{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"institution":[{"name":"bioRxiv"}],"indexed":{"date-parts":[[2026,7,30]],"date-time":"2026-07-30T11:54:49Z","timestamp":1785412489511,"version":"3.56.0"},"posted":{"date-parts":[[2026,5,22]]},"group-title":"Microbiology","reference-count":74,"publisher":"openRxiv","license":[{"start":{"date-parts":[[2026,5,22]],"date-time":"2026-05-22T00:00:00Z","timestamp":1779408000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"award":["AI079059"],"award-info":[{"award-number":["AI079059"]}],"id":[{"id":"https:\/\/ror.org\/043z4tv69","id-type":"ROR","asserted-by":"publisher"}]},{"award":["AI079059-14S1"],"award-info":[{"award-number":["AI079059-14S1"]}],"id":[{"id":"https:\/\/ror.org\/043z4tv69","id-type":"ROR","asserted-by":"publisher"}]},{"award":["AI177392"],"award-info":[{"award-number":["AI177392"]}],"id":[{"id":"https:\/\/ror.org\/043z4tv69","id-type":"ROR","asserted-by":"publisher"}]},{"award":["AI177392-02S1"],"award-info":[{"award-number":["AI177392-02S1"]}],"id":[{"id":"https:\/\/ror.org\/043z4tv69","id-type":"ROR","asserted-by":"publisher"}]},{"award":["AI019838"],"award-info":[{"award-number":["AI019838"]}],"id":[{"id":"https:\/\/ror.org\/043z4tv69","id-type":"ROR","asserted-by":"publisher"}]},{"award":["AI140048"],"award-info":[{"award-number":["AI140048"]}],"id":[{"id":"https:\/\/ror.org\/043z4tv69","id-type":"ROR","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"accepted":{"date-parts":[[2026,5,22]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                <jats:p>How host functions affect resistance to antiviral drugs is poorly understood. Ganciclovir, a chain-terminating nucleoside analog, is a first-line therapy against human cytomegalovirus, a widespread herpesvirus that causes life-threatening disease in immunocompromised individuals and newborns. Ganciclovir resistance, which is caused by mutations that affect the viral kinase, UL97 and\/or the viral polymerase, UL54, can cause treatment failures. Among these mutations, those reducing the exonuclease activity of the viral DNA polymerase permit ganciclovir incorporation without chain termination. However, the fate of DNA strands containing the incorporated nucleotide analog is unknown. We show here that template DNA containing ganciclovir fails to support DNA synthesis of the complementary strand by exonuclease-mutant polymerase. Moreover, while DNA synthesis and ganciclovir incorporation are limited in drug-treated fibroblasts infected by virus with wild-type polymerase, an exonuclease-resistant mutant virus can better synthesize full-length genomes and incorporate substantially more ganciclovir into DNA. Notably, ganciclovir is lost from DNA when drug is removed, suggesting that ganciclovir-containing templates are repaired. We identify the host nucleotide excision repair component, XPA, and the repair enzyme, polymerase kappa, as each being necessary for mutant virus ganciclovir resistance and polymerase kappa as being required for the mutant\u2019s cidofovir resistance, demonstrating a role for host DNA repair machinery in a mechanism of antiviral resistance. We propose a model for this mechanism, which has relevance for at least one other antiviral drug and likely other nucleoside analog therapeutics, and highlights the participation of host DNA repair machinery during human cytomegalovirus DNA replication.<\/jats:p>\n                <jats:sec>\n                  <jats:title>IMPORTANCE<\/jats:title>\n                  <jats:p>Nucleoside analogues such as ganciclovir, which is a leading drug for preventing and treating human cytomegalovirus, are a critical defense against viral diseases, but antiviral resistance often results in treatment failures. This study reveals a critical role for host DNA repair in a mechanism of resistance to ganciclovir, and identifies at least one specific repair pathway that permits viral DNA synthesis in the presence of ganciclovir, defining a mechanism by which cellular DNA repair pathways conspire to enable antiviral drug resistance. This mechanism is relevant to at least one other antiviral drug and may apply to other antiviral and anticancer agents. The study also showcases the participation of host DNA repair machinery during human cytomegalovirus DNA synthesis.<\/jats:p>\n                <\/jats:sec>","DOI":"10.64898\/2026.05.21.726832","type":"posted-content","created":{"date-parts":[[2026,5,23]],"date-time":"2026-05-23T05:30:17Z","timestamp":1779514217000},"source":"Crossref","is-referenced-by-count":0,"title":["Host DNA repair factors empower a mechanism of antiviral nucleoside analog resistance"],"prefix":"10.64898","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-8875-6053","authenticated-orcid":false,"given":"Pierce","family":"Longmire","sequence":"first","affiliation":[{"name":"BIO5 Institute, University of Arizona, Tucson, AZ, 85721, USA"},{"name":"Department of Immunobiology, University of Arizona, Tucson, AZ, 85721, USA"},{"name":"Department of Pathology and Laboratory Medicine, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA"},{"name":"Division of Protective Immunity, Children\u2019s Hospital of Philadelphia, Philadelphia, PA, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Han","family":"Chen","sequence":"additional","affiliation":[{"name":"Department of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, Boston, MA, USA"},{"name":"Kymera Therapeutics, Watertown, MA, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0845-5352","authenticated-orcid":false,"given":"David R.","family":"McKinzey","sequence":"additional","affiliation":[{"name":"BIO5 Institute, University of Arizona, Tucson, AZ, 85721, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2361-7199","authenticated-orcid":false,"given":"Mamata","family":"Savanagouder","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, Geisel School of Medicine at Dartmouth, Hanover, NH, 03756, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Noelle N.","family":"Kosarek","sequence":"additional","affiliation":[{"name":"Research Computing and Data, Information, Technology, and Consulting, Dartmouth College, Hanover, NH, 03755, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5868-8747","authenticated-orcid":false,"given":"Jean M.","family":"Pesola","sequence":"additional","affiliation":[{"name":"Department of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, Boston, MA, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8631-4753","authenticated-orcid":false,"given":"Carly A.","family":"Bobak","sequence":"additional","affiliation":[{"name":"Research Computing and Data, Information, Technology, and Consulting, Dartmouth College, Hanover, NH, 03755, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8889-9895","authenticated-orcid":false,"given":"Giovanni","family":"Bosco","sequence":"additional","affiliation":[{"name":"Department of Molecular and Systems Biology, Geisel School of Medicine at Dartmouth, Hanover, NH, 03755, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6646-7290","authenticated-orcid":false,"given":"Felicia","family":"Goodrum","sequence":"additional","affiliation":[{"name":"BIO5 Institute, University of Arizona, Tucson, AZ, 85721, USA"},{"name":"Department of Immunobiology, University of Arizona, Tucson, AZ, 85721, USA"},{"name":"Department of Microbiology and Immunology, Geisel School of Medicine at Dartmouth, Hanover, NH, 03756, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2148-5671","authenticated-orcid":false,"given":"Donald M.","family":"Coen","sequence":"additional","affiliation":[{"name":"Department of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, Boston, MA, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"54368","reference":[{"key":"2026052609400989000_2026.05.21.726832v1.1","unstructured":"F. 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