{"entity": "researcher", "timestamp": "2026-08-22T06:58:22.999Z", "family": "Li", "given": "Jinlin", "initials": "J", "orcid": "0000-0002-8998-9278", "affiliations": ["Department of Medical Biochemistry and Microbiology, The Biomedical Center, Uppsala University, Uppsala, 75123, Sweden.", "Zoonosis Science Center, Uppsala University, Uppsala, 75123, Sweden."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/ef44854e04b441209560929fc2533974.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/ef44854e04b441209560929fc2533974"}}, "publications": [{"entity": "publication", "iuid": "b113162cd8944a08a4fe94413551f8dc", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/b113162cd8944a08a4fe94413551f8dc.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/b113162cd8944a08a4fe94413551f8dc"}}, "title": "Dual roles of exostosin glycosyltransferase 1 in Zika virus infection.", "authors": [{"family": "Ling", "given": "Jiaxin", "initials": "J"}, {"family": "Khan", "given": "Asifa", "initials": "A"}, {"family": "Denkewitz", "given": "Matthias", "initials": "M"}, {"family": "Maccarana", "given": "Marco", "initials": "M"}, {"family": "Lundkvist", "given": "\u00c5ke", "initials": "\u00c5"}, {"family": "Li", "given": "Jin-Ping", "initials": "JP"}, {"family": "Li", "given": "Jinlin", "initials": "J", "orcid": "0000-0002-8998-9278", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/ef44854e04b441209560929fc2533974.json"}}], "type": "journal article", "published": "2025-12-00", "journal": {"title": "Virulence", "issn": "2150-5608", "volume": "16", "issue": "1", "pages": "2458681", "issn-l": null}, "abstract": "Many factors involved in heparan sulfate (HS) biosynthesis and metabolism have been reported to play roles in viral infection. However, the detailed mechanisms are still not fully understood. In this study, we report that exostosin glycosyltransferase 1 (EXT1), the HS polymerase, is a critical regulatory factor for Zika virus (ZIKV) infection. Knocking out EXT1 dramatically restricts ZIKV infection, which is not due to the inhibition of virus entry resulting from HS deficiency, but mediated by the downregulation of autophagy. Induction of autophagy promotes ZIKV infection, and attenuated autophagy is found in distinct EXT1 knockout (EXT1-KO) cell lines. Induction of autophagy by rapamycin can relieve the ZIKV production defect in EXT1-KO cells. While over-expressing EXT1 results in the reduction of ZIKV production by targeting the viral envelope (E) protein and non-structural protein NS3 in a proteasome-dependent degradation manner. The different roles of EXT1 in ZIKV infection are further confirmed by the data that knocking down EXT1 at the early stage of ZIKV infection represses viral infection, whereas the increase of ZIKV infection is observed when knocking down EXT1 at the late stage of viral infection. This study discovers previously unrecognized intricate roles of EXT1 in ZIKV infection.", "doi": "10.1080/21505594.2025.2458681", "pmid": "39927690", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC11812395"}, {"db": "figshare", "key": "10.6084/m9.figshare.26862613"}], "notes": [], "created": "2026-08-21T12:05:24.950Z", "modified": "2026-08-21T12:05:25.005Z"}, {"entity": "publication", "iuid": "1bfc9496f0e14baaa1d77d2380d008b7", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/1bfc9496f0e14baaa1d77d2380d008b7.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/1bfc9496f0e14baaa1d77d2380d008b7"}}, "title": "A Heparan Sulfate Mimetic RAFT Copolymer Inhibits SARS-CoV-2 Infection and Ameliorates Viral-Induced Inflammation.", "authors": [{"family": "Ling", "given": "Jiaxin", "initials": "J"}, {"family": "Lundkvist", "given": "\u00c5ke", "initials": "\u00c5"}, {"family": "Guerrini", "given": "Marco", "initials": "M"}, {"family": "Ferro", "given": "Vito", "initials": "V"}, {"family": "Li", "given": "Jin-Ping", "initials": "JP"}, {"family": "Li", "given": "Jinlin", "initials": "J", "orcid": "0000-0002-8998-9278", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/ef44854e04b441209560929fc2533974.json"}}], "type": "journal article", "published": "2025-02-00", "journal": {"title": "Adv Sci (Weinh)", "issn": "2198-3844", "volume": "12", "issue": "6", "pages": "e2411737", "issn-l": null}, "abstract": "The high transmissibility and mutation ability of coronaviruses enable them to easily escape existing immune protection and also pose a challenge to existing antiviral drugs. Moreover, drugs only targeting viruses cannot always attenuate the \"cytokine storm\". Herein, a synthetic heparan sulfate (HS) mimetic, HMSA-06 is reported, that exhibited antiviral activities against both the SARS-CoV-2 prototype and Omicron strains by targeting viral entry and replication. Of particular note, HMSA-06 demonstrated more potent anti-SARS-CoV-2 effects than PG545 and Roneparstat. SARS-CoV-2 is reported to hijack autophagy to facilitate its replication, therefore boosting autophagy can attenuate SARS-CoV-2 infection. It is revealed that HMSA-06, but not a similar HS mimetic that failed to inhibit SARS-CoV-2, can upregulate cellular autophagy flux. In addition, HMSA-06 was found to robustly block the NLRP3-mediated inflammatory reaction in SARS-CoV-2 infected THP-1 derived macrophages as evidenced by a reduction in inflammasome formation and the subsequent decreased secretion of mature caspase-1 and IL-1\u03b2. The HMSA-06's inflammation inhibitory function is further confirmed using a LPS/ATP-stimulated THP-1 macrophage model. Altogether, this study has identified a promising HS mimetic to combat SARS-CoV-2-associated diseases by inhibiting viral infection and attenuating viral-induced inflammatory reaction, providing insights into the development of novel anti-coronavirus drugs in the future.", "doi": "10.1002/advs.202411737", "pmid": "39679877", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC11809384"}], "notes": [], "created": "2026-08-21T10:59:31.453Z", "modified": "2026-08-21T10:59:31.521Z"}, {"entity": "publication", "iuid": "19436378bcfb49d384611e71305c32ee", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/19436378bcfb49d384611e71305c32ee.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/19436378bcfb49d384611e71305c32ee"}}, "title": "Is heparan sulfate a target for inhibition of RNA virus infection?", "authors": [{"family": "Ling", "given": "Jiaxin", "initials": "J"}, {"family": "Li", "given": "Jinlin", "initials": "J", "orcid": "0000-0002-8998-9278", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/ef44854e04b441209560929fc2533974.json"}}, {"family": "Khan", "given": "Asifa", "initials": "A"}, {"family": "Lundkvist", "given": "\u00c5ke", "initials": "\u00c5"}, {"family": "Li", "given": "Jin-Ping", "initials": "JP"}], "type": "journal article", "published": "2022-04-01", "journal": {"title": "Am. J. Physiol., Cell Physiol.", "issn": "1522-1563", "volume": "322", "issue": "4", "pages": "C605-C613", "issn-l": "0363-6143"}, "abstract": "Heparan sulfate (HS) is a linear polysaccharide attached to a core protein, forming heparan sulfate proteoglycans (HSPGs) that are ubiquitously expressed on the surface of almost all mammalian cells and the extracellular matrix. HS orchestrates the binding of various signal molecules to their receptors, thus regulating many biological processes, including homeostasis, metabolism, and various pathological processes. Due to its wide distribution and negatively charged properties, HS is exploited by many viruses as a cofactor to attach to host cells. Therefore, inhibition of the interaction between virus and HS is proposed as a promising approach to mitigate viral infection, including SARS-CoV-2. In this review, we summarize the interaction manners of HS with viruses with focus on significant pathogenic RNA viruses, including alphaviruses, flaviviruses, and coronaviruses. We also provide an overview of the challenges we may face when using HS mimetics as antivirals for clinical treatment. More studies are needed to provide a further understanding of the interplay between HS and viruses both in vitro and in vivo, which will favor the development of specific antiviral inhibitors.", "doi": "10.1152/ajpcell.00028.2022", "pmid": "35196165", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC8977144"}], "notes": [], "created": "2026-08-21T12:27:51.080Z", "modified": "2026-08-21T12:27:51.124Z"}]}