{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,3]],"date-time":"2026-03-03T17:18:59Z","timestamp":1772558339580,"version":"3.50.1"},"reference-count":36,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2026,3,3]],"date-time":"2026-03-03T00:00:00Z","timestamp":1772496000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Microbiol."],"abstract":"<jats:sec>\n                    <jats:title>Introduction<\/jats:title>\n                    <jats:p>Human noroviruses (HuNoVs) are genetically diverse RNA viruses that cause acute gastroenteritis, with genogroup II (GII) accounting for over 90% of global infections. Glycans, particularly histo-blood group antigens (HBGAs), have been identified as attachment factors or receptors for HuNoVs infection. However, the glycan-binding receptors of the later-identified GII genotypes GII.23\/24\/25 remain elusive.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Methods<\/jats:title>\n                    <jats:p>We used saliva- and glycan-based ELISA assays to identify the binding spectra of GII.23\/24\/25 strains. We also solved the crystal structures of their P domains, including the GII.25 P domain in complex with the H disaccharide. Single-point mutagenesis was performed to identify key residues involved in glycan binding.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results<\/jats:title>\n                    <jats:p>The P domains of GII.24 and GII.25 can recognize multiple types of saliva samples, including both A\/B\/O secretor and nonsecretor individuals. In contrast, GII.23 primarily binds to B secretor saliva samples. Furthermore, GII.23\/24 P domains are able to interact with the H disaccharide, whereas GII.25 exhibits binding affinity for both H disaccharide and B trisaccharide. Crystal structures of GII.23\/24\/25 P domains revealed high structural similarity, and the complex of GII.25 P domains with H disaccharide was resolved. Single-point mutagenesis identified N352, R353, D382, G443, G444, and H445 as critical residues for H disaccharide binding in GII.25 P domain, while A351 determines glycan-binding specificity.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Discussion<\/jats:title>\n                    <jats:p>Our findings demonstrate that GII.23\/24\/25 exhibit glycan-binding patterns similar to most other GII HuNoV genotypes. The structural insights provide a better understanding of virus-host evolution and inform the development of therapeutic strategies against HuNoVs.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.3389\/fmicb.2026.1767002","type":"journal-article","created":{"date-parts":[[2026,3,3]],"date-time":"2026-03-03T16:09:24Z","timestamp":1772554164000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":0,"title":["GII.23\/24\/25 noroviruses recognize glycans via a conventional glycan-binding site"],"prefix":"10.3389","volume":"17","author":[{"given":"Hanbo","family":"Li","sequence":"first","affiliation":[{"name":"Guangdong Provincial Key Laboratory of Agro-Animal Genomics and Molecular Breeding, College of Animal Science, South China Agricultural University","place":["Guangzhou, China"]},{"name":"National Institute for Viral Disease Control and Prevention, China CDC","place":["Beijing, China"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xin","family":"Cong","sequence":"additional","affiliation":[{"name":"National Institute for Viral Disease Control and Prevention, China CDC","place":["Beijing, China"]},{"name":"Department of Infectious Disease, Children\u2019s Hospital, National Clinical Research Center for Child Health, Zhejiang University School of Medicine","place":["Hangzhou, China"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xiaoman","family":"Sun","sequence":"additional","affiliation":[{"name":"National Institute for Viral Disease Control and Prevention, China CDC","place":["Beijing, China"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jianxun","family":"Qi","sequence":"additional","affiliation":[{"name":"Institute of Microbiology, Chinese Academy of Sciences","place":["Beijing, China"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xinyu","family":"Li","sequence":"additional","affiliation":[{"name":"College of Basic Medicine, Chengde Medical University","place":["Chengde, China"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Miao","family":"Jin","sequence":"additional","affiliation":[{"name":"National Institute for Viral Disease Control and Prevention, China CDC","place":["Beijing, China"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Zhaojun","family":"Duan","sequence":"additional","affiliation":[{"name":"National Institute for Viral Disease Control and Prevention, China CDC","place":["Beijing, China"]}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1965","published-online":{"date-parts":[[2026,3,3]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","first-page":"213","DOI":"10.1107\/s0907444909052925","article-title":"PHENIX: A comprehensive Python-based system for macromolecular structure solution.","volume":"66","author":"Adams","year":"2010","journal-title":"Acta Crystallogr. 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