{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,16]],"date-time":"2026-09-16T16:23:23Z","timestamp":1789575803223,"version":"build-2803163510"},"reference-count":72,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2026,3,31]],"date-time":"2026-03-31T00:00:00Z","timestamp":1774915200000},"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. Cell. Infect. Microbiol."],"abstract":"<jats:p>\n                    Target cell entry of HIV-1 is dependent on the binding of gp120, the outer component of the viral envelope glycoprotein complex (Env), to CD4 and a coreceptor, preferentially CCR5 or CXCR4. Still, other interactions may also contribute to the infectivity of the virus. One such interaction is between the highly glycosylated gp120 and carbohydrate-binding proteins, such as galectins. Here, we studied the interaction between HIV-1 Env and a panel of galectins and found that galectin-8 (Gal-8), bound with highest affinity (K\n                    <jats:sub>D<\/jats:sub>\n                    &amp;lt; 1\u00b5M) and also interacted with soluble CD4. Detailed analysis using probes for different parts of Gal-8 revealed that it was primarily the N-terminal carbohydrate recognition domain that interacted with HIV-1 Env expressing sialylated galactosides and both N- and O-linked glycans. Importantly, in cell cultures Gal-8 enhanced the infectivity of HIV-1, including strains with different coreceptor use and subtype origin, as well as HIV-2. This Gal-8 infectivity enhancement was particularly strong (up to 100-fold) at low virus inoculum doses. Next, we compared Gal-8 infectivity enhancement of primary HIV-1 isolates from people living with HIV at different stages of the infection. Of note, the infectivity of HIV-1 isolates obtained during the chronic, relatively immunocompetent phase, was significantly more enhanced by Gal-8 than isolates obtained at late-stage disease during severe immunodeficiency. Taken together, this study reveals novel carbohydrate dependent interactions between Gal-8 and HIV-1 Env, resulting in enhanced infectivity of HIV-1, with particularly strong effects at low dose exposure of strains circulating during the chronic infection phase. These results suggest that Gal-8 is a cell attachment protein that HIV-1 utilizes for optimized infectivity, which may guide the development of novel intervention strategies targeting this interaction.\n                  <\/jats:p>","DOI":"10.3389\/fcimb.2026.1801072","type":"journal-article","created":{"date-parts":[[2026,3,31]],"date-time":"2026-03-31T05:32:05Z","timestamp":1774935125000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":2,"title":["Galectin-8 binds HIV envelope glycoproteins with high affinity and promotes viral infectivity"],"prefix":"10.3389","volume":"16","author":[{"given":"Enas","family":"Sheik-Khalil","sequence":"first","affiliation":[{"name":"Department of Laboratory Medicine, Lund University","place":["Lund, Sweden"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Barbro","family":"Kahl-Knutson","sequence":"additional","affiliation":[{"name":"Department of Laboratory Medicine, Lund University","place":["Lund, Sweden"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Emil","family":"Johansson","sequence":"additional","affiliation":[{"name":"Department of Translational Medicine, Lund University","place":["Lund, Sweden"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sara","family":"Karlson","sequence":"additional","affiliation":[{"name":"Department of Laboratory Medicine, Lund University","place":["Lund, Sweden"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ulf J.","family":"Nilsson","sequence":"additional","affiliation":[{"name":"Centre for Analysis and Synthesis, Department of Chemistry, Lund University","place":["Lund, Sweden"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hakon","family":"Leffler","sequence":"additional","affiliation":[{"name":"Department of Laboratory Medicine, Lund University","place":["Lund, Sweden"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marianne","family":"Jansson","sequence":"additional","affiliation":[{"name":"Department of Laboratory Medicine, Lund University","place":["Lund, Sweden"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2026,3,31]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","DOI":"10.1016\/s2055-6640(20)31289-9","article-title":"Human galectin-9 is a potent mediator of HIV transcription and reactivation","volume":"12","author":"Abdel-Mohsen","year":"2016","journal-title":"PloS Pathog."},{"key":"B2","doi-asserted-by":"publisher","first-page":"291","DOI":"10.1097\/00002030-199004000-00002","article-title":"Replicative capacity of HIV-2, like HIV-1, correlates with severity of immunodeficiency","volume":"4","author":"Albert","year":"1990","journal-title":"AIDS"},{"key":"B3","doi-asserted-by":"publisher","first-page":"10650","DOI":"10.1073\/pnas.1017954108","article-title":"Galectin-9 binding to cell surface protein disulfide isomerase regulates the redox environment to enhance T-cell migration and HIV entry","volume":"108","author":"Bi","year":"2011","journal-title":"Proc. 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