Transplantation of a quaternary structure neutralizing antibody epitope from dengue virus serotype 3 into serotype 4
Dengue vaccine trials have revealed deficits in our understanding of the mechanisms of protective immunity, demonstrating a need to measure epitope-specific antibody responses against each DENV serotype. HmAb 5J7 binds to a complex, 3-monomer spanning quaternary epitope in the DENV3 envelope (E) pro...
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| creator | Widman, Douglas G. Young, Ellen Nivarthi, Usha Swanstrom, Jesica A. Royal, Scott R. Yount, Boyd L. Debbink, Kari Begley, Matthew Marcet, Stephanie Durbin, Anna de Silva, Aravinda M. Messer, William B. Baric, Ralph S. |
| description | Dengue vaccine trials have revealed deficits in our understanding of the mechanisms of protective immunity, demonstrating a need to measure epitope-specific antibody responses against each DENV serotype. HmAb 5J7 binds to a complex, 3-monomer spanning quaternary epitope in the DENV3 envelope (E) protein, but it is unclear whether all interactions are needed for neutralization. Structure guided design and reverse genetics were used to sequentially transplant larger portions of the DENV3-specific 5J7 mAb epitope into dengue virus serotype 4 (DENV4). We observed complete binding and neutralization only when the entire 3 monomer spanning epitope was transplanted into DENV4, providing empirical proof that cooperative monomer-hmAb 5J7 interactions maximize activity. The rDENV4/3 virus containing the most expanded 5J7 epitope was also significantly more sensitive than WT DENV4 to neutralization by DENV3 primary immune sera. We conclude that the hinge-spanning region of the 5J7 quaternary epitope is a target for serotype-specific neutralizing antibodies after DENV3 infection. |
| doi_str_mv | 10.1038/s41598-017-17355-5 |
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HmAb 5J7 binds to a complex, 3-monomer spanning quaternary epitope in the DENV3 envelope (E) protein, but it is unclear whether all interactions are needed for neutralization. Structure guided design and reverse genetics were used to sequentially transplant larger portions of the DENV3-specific 5J7 mAb epitope into dengue virus serotype 4 (DENV4). We observed complete binding and neutralization only when the entire 3 monomer spanning epitope was transplanted into DENV4, providing empirical proof that cooperative monomer-hmAb 5J7 interactions maximize activity. The rDENV4/3 virus containing the most expanded 5J7 epitope was also significantly more sensitive than WT DENV4 to neutralization by DENV3 primary immune sera. We conclude that the hinge-spanning region of the 5J7 quaternary epitope is a target for serotype-specific neutralizing antibodies after DENV3 infection.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/s41598-017-17355-5</identifier><identifier>PMID: 29215033</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>13/1 ; 45/77 ; 45/91 ; 631/250/590 ; 631/337 ; 692/699/255/2514 ; Amino Acid Sequence ; Animals ; Antibodies, Monoclonal - chemistry ; Antibodies, Monoclonal - genetics ; Antibodies, Monoclonal - immunology ; Antibodies, Neutralizing - chemistry ; Antibodies, Neutralizing - genetics ; Antibodies, Neutralizing - immunology ; Antibodies, Viral - chemistry ; Antibodies, Viral - genetics ; Antibodies, Viral - immunology ; Antisera ; Chlorocebus aethiops ; Dengue - immunology ; Dengue - virology ; Dengue fever ; Dengue Virus - classification ; Dengue Virus - genetics ; Dengue Virus - immunology ; Epitopes ; Epitopes - immunology ; Genetics ; Humanities and Social Sciences ; Humans ; Monoclonal antibodies ; multidisciplinary ; Neutralization ; Neutralization Tests ; Protein structure ; Protein Structure, Quaternary ; Quaternary structure ; Science ; Science (multidisciplinary) ; Sequence Homology ; Serogroup ; Transplantation ; Transplants & implants ; U937 Cells ; Vector-borne diseases ; Vero Cells ; Viral Envelope Proteins - immunology</subject><ispartof>Scientific reports, 2017-12, Vol.7 (1), p.17169-10, Article 17169</ispartof><rights>The Author(s) 2017</rights><rights>2017. 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HmAb 5J7 binds to a complex, 3-monomer spanning quaternary epitope in the DENV3 envelope (E) protein, but it is unclear whether all interactions are needed for neutralization. Structure guided design and reverse genetics were used to sequentially transplant larger portions of the DENV3-specific 5J7 mAb epitope into dengue virus serotype 4 (DENV4). We observed complete binding and neutralization only when the entire 3 monomer spanning epitope was transplanted into DENV4, providing empirical proof that cooperative monomer-hmAb 5J7 interactions maximize activity. The rDENV4/3 virus containing the most expanded 5J7 epitope was also significantly more sensitive than WT DENV4 to neutralization by DENV3 primary immune sera. 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immunology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Widman, Douglas G.</creatorcontrib><creatorcontrib>Young, Ellen</creatorcontrib><creatorcontrib>Nivarthi, Usha</creatorcontrib><creatorcontrib>Swanstrom, Jesica A.</creatorcontrib><creatorcontrib>Royal, Scott R.</creatorcontrib><creatorcontrib>Yount, Boyd L.</creatorcontrib><creatorcontrib>Debbink, Kari</creatorcontrib><creatorcontrib>Begley, Matthew</creatorcontrib><creatorcontrib>Marcet, Stephanie</creatorcontrib><creatorcontrib>Durbin, Anna</creatorcontrib><creatorcontrib>de Silva, Aravinda M.</creatorcontrib><creatorcontrib>Messer, William B.</creatorcontrib><creatorcontrib>Baric, Ralph S.</creatorcontrib><collection>Springer Nature OA/Free Journals</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Widman, Douglas G.</au><au>Young, Ellen</au><au>Nivarthi, Usha</au><au>Swanstrom, Jesica A.</au><au>Royal, Scott R.</au><au>Yount, Boyd L.</au><au>Debbink, Kari</au><au>Begley, Matthew</au><au>Marcet, Stephanie</au><au>Durbin, Anna</au><au>de Silva, Aravinda M.</au><au>Messer, William B.</au><au>Baric, Ralph S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Transplantation of a quaternary structure neutralizing antibody epitope from dengue virus serotype 3 into serotype 4</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2017-12-07</date><risdate>2017</risdate><volume>7</volume><issue>1</issue><spage>17169</spage><epage>10</epage><pages>17169-10</pages><artnum>17169</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>Dengue vaccine trials have revealed deficits in our understanding of the mechanisms of protective immunity, demonstrating a need to measure epitope-specific antibody responses against each DENV serotype. HmAb 5J7 binds to a complex, 3-monomer spanning quaternary epitope in the DENV3 envelope (E) protein, but it is unclear whether all interactions are needed for neutralization. Structure guided design and reverse genetics were used to sequentially transplant larger portions of the DENV3-specific 5J7 mAb epitope into dengue virus serotype 4 (DENV4). We observed complete binding and neutralization only when the entire 3 monomer spanning epitope was transplanted into DENV4, providing empirical proof that cooperative monomer-hmAb 5J7 interactions maximize activity. The rDENV4/3 virus containing the most expanded 5J7 epitope was also significantly more sensitive than WT DENV4 to neutralization by DENV3 primary immune sera. We conclude that the hinge-spanning region of the 5J7 quaternary epitope is a target for serotype-specific neutralizing antibodies after DENV3 infection.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>29215033</pmid><doi>10.1038/s41598-017-17355-5</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0001-5724-0644</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | 13/1 45/77 45/91 631/250/590 631/337 692/699/255/2514 Amino Acid Sequence Animals Antibodies, Monoclonal - chemistry Antibodies, Monoclonal - genetics Antibodies, Monoclonal - immunology Antibodies, Neutralizing - chemistry Antibodies, Neutralizing - genetics Antibodies, Neutralizing - immunology Antibodies, Viral - chemistry Antibodies, Viral - genetics Antibodies, Viral - immunology Antisera Chlorocebus aethiops Dengue - immunology Dengue - virology Dengue fever Dengue Virus - classification Dengue Virus - genetics Dengue Virus - immunology Epitopes Epitopes - immunology Genetics Humanities and Social Sciences Humans Monoclonal antibodies multidisciplinary Neutralization Neutralization Tests Protein structure Protein Structure, Quaternary Quaternary structure Science Science (multidisciplinary) Sequence Homology Serogroup Transplantation Transplants & implants U937 Cells Vector-borne diseases Vero Cells Viral Envelope Proteins - immunology |
| title | Transplantation of a quaternary structure neutralizing antibody epitope from dengue virus serotype 3 into serotype 4 |
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