Helicase–primase complex

{{cs1 config|name-list-style=vanc}} 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.<ref>{{cite book | title = Encyclopedia of toxicology | edition = 2nd | editor-first1 = Philip | editor-last1 = Wexler | editor-first2 = Bruce D. | editor-last2 = Anderson | isbn = 978-0-08-054800-5 | date = 2005 | url = https://books.google.com/books?id=uQEkJw00eqcC&q=Encyclopedia+of+Toxicology+A+helicase-primase+associated+factor+protein&pg=PT1850 | page = 1850| publisher = Academic Press }}</ref>

The complex is used by herpesviruses, in which it is responsible for lytic DNA virus replication.<ref name="springer">{{cite journal | vauthors = Thierry E, Brennich M, Round A, Buisson M, Burmeister WP, Hutin S | title = Production and characterisation of Epstein-Barr virus helicase-primase complex and its accessory protein BBLF2/3 | journal = Virus Genes | volume = 51 | issue = 2 | pages = 171–81 | date = October 2015 | pmid = 26292944 | doi = 10.1007/s11262-015-1233-6 | s2cid = 18462846 }}</ref><ref name="KräusslichBartenschlager2008">{{cite book | first1 = Hans-Georg | last1 = Kräusslich | first2 = Ralf | last2 = Bartenschlager | title = Antiviral Strategies | url=https://books.google.com/books?id=r_Dq0xIZ7d&pg=PA162|date=2 December 2008|publisher=Springer Science & Business Media|isbn=978-3-540-79086-0|pages=162–8}}</ref><ref>{{cite thesis | type = Ph.D. | last = Cavanaugh | first = Nisha Angele | publisher = University of Colorado at Boulder | title = Herpes DNA Synthesis: Initiation of New DNA Strands and Discrimination Between Right and Wrong Bases by the Polymerase|url=https://books.google.com/books?id=X_mfVkcaN20C&pg=PA2|year=2008 | isbn=978-0-549-67366-8|pages=2–12}}</ref> 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.<ref>{{cite journal | vauthors = Kazlauskas D, Krupovic M, Venclovas Č | title = The logic of DNA replication in double-stranded DNA viruses: insights from global analysis of viral genomes | journal = Nucleic Acids Research | volume = 44 | issue = 10 | pages = 4551–64 | date = June 2016 | pmid = 27112572 | pmc = 4889955 | doi = 10.1093/nar/gkw322 }}</ref> 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<ref name="springer"/>

==List of H-P inhibitors== * Amenamevir (ASP2151)<ref name="pmc4098"/> * Pritelivir (BAY 57–1293, AIC316) * BILS 22 BS<ref name="pmc4098"/> * T157602<ref name="pmc4098">{{cite journal | vauthors = Weller SK, Kuchta RD | title = The DNA helicase-primase complex as a target for herpes viral infection | journal = Expert Opinion on Therapeutic Targets | volume = 17 | issue = 10 | pages = 1119–32 | date = October 2013 | pmid = 23930666 | pmc = 4098783 | doi = 10.1517/14728222.2013.827663 }}</ref>

== References == {{reflist|32em}}

{{DEFAULTSORT:Helicase-primase complex}} Category:Viral nonstructural proteins Category:Enzymes Category:Helicases