Construction and next-generation sequencing analysis of a large phage-displayed VNAR single-domain antibody library from six naïve nurse sharks.
Identifieur interne : 000680 ( PubMed/Curation ); précédent : 000679; suivant : 000681Construction and next-generation sequencing analysis of a large phage-displayed VNAR single-domain antibody library from six naïve nurse sharks.
Auteurs : Mingqian Feng [États-Unis] ; Hejiao Bian [États-Unis] ; Xiaolin Wu [États-Unis] ; Tianyun Fu [États-Unis] ; Ying Fu [États-Unis] ; Jessica Hong [États-Unis] ; Bryan D. Fleming [États-Unis] ; Martin F. Flajnik [États-Unis] ; Mitchell Ho [États-Unis]Source :
- Antibody therapeutics [ 2516-4236 ] ; 2019.
Abstract
Background: Shark new antigen receptor variable domain (VNAR) antibodies can bind restricted epitopes that may be inaccessible to conventional antibodies. Methods: Here, we developed a library construction method based on polymerase chain reaction (PCR)-Extension Assembly and Self-Ligation (named "EASeL") to construct a large VNAR antibody library with a size of 1.2 × 1010 from six naïve adult nurse sharks (Ginglymostoma cirratum). Results: The next-generation sequencing analysis of 1.19 million full-length VNARs revealed that this library is highly diversified because it covers all four classical VNAR types (Types I-IV) including 11% of classical Type I and 57% of classical Type II. About 30% of the total VNARs could not be categorized as any of the classical types. The high variability of complementarity determining region (CDR) 3 length and cysteine numbers are important for the diversity of VNARs. To validate the use of the shark VNAR library for antibody discovery, we isolated a panel of VNAR phage binders to cancer therapy-related antigens, including glypican-3, human epidermal growth factor receptor 2 (HER2), and programmed cell death-1 (PD1). Additionally, we identified binders to viral antigens that included the Middle East respiratory syndrome (MERS) and severe acute respiratory syndrome (SARS) spike proteins. The isolated shark single-domain antibodies including Type I and Type II VNARs were produced in Escherichia coli and validated for their antigen binding. A Type II VNAR (PE38-B6) has a high affinity (Kd = 10.1 nM) for its antigen. Conclusions: The naïve nurse shark VNAR library is a useful source for isolating single-domain antibodies to a wide range of antigens. The EASeL method may be applicable to the construction of other large diversity gene expression libraries.
DOI: 10.1093/abt/tby011
PubMed: 30627698
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single-domain antibody library from six naïve nurse sharks.</title>
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<series><title level="j">Antibody therapeutics</title>
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<front><div type="abstract" xml:lang="en"><b>Background:</b>
Shark new antigen receptor variable domain (V<sub>NAR</sub>
) antibodies can bind restricted epitopes that may be inaccessible to conventional antibodies. <b>Methods:</b>
Here, we developed a library construction method based on polymerase chain reaction (PCR)-Extension Assembly and Self-Ligation (named "EASeL") to construct a large V<sub>NAR</sub>
antibody library with a size of 1.2 × 10<sup>10</sup>
from six naïve adult nurse sharks (<i>Ginglymostoma cirratum</i>
). <b>Results:</b>
The next-generation sequencing analysis of 1.19 million full-length V<sub>NAR</sub>
s revealed that this library is highly diversified because it covers all four classical V<sub>NAR</sub>
types (Types I-IV) including 11% of classical Type I and 57% of classical Type II. About 30% of the total V<sub>NAR</sub>
s could not be categorized as any of the classical types. The high variability of complementarity determining region (CDR) 3 length and cysteine numbers are important for the diversity of V<sub>NAR</sub>
s. To validate the use of the shark V<sub>NAR</sub>
library for antibody discovery, we isolated a panel of V<sub>NAR</sub>
phage binders to cancer therapy-related antigens, including glypican-3, human epidermal growth factor receptor 2 (HER2), and programmed cell death-1 (PD1). Additionally, we identified binders to viral antigens that included the Middle East respiratory syndrome (MERS) and severe acute respiratory syndrome (SARS) spike proteins. The isolated shark single-domain antibodies including Type I and Type II V<sub>NAR</sub>
s were produced in <i>Escherichia coli</i>
and validated for their antigen binding. A Type II V<sub>NAR</sub>
(PE38-B6) has a high affinity (K<sub>d</sub>
= 10.1 nM) for its antigen. <b>Conclusions:</b>
The naïve nurse shark V<sub>NAR</sub>
library is a useful source for isolating single-domain antibodies to a wide range of antigens. The EASeL method may be applicable to the construction of other large diversity gene expression libraries.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">30627698</PMID>
<DateRevised><Year>2020</Year>
<Month>03</Month>
<Day>09</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">2516-4236</ISSN>
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<Issue>1</Issue>
<PubDate><Year>2019</Year>
<Month>Jan</Month>
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<Title>Antibody therapeutics</Title>
<ISOAbbreviation>Antib Ther</ISOAbbreviation>
</Journal>
<ArticleTitle>Construction and next-generation sequencing analysis of a large phage-displayed V<sub>NAR</sub>
single-domain antibody library from six naïve nurse sharks.</ArticleTitle>
<Pagination><MedlinePgn>1-11</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1093/abt/tby011</ELocationID>
<Abstract><AbstractText><b>Background:</b>
Shark new antigen receptor variable domain (V<sub>NAR</sub>
) antibodies can bind restricted epitopes that may be inaccessible to conventional antibodies. <b>Methods:</b>
Here, we developed a library construction method based on polymerase chain reaction (PCR)-Extension Assembly and Self-Ligation (named "EASeL") to construct a large V<sub>NAR</sub>
antibody library with a size of 1.2 × 10<sup>10</sup>
from six naïve adult nurse sharks (<i>Ginglymostoma cirratum</i>
). <b>Results:</b>
The next-generation sequencing analysis of 1.19 million full-length V<sub>NAR</sub>
s revealed that this library is highly diversified because it covers all four classical V<sub>NAR</sub>
types (Types I-IV) including 11% of classical Type I and 57% of classical Type II. About 30% of the total V<sub>NAR</sub>
s could not be categorized as any of the classical types. The high variability of complementarity determining region (CDR) 3 length and cysteine numbers are important for the diversity of V<sub>NAR</sub>
s. To validate the use of the shark V<sub>NAR</sub>
library for antibody discovery, we isolated a panel of V<sub>NAR</sub>
phage binders to cancer therapy-related antigens, including glypican-3, human epidermal growth factor receptor 2 (HER2), and programmed cell death-1 (PD1). Additionally, we identified binders to viral antigens that included the Middle East respiratory syndrome (MERS) and severe acute respiratory syndrome (SARS) spike proteins. The isolated shark single-domain antibodies including Type I and Type II V<sub>NAR</sub>
s were produced in <i>Escherichia coli</i>
and validated for their antigen binding. A Type II V<sub>NAR</sub>
(PE38-B6) has a high affinity (K<sub>d</sub>
= 10.1 nM) for its antigen. <b>Conclusions:</b>
The naïve nurse shark V<sub>NAR</sub>
library is a useful source for isolating single-domain antibodies to a wide range of antigens. The EASeL method may be applicable to the construction of other large diversity gene expression libraries.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Feng</LastName>
<ForeName>Mingqian</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>Laboratory of Molecular Biology, Center for Cancer Research, National Cancer Institute, Bethesda, MD, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Bian</LastName>
<ForeName>Hejiao</ForeName>
<Initials>H</Initials>
<AffiliationInfo><Affiliation>Laboratory of Molecular Biology, Center for Cancer Research, National Cancer Institute, Bethesda, MD, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Wu</LastName>
<ForeName>Xiaolin</ForeName>
<Initials>X</Initials>
<AffiliationInfo><Affiliation>Cancer Research Technology Program, Leidos Biomedical Research, Inc., Frederick National Laboratory for Cancer Research, Frederick, MD, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Fu</LastName>
<ForeName>Tianyun</ForeName>
<Initials>T</Initials>
<AffiliationInfo><Affiliation>Laboratory of Molecular Biology, Center for Cancer Research, National Cancer Institute, Bethesda, MD, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Fu</LastName>
<ForeName>Ying</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>Laboratory of Molecular Biology, Center for Cancer Research, National Cancer Institute, Bethesda, MD, USA.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Hong</LastName>
<ForeName>Jessica</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>Laboratory of Molecular Biology, Center for Cancer Research, National Cancer Institute, Bethesda, MD, USA.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Fleming</LastName>
<ForeName>Bryan D</ForeName>
<Initials>BD</Initials>
<AffiliationInfo><Affiliation>Laboratory of Molecular Biology, Center for Cancer Research, National Cancer Institute, Bethesda, MD, USA.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Flajnik</LastName>
<ForeName>Martin F</ForeName>
<Initials>MF</Initials>
<AffiliationInfo><Affiliation>Department of Microbiology and Immunology, University of Maryland Baltimore School of Medicine, Baltimore, MD, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Ho</LastName>
<ForeName>Mitchell</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>Laboratory of Molecular Biology, Center for Cancer Research, National Cancer Institute, Bethesda, MD, USA.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
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</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2018</Year>
<Month>11</Month>
<Day>07</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>Antib Ther</MedlineTA>
<NlmUniqueID>101730822</NlmUniqueID>
<ISSNLinking>2516-4236</ISSNLinking>
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<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">gene library construction</Keyword>
<Keyword MajorTopicYN="N">next-generation sequencing</Keyword>
<Keyword MajorTopicYN="N">phage display</Keyword>
<Keyword MajorTopicYN="N">shark VNAR</Keyword>
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<Day>27</Day>
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