{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,27]],"date-time":"2026-02-27T21:17:13Z","timestamp":1772227033509,"version":"3.50.1"},"update-to":[{"DOI":"10.1371\/journal.ppat.1009523","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2021,7,8]],"date-time":"2021-07-08T00:00:00Z","timestamp":1625702400000}}],"reference-count":73,"publisher":"Public Library of Science (PLoS)","issue":"6","license":[{"start":{"date-parts":[[2021,6,25]],"date-time":"2021-06-25T00:00:00Z","timestamp":1624579200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"National Science Foundation","award":["NSF DGE-1762114"],"award-info":[{"award-number":["NSF DGE-1762114"]}]},{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["P50AI150476"],"award-info":[{"award-number":["P50AI150476"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["R01 AI030927"],"award-info":[{"award-number":["R01 AI030927"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000024","name":"Canadian Institutes of Health Research","doi-asserted-by":"publisher","award":["PJT-162407"],"award-info":[{"award-number":["PJT-162407"]}],"id":[{"id":"10.13039\/501100000024","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.plospathogens.org"],"crossmark-restriction":false},"short-container-title":["PLoS Pathog"],"abstract":"<jats:p>\n                    The\n                    <jats:italic>APOBEC3<\/jats:italic>\n                    (\n                    <jats:italic>A3<\/jats:italic>\n                    ) genes encode cytidine deaminase proteins with potent antiviral and anti-retroelement activity. This locus is characterized by duplication, recombination, and deletion events that gave rise to the seven\n                    <jats:italic>A3<\/jats:italic>\n                    s found in primates. These include three single deaminase domain\n                    <jats:italic>A3s<\/jats:italic>\n                    (\n                    <jats:italic>A3A<\/jats:italic>\n                    ,\n                    <jats:italic>A3C<\/jats:italic>\n                    , and\n                    <jats:italic>A3H<\/jats:italic>\n                    ) and four double deaminase domain\n                    <jats:italic>A3s<\/jats:italic>\n                    (\n                    <jats:italic>A3B<\/jats:italic>\n                    ,\n                    <jats:italic>A3D<\/jats:italic>\n                    ,\n                    <jats:italic>A3F<\/jats:italic>\n                    , and\n                    <jats:italic>A3G<\/jats:italic>\n                    ). The most potent of the A3 proteins against HIV-1 is A3G. However, it is not clear if double deaminase domain A3s have a generalized functional advantage to restrict HIV-1. In order to test whether superior restriction factors could be created by genetically linking single A3 domains into synthetic double domains, we linked A3C and A3H single domains in novel combinations. We found that A3C\/A3H double domains acquired enhanced antiviral activity that is at least as potent, if not better than, A3G. Although these synthetic double domain A3s package into budding virions more efficiently than their respective single domains, this does not fully explain their gain of antiviral potency. The antiviral activity is conferred both by cytidine-deaminase dependent and independent mechanisms, with the latter correlating to an increase in RNA binding affinity. T cell lines expressing this A3C-A3H super restriction factor are able to control replicating HIV-1\u0394Vif infection to similar levels as A3G. Together, these data show that novel combinations of A3 domains are capable of gaining potent antiviral activity to levels similar to the most potent genome-encoded A3s, via a primarily non-catalytic mechanism.\n                  <\/jats:p>","DOI":"10.1371\/journal.ppat.1009523","type":"journal-article","created":{"date-parts":[[2021,6,25]],"date-time":"2021-06-25T13:35:23Z","timestamp":1624628123000},"page":"e1009523","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":4,"title":["Highly-potent, synthetic APOBEC3s restrict HIV-1 through deamination-independent mechanisms"],"prefix":"10.1371","volume":"17","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-6984-3562","authenticated-orcid":true,"given":"Mollie M.","family":"McDonnell","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1427-8647","authenticated-orcid":true,"given":"Suzanne C.","family":"Karvonen","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8939-8101","authenticated-orcid":true,"given":"Amit","family":"Gaba","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ben","family":"Flath","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4673-8978","authenticated-orcid":true,"given":"Linda","family":"Chelico","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4181-6335","authenticated-orcid":true,"given":"Michael","family":"Emerman","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"340","published-online":{"date-parts":[[2021,6,25]]},"reference":[{"key":"ppat.1009523.ref001","doi-asserted-by":"crossref","first-page":"677","DOI":"10.1146\/annurev-genet-110711-155522","article-title":"Rules 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