Design, display and immunogenicity of HIV1 gp120 fragment immunogens on virus-like particles
•gp120 fragments with enhanced stability, affinity to CD4bs antibody b12 were designed.•Stabilized fragments were displayed on Qβ VLP’s and used in rabbit immunizations.•The most stable fragment elicited cross clade Tier 1 and weak Tier 2 neutralization.•Priming with the fragments resulted in an epi...
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Published in | Vaccine Vol. 36; no. 42; pp. 6345 - 6353 |
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Main Authors | , , , , , , , , , |
Format | Journal Article |
Language | English |
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08.10.2018
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Abstract | •gp120 fragments with enhanced stability, affinity to CD4bs antibody b12 were designed.•Stabilized fragments were displayed on Qβ VLP’s and used in rabbit immunizations.•The most stable fragment elicited cross clade Tier 1 and weak Tier 2 neutralization.•Priming with the fragments resulted in an epitope focused response to the CD4bs.
The broadly neutralizing antibody against HIV-1, b12, binds to the CD4 binding site (CD4bs) on the outer domain (OD) of the gp120 subunit of HIV-1 Env. We have previously reported the design of an E. coli expressed fragment of HIV-1 gp120, b122a, containing about 70% of the b12 epitope with the idea of focusing the immune response to this structure. Since the b122a structure was found to be only partially folded, as assessed by circular dichroism and protease resistance, we attempted to stabilize it by the introduction of additional disulfide bonds. One such mutant, b122a1-b showed increased stability and bound b12 with 30-fold greater affinity as compared to b122a. Various b122a and OD fragment proteins were displayed on the surface of Qβ virus-like particles. Sera raised against these particles in six-month long rabbit immunization studies could neutralize Tier1 viruses across different subtypes with the best results observed with b122a1-b displayed particles. Significantly higher amounts of antibodies directed towards the CD4bs were also elicited by particles displaying b122a1-b. This study highlights the ability of fragment immunogens to focus the antibody response to the conserved CD4bs of HIV-1. |
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AbstractList | The broadly neutralizing antibody against HIV-1, bl2, binds to the CD4 binding site (CD4bs) on the outer domain (OD) of the gp120 subunit of HIV-1 Env. We have previously reported the design of an
E.coli
expressed fragment of HIV-1 gp120, b122a, containing about 70% of the b12 epitope with the idea of focusing the immune response to this structure. Since the b122a structure was found to be only partially folded, as assessed by circular dichroism and protease resistance, we attempted to stabilize it by the introduction of additional disulfide bonds. One such mutant, b122al-b showed increased stability and bound bl2 with 30-fold greater affinity as compared to b122a. Various b122a and OD fragment proteins were displayed on the surface of Qβ virus-like particles. Sera raised against these particles in six-month long rabbit immunization studies could neutralize Tierl viruses across different subtypes with the best results observed with b122a1-b displayed particles. Significantly higher amounts of antibodies directed towards the CD4bs were also elicited by particles displaying b122a1-b. This study highlights the ability of fragment immunogens to focus the antibody response to the conserved CD4bs of HIV-1. The broadly neutralizing antibody against HIV-1, b12, binds to the CD4 binding site (CD4bs) on the outer domain (OD) of the gp120 subunit of HIV-1 Env. We have previously reported the design of an E. coli expressed fragment of HIV-1 gp120, b122a, containing about 70% of the b12 epitope with the idea of focusing the immune response to this structure. Since the b122a structure was found to be only partially folded, as assessed by circular dichroism and protease resistance, we attempted to stabilize it by the introduction of additional disulfide bonds. One such mutant, b122a1-b showed increased stability and bound b12 with 30-fold greater affinity as compared to b122a. Various b122a and OD fragment proteins were displayed on the surface of Qβ virus-like particles. Sera raised against these particles in six-month long rabbit immunization studies could neutralize Tier1 viruses across different subtypes with the best results observed with b122a1-b displayed particles. Significantly higher amounts of antibodies directed towards the CD4bs were also elicited by particles displaying b122a1-b. This study highlights the ability of fragment immunogens to focus the antibody response to the conserved CD4bs of HIV-1. •gp120 fragments with enhanced stability, affinity to CD4bs antibody b12 were designed.•Stabilized fragments were displayed on Qβ VLP’s and used in rabbit immunizations.•The most stable fragment elicited cross clade Tier 1 and weak Tier 2 neutralization.•Priming with the fragments resulted in an epitope focused response to the CD4bs. The broadly neutralizing antibody against HIV-1, b12, binds to the CD4 binding site (CD4bs) on the outer domain (OD) of the gp120 subunit of HIV-1 Env. We have previously reported the design of an E. coli expressed fragment of HIV-1 gp120, b122a, containing about 70% of the b12 epitope with the idea of focusing the immune response to this structure. Since the b122a structure was found to be only partially folded, as assessed by circular dichroism and protease resistance, we attempted to stabilize it by the introduction of additional disulfide bonds. One such mutant, b122a1-b showed increased stability and bound b12 with 30-fold greater affinity as compared to b122a. Various b122a and OD fragment proteins were displayed on the surface of Qβ virus-like particles. Sera raised against these particles in six-month long rabbit immunization studies could neutralize Tier1 viruses across different subtypes with the best results observed with b122a1-b displayed particles. Significantly higher amounts of antibodies directed towards the CD4bs were also elicited by particles displaying b122a1-b. This study highlights the ability of fragment immunogens to focus the antibody response to the conserved CD4bs of HIV-1. |
Author | Pokorski, Jonathan K. Bhattacharyya, Sanchari Varadarajan, Raghavan Purwar, Mansi DeStefano, Joanne Arendt, Heather Montefiori, David C. La Branche, Celia C. Finn, M.G. Singh, Pranveer |
AuthorAffiliation | 1 Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India 560012 4 Department of Surgery, Duke University Medical Center, Durham, NC, USA 2 Department of Chemistry and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, CA 92037, USA 3 International AIDS Vaccine Initiative, Brooklyn, NY 11226, USA |
AuthorAffiliation_xml | – name: 1 Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India 560012 – name: 3 International AIDS Vaccine Initiative, Brooklyn, NY 11226, USA – name: 2 Department of Chemistry and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, CA 92037, USA – name: 4 Department of Surgery, Duke University Medical Center, Durham, NC, USA |
Author_xml | – sequence: 1 givenname: Mansi surname: Purwar fullname: Purwar, Mansi organization: Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India – sequence: 2 givenname: Jonathan K. surname: Pokorski fullname: Pokorski, Jonathan K. organization: Department of Chemistry and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, CA 92037, USA – sequence: 3 givenname: Pranveer surname: Singh fullname: Singh, Pranveer organization: Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India – sequence: 4 givenname: Sanchari surname: Bhattacharyya fullname: Bhattacharyya, Sanchari organization: Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India – sequence: 5 givenname: Heather surname: Arendt fullname: Arendt, Heather organization: International AIDS Vaccine Initiative, Brooklyn, NY 11226, USA – sequence: 6 givenname: Joanne surname: DeStefano fullname: DeStefano, Joanne organization: International AIDS Vaccine Initiative, Brooklyn, NY 11226, USA – sequence: 7 givenname: Celia C. surname: La Branche fullname: La Branche, Celia C. organization: Department of Surgery, Duke University Medical Center, Durham, NC, USA – sequence: 8 givenname: David C. surname: Montefiori fullname: Montefiori, David C. organization: Department of Surgery, Duke University Medical Center, Durham, NC, USA – sequence: 9 givenname: M.G. surname: Finn fullname: Finn, M.G. email: mgfinn@gatech.edu organization: Department of Chemistry and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, CA 92037, USA – sequence: 10 givenname: Raghavan surname: Varadarajan fullname: Varadarajan, Raghavan email: varadar@mbu.iisc.ernet.in organization: Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India |
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CitedBy_id | crossref_primary_10_1002_cbic_202100607 crossref_primary_10_1002_wnan_1681 crossref_primary_10_3390_vaccines9020074 crossref_primary_10_1021_jacs_1c05090 |
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Keywords | PBS RU PBSB Neutralizing antibodies Protein stability Vaccine CD4bs MODIP Env CP Immune focusing Nanoparticles VLPs SPR OD PBST RLU Cys SMCC ELISA |
Language | English |
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Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Current address: Department of Zoology, Mahatma Gandhi Central University Bihar, Motihari-845401, Bihar, India Current address: School of Chemistry & Biochemistry, Georgia Institute of Technology, 901 Atlantic Drive, Atlanta, Georgia 30332, USA SB and RV designed the immunogens; SB and PS carried out the biophysical characterization and SPR studies of the immunogens; JKP and MGF were responsible for production and characterization of Qβ VLP’s displaying fragment immunogens; HA and JDS planned the immunization studies; DCM, CC and MP were responsible for neutralization assays; MP also determined ELISA titers against priming immunogens, competition binding experiments and in vivo stability experiments; MP, RV JKP and MGF wrote the manuscript. Current address: Department of Macromolecular Science and Engineering, Case Western Reserve University, Case School of Engineering, Cleveland, Ohio 44106, USA Author Contributions |
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fullname: Yang |
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Snippet | •gp120 fragments with enhanced stability, affinity to CD4bs antibody b12 were designed.•Stabilized fragments were displayed on Qβ VLP’s and used in rabbit... The broadly neutralizing antibody against HIV-1, b12, binds to the CD4 binding site (CD4bs) on the outer domain (OD) of the gp120 subunit of HIV-1 Env. We have... The broadly neutralizing antibody against HIV-1, bl2, binds to the CD4 binding site (CD4bs) on the outer domain (OD) of the gp120 subunit of HIV-1 Env. We have... |
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SubjectTerms | Animals Antibodies Antibodies, Neutralizing - immunology Antibody response Antigens Binding Sites CD4 antigen CD4 Antigens - metabolism Circular dichroism Competition Design Dichroism Displays Disulfide bonds E coli Epitopes Escherichia coli - metabolism Fragmentation Glycoprotein gp120 Glycoproteins HIV HIV Envelope Protein gp120 - immunology HIV Envelope Protein gp120 - metabolism Human immunodeficiency virus Immune focusing Immune response Immune system Immunization Immunogenicity Immunoglobulins Ligands Mutation Nanoparticles Nanoparticles - chemistry Neutralizing antibodies Polypeptides Protein Stability Proteins Rabbits Surface Plasmon Resonance Vaccine Vaccines Virus-like particles Viruses |
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Title | Design, display and immunogenicity of HIV1 gp120 fragment immunogens on virus-like particles |
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