RRC ID 86329
著者 Ide M, Tabata N, Murai K, Yonemura Y, Wang Y, Ishida A, Shirasaki T, Kaneko S, Ito S, Honda M, Yanagawa H.
タイトル Endothelial lipase-binding peptides similar to netrin-1 inhibit hepatitis B virus infection.
ジャーナル FEBS Lett
Abstract Hepatitis B virus (HBV) infects cells by attaching to heparan sulfate proteoglycans (HSPG) and Na+/taurocholate cotransporting polypeptide (NTCP). The endothelial lipase LIPG bridges HSPG and HBV, facilitating HBV attachment. From a randomized peptide expression library, we identified a short sequence binding to LIPG. This identified sequence closely resembled a sequence in the V domain of netrin-1, a protein known to bind heparin through its V domain. We designed two synthetic peptides based on this sequence and found that both synthetic peptides and netrin-1 suppressed HBV infection in chimeric mice with humanized livers and in primary hepatocytes isolated from them. The data reveal an antiviral function of the peptides and netrin-1 in HBV infection that is independent of LIPG lipase activity.
巻・号 599(9)
ページ 1285-1298
公開日 2025-5-1
DOI 10.1002/1873-3468.15101
PMID 39865491
MeSH Amino Acid Sequence Animals Antiviral Agents* / chemistry Antiviral Agents* / metabolism Antiviral Agents* / pharmacology Hepatitis B* / drug therapy Hepatitis B* / metabolism Hepatitis B* / virology Hepatitis B virus* / drug effects Hepatitis B virus* / physiology Hepatocytes / drug effects Hepatocytes / metabolism Hepatocytes / virology Humans Lipase* / metabolism Mice Netrin-1* / chemistry Netrin-1* / metabolism Peptides* / chemical synthesis Peptides* / chemistry Peptides* / metabolism Peptides* / pharmacology Protein Binding
IF 3.057
リソース情報
ヒト・動物細胞 293T(RCB2202)