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Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2026,9,29]]},"abstract":"<jats:p>\n                    Viruses must recognize receptors on host surfaces to initiate infection, but these receptors can evolve rapidly, posing a fundamental challenge to viral persistence. The type IV pilus of\n                    <jats:italic toggle=\"yes\">Pseudomonas aeruginosa<\/jats:italic>\n                    is an ideal model system to study virus\u2013receptor coevolution because its major pilin subunit PilA exhibits extensive sequence and chemical diversity while remaining essential for bacteriophage (phage) attachment. Here, we combined comparative genomics with structural and functional analyses to determine how pilus-dependent phages maintain infectivity despite extensive receptor diversification. Pilin variation was concentrated at solvent-exposed regions, altering filament surface chemistry while preserving key subunit\u2013subunit interfaces required for pilus assembly. Despite this variation, phages recognized divergent pilins more effectively than polyclonal antisera. However, phages differed markedly in their sensitivity to receptor perturbation: some required electrostatic and structural compatibility, whereas others tolerated substantial receptor variation, including posttranslational glycosylation. Comparisons of AlphaFold3 models revealed two structurally distinct classes of tail fiber architecture associated with those phenotypes. Phages encoding tail fibers with structurally and sequence-conserved C-terminal domains were more sensitive to receptor perturbation, while those encoding structurally conserved but sequence-diverse C-terminal domains infected strains expressing highly divergent pilins. Together, these findings suggest that modular diversification of tail fibers provides a structural route by which phages accommodate receptor evolution.\n                  <\/jats:p>","DOI":"10.1073\/pnas.2626959123","type":"journal-article","created":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T16:12:31Z","timestamp":1790093551000},"update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":0,"title":["Structural diversification of phage tail fibers enables recognition of diverse type IV pili"],"prefix":"10.1073","volume":"123","author":[{"given":"Ikram","family":"Qaderi","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/02fa3aq29","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Biochemistry and Biomedical Sciences and the Michael G. 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Shen Y. Nguyen A. Guarn\u00e9 L. L. Burrows N-terminally truncated group I PilA from Pseudomonas aeruginosa strain 1244. Protein Data Bank. https:\/\/www.rcsb.org\/structure\/6BBK. Deposited 18 October 2017.","DOI":"10.2210\/pdb6bbk\/pdb"},{"key":"e_1_3_4_34_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.70.6.2837-2845.2002"},{"key":"e_1_3_4_35_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2958.2002.03171.x"},{"key":"e_1_3_4_36_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.00943-09"},{"key":"e_1_3_4_37_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.00938-08"},{"key":"e_1_3_4_38_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.biologicals.2016.06.009"},{"key":"e_1_3_4_39_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.imlet.2016.04.002"},{"key":"e_1_3_4_40_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.micpath.2016.10.027"},{"key":"e_1_3_4_41_2","unstructured":"I. Qaderi I. Chan H. Harvey L.L. Burrows Pseudomonas phage Kipling complete genome. 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