Structure-Based Stabilization of Non-native Protein-Protein Interactions of Coronavirus Nucleocapsid Proteins in Antiviral Drug Design.
Identifieur interne : 000214 ( PubMed/Corpus ); précédent : 000213; suivant : 000215Structure-Based Stabilization of Non-native Protein-Protein Interactions of Coronavirus Nucleocapsid Proteins in Antiviral Drug Design.
Auteurs : Shan-Meng Lin ; Shih-Chao Lin ; Jia-Ning Hsu ; Chung-Ke Chang ; Ching-Ming Chien ; Yong-Sheng Wang ; Hung-Yi Wu ; U-Ser Jeng ; Kylene Kehn-Hall ; Ming-Hon HouSource :
- Journal of medicinal chemistry [ 1520-4804 ] ; 2020.
Abstract
Structure-based stabilization of protein-protein interactions (PPIs) is a promising strategy for drug discovery. However, this approach has mainly focused on the stabilization of native PPIs, and non-native PPIs have received little consideration. Here, we identified a non-native interaction interface on the three-dimensional dimeric structure of the N-terminal domain of the MERS-CoV nucleocapsid protein (MERS-CoV N-NTD). The interface formed a conserved hydrophobic cavity suitable for targeted drug screening. By considering the hydrophobic complementarity during the virtual screening step, we identified 5-benzyloxygramine as a new N protein PPI orthosteric stabilizer that exhibits both antiviral and N-NTD protein-stabilizing activities. X-ray crystallography and small-angle X-ray scattering showed that 5-benzyloxygramine stabilizes the N-NTD dimers through simultaneous hydrophobic interactions with both partners, resulting in abnormal N protein oligomerization that was further confirmed in the cell. This unique approach based on the identification and stabilization of non-native PPIs of N protein could be applied toward drug discovery against CoV diseases.
DOI: 10.1021/acs.jmedchem.9b01913
PubMed: 32105468
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uniqKey="Lin S" first="Shan-Meng" last="Lin">Shan-Meng Lin</name><affiliation><nlm:affiliation>Institute of Genomics and Bioinformatics, National Chung Hsing University, Taichung 402, Taiwan.</nlm:affiliation></affiliation></author><author><name sortKey="Lin, Shih Chao" sort="Lin, Shih Chao" uniqKey="Lin S" first="Shih-Chao" last="Lin">Shih-Chao Lin</name><affiliation><nlm:affiliation>National Center for Biodefense and Infectious Diseases, School of Systems Biology, George Mason University, Manassas, Virginia 20110, United States.</nlm:affiliation></affiliation></author><author><name sortKey="Hsu, Jia Ning" sort="Hsu, Jia Ning" uniqKey="Hsu J" first="Jia-Ning" last="Hsu">Jia-Ning Hsu</name><affiliation><nlm:affiliation>Institute of Genomics and Bioinformatics, National Chung Hsing University, Taichung 402, Taiwan.</nlm:affiliation></affiliation></author><author><name sortKey="Chang, Chung Ke" sort="Chang, Chung Ke" uniqKey="Chang C" first="Chung-Ke" last="Chang">Chung-Ke Chang</name><affiliation><nlm:affiliation>Institute of Biomedical Sciences, Academia Sinica, Taipei 115, Taiwan.</nlm:affiliation></affiliation></author><author><name sortKey="Chien, Ching Ming" sort="Chien, Ching Ming" uniqKey="Chien C" first="Ching-Ming" last="Chien">Ching-Ming Chien</name><affiliation><nlm:affiliation>Institute of Genomics and Bioinformatics, National Chung Hsing University, Taichung 402, Taiwan.</nlm:affiliation></affiliation></author><author><name sortKey="Wang, Yong Sheng" sort="Wang, Yong Sheng" uniqKey="Wang Y" first="Yong-Sheng" last="Wang">Yong-Sheng Wang</name><affiliation><nlm:affiliation>Institute of Genomics and Bioinformatics, National Chung Hsing University, Taichung 402, Taiwan.</nlm:affiliation></affiliation></author><author><name sortKey="Wu, Hung Yi" sort="Wu, Hung Yi" uniqKey="Wu H" first="Hung-Yi" last="Wu">Hung-Yi Wu</name><affiliation><nlm:affiliation>Graduate Institute of Veterinary Pathobiology, College of Veterinary Medicine, National Chung Hsing University, Taichung 40227, Taiwan.</nlm:affiliation></affiliation></author><author><name sortKey="Jeng, U Ser" sort="Jeng, U Ser" uniqKey="Jeng U" first="U-Ser" last="Jeng">U-Ser Jeng</name><affiliation><nlm:affiliation>National Synchrotron Radiation Research Center, 101 Hsin-Ann Road, Hsinchu Science Park, Hsinchu 30076, Taiwan.</nlm:affiliation></affiliation></author><author><name sortKey="Kehn Hall, Kylene" sort="Kehn Hall, Kylene" uniqKey="Kehn Hall K" first="Kylene" last="Kehn-Hall">Kylene Kehn-Hall</name><affiliation><nlm:affiliation>National Center for Biodefense and Infectious Diseases, School of Systems Biology, George Mason University, Manassas, Virginia 20110, United States.</nlm:affiliation></affiliation></author><author><name sortKey="Hou, Ming Hon" sort="Hou, Ming Hon" uniqKey="Hou M" first="Ming-Hon" last="Hou">Ming-Hon Hou</name><affiliation><nlm:affiliation>Institute of Genomics and Bioinformatics, National Chung Hsing University, Taichung 402, Taiwan.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Journal of medicinal chemistry</title><idno type="eISSN">1520-4804</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Structure-based stabilization of protein-protein interactions (PPIs) is a promising strategy for drug discovery. However, this approach has mainly focused on the stabilization of native PPIs, and non-native PPIs have received little consideration. Here, we identified a non-native interaction interface on the three-dimensional dimeric structure of the N-terminal domain of the MERS-CoV nucleocapsid protein (MERS-CoV N-NTD). The interface formed a conserved hydrophobic cavity suitable for targeted drug screening. By considering the hydrophobic complementarity during the virtual screening step, we identified 5-benzyloxygramine as a new N protein PPI orthosteric stabilizer that exhibits both antiviral and N-NTD protein-stabilizing activities. X-ray crystallography and small-angle X-ray scattering showed that 5-benzyloxygramine stabilizes the N-NTD dimers through simultaneous hydrophobic interactions with both partners, resulting in abnormal N protein oligomerization that was further confirmed in the cell. This unique approach based on the identification and stabilization of non-native PPIs of N protein could be applied toward drug discovery against CoV diseases.</div></front></TEI><pubmed><MedlineCitation Status="In-Data-Review" Owner="NLM"><PMID Version="1">32105468</PMID><DateRevised><Year>2020</Year><Month>03</Month><Day>27</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1520-4804</ISSN><JournalIssue CitedMedium="Internet"><Volume>63</Volume><Issue>6</Issue><PubDate><Year>2020</Year><Month>Mar</Month><Day>26</Day></PubDate></JournalIssue><Title>Journal of medicinal chemistry</Title><ISOAbbreviation>J. Med. Chem.</ISOAbbreviation></Journal><ArticleTitle>Structure-Based Stabilization of Non-native Protein-Protein Interactions of Coronavirus Nucleocapsid Proteins in Antiviral Drug Design.</ArticleTitle><Pagination><MedlinePgn>3131-3141</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1021/acs.jmedchem.9b01913</ELocationID><Abstract><AbstractText>Structure-based stabilization of protein-protein interactions (PPIs) is a promising strategy for drug discovery. However, this approach has mainly focused on the stabilization of native PPIs, and non-native PPIs have received little consideration. Here, we identified a non-native interaction interface on the three-dimensional dimeric structure of the N-terminal domain of the MERS-CoV nucleocapsid protein (MERS-CoV N-NTD). The interface formed a conserved hydrophobic cavity suitable for targeted drug screening. By considering the hydrophobic complementarity during the virtual screening step, we identified 5-benzyloxygramine as a new N protein PPI orthosteric stabilizer that exhibits both antiviral and N-NTD protein-stabilizing activities. X-ray crystallography and small-angle X-ray scattering showed that 5-benzyloxygramine stabilizes the N-NTD dimers through simultaneous hydrophobic interactions with both partners, resulting in abnormal N protein oligomerization that was further confirmed in the cell. This unique approach based on the identification and stabilization of non-native PPIs of N protein could be applied toward drug discovery against CoV diseases.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lin</LastName><ForeName>Shan-Meng</ForeName><Initials>SM</Initials><AffiliationInfo><Affiliation>Institute of Genomics and Bioinformatics, National Chung Hsing University, Taichung 402, Taiwan.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Life Sciences, National Chung Hsing University, Taichung 402, Taiwan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lin</LastName><ForeName>Shih-Chao</ForeName><Initials>SC</Initials><Identifier Source="ORCID">http://orcid.org/0000-0003-2942-5937</Identifier><AffiliationInfo><Affiliation>National Center for Biodefense and Infectious Diseases, School of Systems Biology, George Mason University, Manassas, Virginia 20110, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hsu</LastName><ForeName>Jia-Ning</ForeName><Initials>JN</Initials><AffiliationInfo><Affiliation>Institute of Genomics and Bioinformatics, National Chung Hsing University, Taichung 402, Taiwan.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Life Sciences, National Chung Hsing University, Taichung 402, Taiwan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chang</LastName><ForeName>Chung-Ke</ForeName><Initials>CK</Initials><AffiliationInfo><Affiliation>Institute of Biomedical Sciences, Academia Sinica, Taipei 115, Taiwan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chien</LastName><ForeName>Ching-Ming</ForeName><Initials>CM</Initials><AffiliationInfo><Affiliation>Institute of Genomics and Bioinformatics, National Chung Hsing University, Taichung 402, Taiwan.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Life Sciences, National Chung Hsing University, Taichung 402, Taiwan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Yong-Sheng</ForeName><Initials>YS</Initials><AffiliationInfo><Affiliation>Institute of Genomics and Bioinformatics, National Chung Hsing University, Taichung 402, Taiwan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wu</LastName><ForeName>Hung-Yi</ForeName><Initials>HY</Initials><AffiliationInfo><Affiliation>Graduate Institute of Veterinary Pathobiology, College of Veterinary Medicine, National Chung Hsing University, Taichung 40227, Taiwan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jeng</LastName><ForeName>U-Ser</ForeName><Initials>US</Initials><Identifier Source="ORCID">http://orcid.org/0000-0002-2247-5061</Identifier><AffiliationInfo><Affiliation>National Synchrotron Radiation Research Center, 101 Hsin-Ann Road, Hsinchu Science Park, Hsinchu 30076, Taiwan.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Chemical Engineering, National Tsing Hua University, Hsinchu 30013, Taiwan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kehn-Hall</LastName><ForeName>Kylene</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>National Center for Biodefense and Infectious Diseases, School of Systems Biology, George Mason University, Manassas, Virginia 20110, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hou</LastName><ForeName>Ming-Hon</ForeName><Initials>MH</Initials><Identifier Source="ORCID">http://orcid.org/0000-0003-4170-1527</Identifier><AffiliationInfo><Affiliation>Institute of Genomics and Bioinformatics, National Chung Hsing University, Taichung 402, Taiwan.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Life Sciences, National Chung Hsing University, Taichung 402, 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