Helicase–primase complex

A helicase–primase complex (also helicase-primase, Hel/Prim, H-P or H/P) is a complex of enzymes including DNA helicase and DNA primase. A helicase-primase associated factor protein may also be present.[1]

The complex is used by herpesviruses, in which it is responsible for lytic DNA virus replication.[2][3][4] In many dsDNA viruses, primase and helicase are fused into a single polypeptide chain, so that the primase and helicase domains correspond to the N-terminal and C-terminal parts of the protein, respectively.[5] A helicase-primase inhibitor (HPI) is a drug that blocks this action through acting as an enzyme inhibitor.

List of H-P by virus name

EBV: helicase:BBLF4 primase: BSLF1 accessory protein:BBLF2/3[2]

List of H-P inhibitors

Amenamevir (ASP2151)[6]
Pritelivir (BAY 57-1293, AIC316)
BILS 22 BS[6]
T157602[6]

References

Wexler P, Anderson BD, eds. (2005). Encyclopedia of toxicology (2nd ed.). p. 1850. ISBN 978-0-08-054800-5.
Thierry E, Brennich M, Round A, Buisson M, Burmeister WP, Hutin S (October 2015). "Production and characterisation of Epstein-Barr virus helicase-primase complex and its accessory protein BBLF2/3". Virus Genes. 51 (2): 171–81. doi:10.1007/s11262-015-1233-6. PMID 26292944. S2CID 18462846.
Kräusslich H, Bartenschlager R (2 December 2008). Antiviral Strategies. Springer Science & Business Media. pp. 162–8. ISBN 978-3-540-79086-0.
Cavanaugh NA (2008). Herpes DNA Synthesis: Initiation of New DNA Strands and Discrimination Between Right and Wrong Bases by the Polymerase (Ph.D.). University of Colorado at Boulder. pp. 2–12. ISBN 978-0-549-67366-8.
Kazlauskas D, Krupovic M, Venclovas Č (June 2016). "The logic of DNA replication in double-stranded DNA viruses: insights from global analysis of viral genomes". Nucleic Acids Research. 44 (10): 4551–64. doi:10.1093/nar/gkw322. PMC 4889955. PMID 27112572.
Weller SK, Kuchta RD (October 2013). "The DNA helicase-primase complex as a target for herpes viral infection". Expert Opinion on Therapeutic Targets. 17 (10): 1119–32. doi:10.1517/14728222.2013.827663. PMC 4098783. PMID 23930666.

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[1] Wexler P, Anderson BD, eds. (2005). Encyclopedia of toxicology (2nd ed.). p. 1850. ISBN 978-0-08-054800-5.

[springer-2] Thierry E, Brennich M, Round A, Buisson M, Burmeister WP, Hutin S (October 2015). "Production and characterisation of Epstein-Barr virus helicase-primase complex and its accessory protein BBLF2/3". Virus Genes. 51 (2): 171–81. doi:10.1007/s11262-015-1233-6. PMID 26292944. S2CID 18462846.

[KräusslichBartenschlager2008-3] Kräusslich H, Bartenschlager R (2 December 2008). Antiviral Strategies. Springer Science & Business Media. pp. 162–8. ISBN 978-3-540-79086-0.

[4] Cavanaugh NA (2008). Herpes DNA Synthesis: Initiation of New DNA Strands and Discrimination Between Right and Wrong Bases by the Polymerase (Ph.D.). University of Colorado at Boulder. pp. 2–12. ISBN 978-0-549-67366-8.

[5] Kazlauskas D, Krupovic M, Venclovas Č (June 2016). "The logic of DNA replication in double-stranded DNA viruses: insights from global analysis of viral genomes". Nucleic Acids Research. 44 (10): 4551–64. doi:10.1093/nar/gkw322. PMC 4889955. PMID 27112572.

[pmc4098-6] Weller SK, Kuchta RD (October 2013). "The DNA helicase-primase complex as a target for herpes viral infection". Expert Opinion on Therapeutic Targets. 17 (10): 1119–32. doi:10.1517/14728222.2013.827663. PMC 4098783. PMID 23930666.