Immunity Institute, 1105 AZ Amsterdam, the Netherlands.
  • Antanasijevic A; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
  • Veesler D; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA; Howard Hughes Medical Institute, Seattle, WA 98195, USA.
  • Ward AB; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
  • Kanekiyo M; Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
  • Pepper M; Department of Immunology, University of Washington, Seattle, WA 98195, USA.
  • Sanders RW; Department of Medical Microbiology, Amsterdam UMC, University of Amsterdam, Amsterdam Infection and Immunity Institute, 1105 AZ Amsterdam, the Netherlands; Department of Microbiology and Immunology, Weill Medical College of Cornell University, New York, NY 10021, USA.
  • King NP; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA; Institute for Protein Design, University of Washington, Seattle, WA 98195, USA. Electronic address: neil@ipd.uw.edu.
Cell Rep Med ; 3(10): 100780, 2022 10 18.
Article in English | MEDLINE | ID: covidwho-2267177
ABSTRACT
Protein nanoparticle scaffolds are increasingly used in next-generation vaccine designs, and several have established records of clinical safety and efficacy. Yet the rules for how immune responses specific to nanoparticle scaffolds affect the immunogenicity of displayed antigens have not been established. Here we define relationships between anti-scaffold and antigen-specific antibody responses elicited by protein nanoparticle immunogens. We report that dampening anti-scaffold responses by physical masking does not enhance antigen-specific antibody responses. In a series of immunogens that all use the same nanoparticle scaffold but display four different antigens, only HIV-1 envelope glycoprotein (Env) is subdominant to the scaffold. However, we also demonstrate that scaffold-specific antibody responses can competitively inhibit antigen-specific responses when the scaffold is provided in excess. Overall, our results suggest that anti-scaffold antibody responses are unlikely to suppress antigen-specific antibody responses for protein nanoparticle immunogens in which the antigen is immunodominant over the scaffold.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Vaccines / HIV-1 / Nanoparticles Type of study: Prognostic study Topics: Vaccines Language: English Journal: Cell Rep Med Year: 2022 Document Type: Article Affiliation country: J.xcrm.2022.100780

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Vaccines / HIV-1 / Nanoparticles Type of study: Prognostic study Topics: Vaccines Language: English Journal: Cell Rep Med Year: 2022 Document Type: Article Affiliation country: J.xcrm.2022.100780