{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T23:29:24Z","timestamp":1787009364997,"version":"build-2736575974"},"reference-count":62,"publisher":"Oxford University Press (OUP)","issue":"10","license":[{"start":{"date-parts":[[2026,5,28]],"date-time":"2026-05-28T00:00:00Z","timestamp":1779926400000},"content-version":"vor","delay-in-days":8,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100020806","name":"ANR","doi-asserted-by":"publisher","award":["ANR-20-CE12-0008-02"],"award-info":[{"award-number":["ANR-20-CE12-0008-02"]}],"id":[{"id":"10.13039\/100020806","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100009708","name":"Novo Nordisk Fonden","doi-asserted-by":"publisher","award":["NNF21OC0067491"],"award-info":[{"award-number":["NNF21OC0067491"]}],"id":[{"id":"10.13039\/501100009708","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,5,20]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Bacteriophages encode diverse nucleotide-modification pathways to evade host restriction-modification (RM) and CRISPR\u2013Cas systems. On the other hand, modifications can also serve as a target for host defense systems, illustrating the complexity of the defense and counter defense landscape. Bacteriophage T4 encodes two glucosyltransferases (GTs), \u03b1-GT and \u03b2-GT, that post-replicatively add a glucose moiety to the hydroxymethylated deoxycytosines (5-hmC) on phage DNA in the \u03b1- and \u03b2-conformation, respectively. Among all fully sequenced phages, only six closely related phages encode both \u03b1-GT and \u03b2-GT. Here, through biochemical and genetic analysis, we show that \u03b2-GT has higher catalytic activity, whereas \u03b1-GT is more strongly expressed. During T4 infection, these factors determine the contributions of both GTs, with 66% of all 5-hmC \u03b1-glucosylated and 33% \u03b2-glucosylated. Encoding a single GT is sufficient to overcome the Escherichia coli RM systems, unless the glucosylation levels decrease below 80%, which constitute a complete protection threshold. However, when encountering a host encoding DNA glycosylase Brig1, in addition to type I and type IV RM systems, a second GT is necessary to enable Brig1 escapers to resist RM systems. These results demonstrate that encoding multiple GTs serves as a counter-defense mechanism when simultaneously confronted with several antiphage defense systems.<\/jats:p>","DOI":"10.1093\/nar\/gkag531","type":"journal-article","created":{"date-parts":[[2026,5,14]],"date-time":"2026-05-14T12:03:29Z","timestamp":1778760209000},"source":"Crossref","is-referenced-by-count":3,"title":["A pair of DNA glucosyltransferases elevate counter-defense in bacteriophage T4"],"prefix":"10.1093","volume":"54","author":[{"given":"Luis","family":"Ramirez-Chamorro","sequence":"first","affiliation":[{"name":"Universit\u00e9 Paris-Saclay, INRAE, AgroParisTech, Micalis Institute , Jouy-en-Josas 78350 ,","place":["France"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fr\u00e9d\u00e9ric","family":"Bonhomme","sequence":"additional","affiliation":[{"name":"Institut Pasteur, Universit\u00e9 Paris Cit\u00e9, CNRS UMR3523, Department of Structural Biology and Chemistry, Unit\u00e9 de Chimie 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