{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Brown E"],"funding":["University of Leeds","Medical Research Council","UK Research and Innovation"],"pagination":["e68404"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11449487"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13"],"pubmed_abstract":["<i>Flaviviruses</i>, including <i>Zika virus</i> (ZIKV), are a significant global health concern, yet no licensed antivirals exist to treat disease. The small membrane (M) protein plays well-defined roles during viral egress and remains within virion membranes following release and maturation. However, it is unclear whether M plays a functional role in this setting. Here, we show that M forms oligomeric membrane-permeabilising channels in vitro, with increased activity at acidic pH and sensitivity to the prototypic channel-blocker, rimantadine. Accordingly, rimantadine blocked an early stage of ZIKV cell culture infection. Structure-based channel models, comprising hexameric arrangements of two <i>trans</i>-membrane domain protomers were shown to comprise more stable assemblages than other"],"journal":["eLife"],"pubmed_title":["Inhibitors of the small membrane (M) protein viroporin prevent Zika virus infection."],"pmcid":["PMC11449487"],"funding_grant_id":["G0700124","Impact Acceleration Account ( IAA)","LIMR Studentship","MR/T016205/1","MC_UU_12014/8","Impact Acceleration Account (IAA)","MR/N017552/1"],"pubmed_authors":["Lefteri DA","Kohl A","Moran A","Brown E","Beaumont H","Kalli AC","Maskell D","Thompson RF","McKimmie CS","Bentham MJ","Swinscoe G","Macdonald A","Griffin S","Singh R","Donald C","Ranson N","Foster R"],"additional_accession":[]},"is_claimable":false,"name":"Inhibitors of the small membrane (M) protein viroporin prevent Zika virus infection.","description":"<i>Flaviviruses</i>, including <i>Zika virus</i> (ZIKV), are a significant global health concern, yet no licensed antivirals exist to treat disease. The small membrane (M) protein plays well-defined roles during viral egress and remains within virion membranes following release and maturation. However, it is unclear whether M plays a functional role in this setting. Here, we show that M forms oligomeric membrane-permeabilising channels in vitro, with increased activity at acidic pH and sensitivity to the prototypic channel-blocker, rimantadine. Accordingly, rimantadine blocked an early stage of ZIKV cell culture infection. Structure-based channel models, comprising hexameric arrangements of two <i>trans</i>-membrane domain protomers were shown to comprise more stable assemblages than other","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Aug","modification":"2026-06-02T18:40:25.872Z","creation":"2025-04-06T22:28:46.92Z"},"accession":"S-EPMC11449487","cross_references":{"pubmed":["39177307"],"doi":["10.7554/eLife.68404"]}}