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Structure of monkeypox virus poxin: implications for drug design
Vojtech Duchoslav1, Evzen Boura2
1Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, v.v.i, Flemingovo nám. 2, 166 10, Prague 6, Czech Republic.
Archives of Virology
|June 28, 2023
Summary
Researchers determined the crystal structure of mpox poxin, a viral enzyme. This finding suggests that inhibitors targeting poxin could be developed to combat mpox and other poxvirus diseases.
Area of Science:
- Structural Biology
- Virology
- Immunology
Background:
- Mpox (monkeypox) is a global health concern, with existing vaccines and drugs.
- Viruses, including mpox virus, employ strategies to evade host immune responses.
- Poxviruses utilize a unique nuclease, poxin, to interfere with the cGAS-STING innate immune pathway by cleaving the second messenger 2'-3'-cGAMP.
Purpose of the Study:
- To elucidate the three-dimensional structure of the mpox poxin enzyme.
- To identify conserved structural features, particularly in the active site, for potential therapeutic targeting.
Main Methods:
- X-ray crystallography was employed to determine the atomic structure of mpox poxin.
- Structural analysis focused on identifying conserved regions, including the cGAMP binding site and catalytic residues.
Main Results:
- The crystal structure of mpox poxin revealed a conserved, predominantly beta-sheet fold.
- High conservation was observed in the 2'-3'-cGAMP binding site and key catalytic residues (His17, Tyr138, Lys142).
Conclusions:
- The structural data provides a detailed understanding of mpox poxin's architecture.
- The conserved nature of the poxin active site suggests that poxin inhibitors could be effective broad-spectrum antiviral agents against multiple poxviruses.
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