{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,19]],"date-time":"2026-10-19T23:36:28Z","timestamp":1792452988481,"version":"4.5.0"},"reference-count":115,"publisher":"MDPI AG","issue":"20","license":[{"start":{"date-parts":[[2025,10,21]],"date-time":"2025-10-21T00:00:00Z","timestamp":1761004800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"University North","award":["UNIN-BIOMED-25-1-2"],"award-info":[{"award-number":["UNIN-BIOMED-25-1-2"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Mannose is a natural monosaccharide that plays a central role in host\u2013pathogen interactions and has emerged as a versatile scaffold for designing anti-infective agents. This review summarizes recent advances in mannose-based glycoconjugates with antibacterial, antiviral, antifungal, and antiparasitic activity. In bacteria, FimH antagonists prevent Escherichia coli adhesion, while mannose-functionalized materials disrupt Pseudomonas and Burkholderia biofilms or enhance delivery of anti-tubercular drugs. In virology, mannose-containing dendrimers, glycopolymers, and nanoparticles inhibit HIV, SARS-CoV-2, Ebola, HPV, and HSV by targeting viral glycoproteins or blocking lectin-mediated transmission. Mannose-decorated vaccines and nanocarriers also show promise against fungal pathogens and parasites. Continued optimization of presented structures could lead to the promising candidates for clinically applicable therapies.<\/jats:p>","DOI":"10.3390\/ijms262010230","type":"journal-article","created":{"date-parts":[[2025,10,21]],"date-time":"2025-10-21T13:42:03Z","timestamp":1761054123000},"page":"10230","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["Mannose Derivatives as Anti-Infective Agents"],"prefix":"10.3390","volume":"26","author":[{"given":"Rosana","family":"Ribi\u0107","sequence":"first","affiliation":[{"name":"Department of Nursing, Univeristy Center Vara\u017edin, University North, Jurja Kri\u017eani\u0107a 31b, 42000 Vara\u017edin, Croatia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,10,21]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1186\/s12964-025-02216-w","article-title":"Glycosylation as an Intricate Post-Translational Modification Process Takes Part in Glycoproteins Related Immunity","volume":"23","author":"Tian","year":"2025","journal-title":"Cell Commun. 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