Vaccine based on folded receptor binding domain‐PreS fusion protein with potential to induce sterilizing immunity to SARS‐CoV‐2 variants

Background Severe acute respiratory syndrome coronavirus 2 (SARS‐CoV‐2) is responsible for the ongoing global COVID‐19 pandemic. One possibility to control the pandemic is to induce sterilizing immunity through the induction and maintenance of neutralizing antibodies preventing SARS‐CoV‐2 from enter...

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Published inAllergy (Copenhagen) Vol. 77; no. 8; pp. 2431 - 2445
Main Authors Gattinger, Pia, Kratzer, Bernhard, Tulaeva, Inna, Niespodziana, Katarzyna, Ohradanova‐Repic, Anna, Gebetsberger, Laura, Borochova, Kristina, Garner‐Spitzer, Erika, Trapin, Doris, Hofer, Gerhard, Keller, Walter, Baumgartner, Isabella, Tancevski, Ivan, Khaitov, Musa, Karaulov, Alexander, Stockinger, Hannes, Wiedermann, Ursula, Pickl, Winfried F., Valenta, Rudolf
Format Journal Article
LanguageEnglish
Published Denmark Blackwell Publishing Ltd 01.08.2022
Subjects
ACE2
Angiotensin-converting enzyme 2
Animals
Antibodies
Antibodies, Neutralizing
Antibodies, Viral
Antibody response
Binding sites
Coronaviruses
COVID-19
COVID-19 - prevention & control
COVID-19 vaccines
COVID-19 Vaccines - immunology
Fusion protein
Genotypes
Hepatitis B
Humans
Immunity
Immunoglobulin G
Mucosa
neutralizing antibodies
Pandemics
Pandemics - prevention & control
Proteins
Rabbits
SARS-CoV-2
Secretions
Severe acute respiratory syndrome coronavirus 2
Spike Glycoprotein, Coronavirus - immunology
Spike protein
sterilizing immunity
vaccine
Vaccines
Viruses
COVID-19
neutralizing antibodies
SARS-CoV-2
vaccine
antibody response
sterilizing immunity
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Abstract Background Severe acute respiratory syndrome coronavirus 2 (SARS‐CoV‐2) is responsible for the ongoing global COVID‐19 pandemic. One possibility to control the pandemic is to induce sterilizing immunity through the induction and maintenance of neutralizing antibodies preventing SARS‐CoV‐2 from entering human cells to replicate in. Methods We report the construction and in vitro and in vivo characterization of a SARS‐CoV‐2 subunit vaccine (PreS‐RBD) based on a structurally folded recombinant fusion protein consisting of two SARS‐CoV‐2 Spike protein receptor‐binding domains (RBD) fused to the N‐ and C‐terminus of hepatitis B virus (HBV) surface antigen PreS to enable the two unrelated proteins serving as immunologic carriers for each other. Results PreS‐RBD, but not RBD alone, induced a robust and uniform RBD‐specific IgG response in rabbits. Currently available genetic SARS‐CoV‐2 vaccines induce mainly transient IgG1 responses in vaccinated subjects whereas the PreS‐RBD vaccine induced RBD‐specific IgG antibodies consisting of an early IgG1 and sustained IgG4 antibody response in a SARS‐CoV‐2 naive subject. PreS‐RBD‐specific IgG antibodies were detected in serum and mucosal secretions, reacted with SARS‐CoV‐2 variants, including the omicron variant of concern and the HBV receptor‐binding sites on PreS of currently known HBV genotypes. PreS‐RBD‐specific antibodies of the immunized subject more potently inhibited the interaction of RBD with its human receptor ACE2 and their virus‐neutralizing titers (VNTs) were higher than median VNTs in a random sample of healthy subjects fully immunized with registered SARS‐CoV‐2 vaccines or in COVID‐19 convalescent subjects. Conclusion The PreS‐RBD vaccine has the potential to serve as a combination vaccine for inducing sterilizing immunity against SARS‐CoV‐2 and HBV by stopping viral replication through the inhibition of cellular virus entry. This study reports the design and characterization of a SARS‐CoV‐2 subunit vaccine (PreS‐RBD). PreS‐RBD, but not RBD alone, induces RBD‐specific IgG1 and long‐lasting IgG4 in serum and mucosal fluids, and cross‐reacts with SARS‐CoV‐2 variants of concern. PreS‐RBD‐specific antibodies of the immunized subject more potently inhibit the interaction of RBD with angiotensin converting enzyme 2 (ACE2), and their virus‐neutralizing titers are higher than median titers in a random sample of healthy subjects fully immunized with registered SARS‐CoV‐2 vaccines or in COVID‐19 convalescent subjects.Abbreviations: COVID‐19, coronavirus disease 2019; IgG, immunoglobulin G; HBV, hepatitis B virus; RBD, receptor‐binding domain; PreS, HVB domain; SARS‐CoV‐2, severe acute respiratory syndrome coronavirus 2
AbstractList BackgroundSevere acute respiratory syndrome coronavirus 2 (SARS‐CoV‐2) is responsible for the ongoing global COVID‐19 pandemic. One possibility to control the pandemic is to induce sterilizing immunity through the induction and maintenance of neutralizing antibodies preventing SARS‐CoV‐2 from entering human cells to replicate in.MethodsWe report the construction and in vitro and in vivo characterization of a SARS‐CoV‐2 subunit vaccine (PreS‐RBD) based on a structurally folded recombinant fusion protein consisting of two SARS‐CoV‐2 Spike protein receptor‐binding domains (RBD) fused to the N‐ and C‐terminus of hepatitis B virus (HBV) surface antigen PreS to enable the two unrelated proteins serving as immunologic carriers for each other.ResultsPreS‐RBD, but not RBD alone, induced a robust and uniform RBD‐specific IgG response in rabbits. Currently available genetic SARS‐CoV‐2 vaccines induce mainly transient IgG1 responses in vaccinated subjects whereas the PreS‐RBD vaccine induced RBD‐specific IgG antibodies consisting of an early IgG1 and sustained IgG4 antibody response in a SARS‐CoV‐2 naive subject. PreS‐RBD‐specific IgG antibodies were detected in serum and mucosal secretions, reacted with SARS‐CoV‐2 variants, including the omicron variant of concern and the HBV receptor‐binding sites on PreS of currently known HBV genotypes. PreS‐RBD‐specific antibodies of the immunized subject more potently inhibited the interaction of RBD with its human receptor ACE2 and their virus‐neutralizing titers (VNTs) were higher than median VNTs in a random sample of healthy subjects fully immunized with registered SARS‐CoV‐2 vaccines or in COVID‐19 convalescent subjects.ConclusionThe PreS‐RBD vaccine has the potential to serve as a combination vaccine for inducing sterilizing immunity against SARS‐CoV‐2 and HBV by stopping viral replication through the inhibition of cellular virus entry.
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is responsible for the ongoing global COVID-19 pandemic. One possibility to control the pandemic is to induce sterilizing immunity through the induction and maintenance of neutralizing antibodies preventing SARS-CoV-2 from entering human cells to replicate in. We report the construction and in vitro and in vivo characterization of a SARS-CoV-2 subunit vaccine (PreS-RBD) based on a structurally folded recombinant fusion protein consisting of two SARS-CoV-2 Spike protein receptor-binding domains (RBD) fused to the N- and C-terminus of hepatitis B virus (HBV) surface antigen PreS to enable the two unrelated proteins serving as immunologic carriers for each other. PreS-RBD, but not RBD alone, induced a robust and uniform RBD-specific IgG response in rabbits. Currently available genetic SARS-CoV-2 vaccines induce mainly transient IgG responses in vaccinated subjects whereas the PreS-RBD vaccine induced RBD-specific IgG antibodies consisting of an early IgG and sustained IgG antibody response in a SARS-CoV-2 naive subject. PreS-RBD-specific IgG antibodies were detected in serum and mucosal secretions, reacted with SARS-CoV-2 variants, including the omicron variant of concern and the HBV receptor-binding sites on PreS of currently known HBV genotypes. PreS-RBD-specific antibodies of the immunized subject more potently inhibited the interaction of RBD with its human receptor ACE2 and their virus-neutralizing titers (VNTs) were higher than median VNTs in a random sample of healthy subjects fully immunized with registered SARS-CoV-2 vaccines or in COVID-19 convalescent subjects. The PreS-RBD vaccine has the potential to serve as a combination vaccine for inducing sterilizing immunity against SARS-CoV-2 and HBV by stopping viral replication through the inhibition of cellular virus entry.
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is responsible for the ongoing global COVID-19 pandemic. One possibility to control the pandemic is to induce sterilizing immunity through the induction and maintenance of neutralizing antibodies preventing SARS-CoV-2 from entering human cells to replicate in.BACKGROUNDSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is responsible for the ongoing global COVID-19 pandemic. One possibility to control the pandemic is to induce sterilizing immunity through the induction and maintenance of neutralizing antibodies preventing SARS-CoV-2 from entering human cells to replicate in.We report the construction and in vitro and in vivo characterization of a SARS-CoV-2 subunit vaccine (PreS-RBD) based on a structurally folded recombinant fusion protein consisting of two SARS-CoV-2 Spike protein receptor-binding domains (RBD) fused to the N- and C-terminus of hepatitis B virus (HBV) surface antigen PreS to enable the two unrelated proteins serving as immunologic carriers for each other.METHODSWe report the construction and in vitro and in vivo characterization of a SARS-CoV-2 subunit vaccine (PreS-RBD) based on a structurally folded recombinant fusion protein consisting of two SARS-CoV-2 Spike protein receptor-binding domains (RBD) fused to the N- and C-terminus of hepatitis B virus (HBV) surface antigen PreS to enable the two unrelated proteins serving as immunologic carriers for each other.PreS-RBD, but not RBD alone, induced a robust and uniform RBD-specific IgG response in rabbits. Currently available genetic SARS-CoV-2 vaccines induce mainly transient IgG1 responses in vaccinated subjects whereas the PreS-RBD vaccine induced RBD-specific IgG antibodies consisting of an early IgG1 and sustained IgG4 antibody response in a SARS-CoV-2 naive subject. PreS-RBD-specific IgG antibodies were detected in serum and mucosal secretions, reacted with SARS-CoV-2 variants, including the omicron variant of concern and the HBV receptor-binding sites on PreS of currently known HBV genotypes. PreS-RBD-specific antibodies of the immunized subject more potently inhibited the interaction of RBD with its human receptor ACE2 and their virus-neutralizing titers (VNTs) were higher than median VNTs in a random sample of healthy subjects fully immunized with registered SARS-CoV-2 vaccines or in COVID-19 convalescent subjects.RESULTSPreS-RBD, but not RBD alone, induced a robust and uniform RBD-specific IgG response in rabbits. Currently available genetic SARS-CoV-2 vaccines induce mainly transient IgG1 responses in vaccinated subjects whereas the PreS-RBD vaccine induced RBD-specific IgG antibodies consisting of an early IgG1 and sustained IgG4 antibody response in a SARS-CoV-2 naive subject. PreS-RBD-specific IgG antibodies were detected in serum and mucosal secretions, reacted with SARS-CoV-2 variants, including the omicron variant of concern and the HBV receptor-binding sites on PreS of currently known HBV genotypes. PreS-RBD-specific antibodies of the immunized subject more potently inhibited the interaction of RBD with its human receptor ACE2 and their virus-neutralizing titers (VNTs) were higher than median VNTs in a random sample of healthy subjects fully immunized with registered SARS-CoV-2 vaccines or in COVID-19 convalescent subjects.The PreS-RBD vaccine has the potential to serve as a combination vaccine for inducing sterilizing immunity against SARS-CoV-2 and HBV by stopping viral replication through the inhibition of cellular virus entry.CONCLUSIONThe PreS-RBD vaccine has the potential to serve as a combination vaccine for inducing sterilizing immunity against SARS-CoV-2 and HBV by stopping viral replication through the inhibition of cellular virus entry.
Background Severe acute respiratory syndrome coronavirus 2 (SARS‐CoV‐2) is responsible for the ongoing global COVID‐19 pandemic. One possibility to control the pandemic is to induce sterilizing immunity through the induction and maintenance of neutralizing antibodies preventing SARS‐CoV‐2 from entering human cells to replicate in. Methods We report the construction and in vitro and in vivo characterization of a SARS‐CoV‐2 subunit vaccine (PreS‐RBD) based on a structurally folded recombinant fusion protein consisting of two SARS‐CoV‐2 Spike protein receptor‐binding domains (RBD) fused to the N‐ and C‐terminus of hepatitis B virus (HBV) surface antigen PreS to enable the two unrelated proteins serving as immunologic carriers for each other. Results PreS‐RBD, but not RBD alone, induced a robust and uniform RBD‐specific IgG response in rabbits. Currently available genetic SARS‐CoV‐2 vaccines induce mainly transient IgG1 responses in vaccinated subjects whereas the PreS‐RBD vaccine induced RBD‐specific IgG antibodies consisting of an early IgG1 and sustained IgG4 antibody response in a SARS‐CoV‐2 naive subject. PreS‐RBD‐specific IgG antibodies were detected in serum and mucosal secretions, reacted with SARS‐CoV‐2 variants, including the omicron variant of concern and the HBV receptor‐binding sites on PreS of currently known HBV genotypes. PreS‐RBD‐specific antibodies of the immunized subject more potently inhibited the interaction of RBD with its human receptor ACE2 and their virus‐neutralizing titers (VNTs) were higher than median VNTs in a random sample of healthy subjects fully immunized with registered SARS‐CoV‐2 vaccines or in COVID‐19 convalescent subjects. Conclusion The PreS‐RBD vaccine has the potential to serve as a combination vaccine for inducing sterilizing immunity against SARS‐CoV‐2 and HBV by stopping viral replication through the inhibition of cellular virus entry. This study reports the design and characterization of a SARS‐CoV‐2 subunit vaccine (PreS‐RBD). PreS‐RBD, but not RBD alone, induces RBD‐specific IgG1 and long‐lasting IgG4 in serum and mucosal fluids, and cross‐reacts with SARS‐CoV‐2 variants of concern. PreS‐RBD‐specific antibodies of the immunized subject more potently inhibit the interaction of RBD with angiotensin converting enzyme 2 (ACE2), and their virus‐neutralizing titers are higher than median titers in a random sample of healthy subjects fully immunized with registered SARS‐CoV‐2 vaccines or in COVID‐19 convalescent subjects.Abbreviations: COVID‐19, coronavirus disease 2019; IgG, immunoglobulin G; HBV, hepatitis B virus; RBD, receptor‐binding domain; PreS, HVB domain; SARS‐CoV‐2, severe acute respiratory syndrome coronavirus 2
Author Niespodziana, Katarzyna
Hofer, Gerhard
Karaulov, Alexander
Stockinger, Hannes
Ohradanova‐Repic, Anna
Tancevski, Ivan
Valenta, Rudolf
Gebetsberger, Laura
Khaitov, Musa
Baumgartner, Isabella
Tulaeva, Inna
Kratzer, Bernhard
Wiedermann, Ursula
Borochova, Kristina
Keller, Walter
Pickl, Winfried F.
Gattinger, Pia
Garner‐Spitzer, Erika
Trapin, Doris
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Issue 8
Keywords COVID-19
neutralizing antibodies
SARS-CoV-2
vaccine
antibody response
sterilizing immunity
Language English
License Attribution
2022 The Authors. Allergy published by European Academy of Allergy and Clinical Immunology and John Wiley & Sons Ltd.
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Notes Funding information
This study was supported by grants from Austrian Science Fund, Grant numbers: DK‐W1248 and P29398; Viravaxx AG; and Danube Allergy Research Cluster of Lower Austria, Grant number: 330950005. AOR and HS also acknowledge funding by the Austrian Science Fund (FWF, grant number P34253‐B). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
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Snippet Background Severe acute respiratory syndrome coronavirus 2 (SARS‐CoV‐2) is responsible for the ongoing global COVID‐19 pandemic. One possibility to control the...
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is responsible for the ongoing global COVID-19 pandemic. One possibility to control the pandemic...
BackgroundSevere acute respiratory syndrome coronavirus 2 (SARS‐CoV‐2) is responsible for the ongoing global COVID‐19 pandemic. One possibility to control the...
SourceID proquest
pubmed
crossref
wiley
SourceType Aggregation Database
Index Database
Enrichment Source
Publisher
StartPage 2431
SubjectTerms ACE2
Angiotensin-converting enzyme 2
Animals
Antibodies
Antibodies, Neutralizing
Antibodies, Viral
Antibody response
Binding sites
Coronaviruses
COVID-19
COVID-19 - prevention & control
COVID-19 vaccines
COVID-19 Vaccines - immunology
Fusion protein
Genotypes
Hepatitis B
Humans
Immunity
Immunoglobulin G
Mucosa
neutralizing antibodies
Pandemics
Pandemics - prevention & control
Proteins
Rabbits
SARS-CoV-2
Secretions
Severe acute respiratory syndrome coronavirus 2
Spike Glycoprotein, Coronavirus - immunology
Spike protein
sterilizing immunity
vaccine
Vaccines
Viruses
Title Vaccine based on folded receptor binding domain‐PreS fusion protein with potential to induce sterilizing immunity to SARS‐CoV‐2 variants
URI https://onlinelibrary.wiley.com/doi/abs/10.1111%2Fall.15305
https://www.ncbi.nlm.nih.gov/pubmed/35357709
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