{"id":1641,"date":"2025-02-25T08:07:57","date_gmt":"2025-02-25T08:07:57","guid":{"rendered":"https:\/\/zoonoses-journal.org\/?p=1641"},"modified":"2025-02-25T08:07:57","modified_gmt":"2025-02-25T08:07:57","slug":"lassa-virus-fusion-inhibitor","status":"publish","type":"post","link":"https:\/\/zoonoses-journal.org\/index.php\/2025\/02\/25\/lassa-virus-fusion-inhibitor\/","title":{"rendered":"Functional Characterization of a Lassa Virus Fusion Inhibitor Adaptive Mutant"},"content":{"rendered":"<p>Announcing a new article publication for <em>Zoonoses<\/em> journal. Lassa virus (LASV) glycoprotein complex (GPC) contains retained stable-signal peptide (SSP), glycoprotein 1 (GP1), and glycoprotein 2 (GP2). Through serial passaging of LASV with inhibitors, adaptive mutants were obtained, most of which had mutations in the transmembrane (TM) domain of GP2. Characterizing the fusion inhibitor target within the TM domain of GP2 provided insights for the development of drugs and vaccines.<\/p>\n<p>Membrane fusion, IIH6 inhibition, thermostability, and viral growth kinetics assays were conducted to characterize the effects of the F446L mutation on GPC-mediated membrane fusion, receptor binding, thermostability, growth kinetics, and fitness.<\/p>\n<p>F446L conferred cross-resistance to structurally distinct inhibitors. Additionally, F446L increased the fusion activity of LASV and Mopeia virus (MOPV) GPC, thus elevating the pH threshold for LASV fusion and promoting MOPV fusion at neutral pH. However, F446L exerted little effect on the pseudotype viral growth profile or thermostability. Introduction of other residues at the conserved F446 locus indicated that this site showed low compatibility with similar retained aromatic cyclic tyrosine residues and did not tolerate charged residues.<\/p>\n<p>The effects of the F446L mutation on LASV were characterised, thus providing useful information for the development of vaccines and drugs.<\/p>\n<p>Read Open access article at <a href=\"https:\/\/www.scienceopen.com\/hosted-document?doi=10.15212\/ZOONOSES-2024-0051\">ScienceOpen<\/a>: <a href=\"https:\/\/www.scienceopen.com\/hosted-document?doi=10.15212\/ZOONOSES-2024-0051\">https:\/\/www.scienceopen.com\/hosted-document?doi=10.15212\/ZOONOSES-2024-0051<\/a><\/p>\n<p><em>Zoonoses<\/em> is fully open access journal for research scientists, physicians, veterinarians, and public health professionals working on diverse disciplinaries of zoonotic diseases. Please visit <a href=\"https:\/\/zoonoses-journal.org\/%20\">https:\/\/zoonoses-journal.org\/<\/a> to learn more about the journal.<\/p>\n<p><em>Zoonoses<\/em> is now open for submissions; articles can be submitted online at <a href=\"https:\/\/mc04.manuscriptcentral.com\/zoonoses\">https:\/\/mc04.manuscriptcentral.com\/zoonoses<\/a><\/p>\n<p>There are no author submission or article processing fees.<\/p>\n<p><strong>Editorial Board:<\/strong> <a href=\"https:\/\/zoonoses-journal.org\/index.php\/editorial-board\/\">https:\/\/zoonoses-journal.org\/index.php\/editorial-board\/<\/a><\/p>\n<p><strong><em>Zoonoses<\/em><\/strong> is available on <a href=\"https:\/\/www.scienceopen.com\/search#collection\/839df240-327f-47dd-b636-9b728dff9700\">ScienceOpen<\/a> (<a href=\"https:\/\/www.scienceopen.com\/search#collection\/839df240-327f-47dd-b636-9b728dff9700\">https:\/\/www.scienceopen.com\/search#collection\/839df240-327f-47dd-b636-9b728dff9700<\/a>).<\/p>\n<p>Follow <strong><em>Zoonoses <\/em><\/strong>on Twitter <a href=\"https:\/\/twitter.com\/ZoonosesJ\">@ZoonosesJ<\/a>; <a href=\"https:\/\/www.facebook.com\/Zoonoses-Journal-100462755574114\">Facebook<\/a> (<a href=\"https:\/\/www.facebook.com\/Zoonoses-Journal-100462755574114\">https:\/\/www.facebook.com\/Zoonoses-Journal-100462755574114<\/a> ) and <a href=\"https:\/\/www.linkedin.com\/company\/zoonoses\/\">LinkedIn<\/a> (<a href=\"https:\/\/www.linkedin.com\/company\/zoonoses\/\">https:\/\/www.linkedin.com\/company\/zoonoses\/<\/a>)<\/p>\n<p><strong>eISSN <\/strong>2737-7474<\/p>\n<p><strong>ISSN<\/strong> 2737-7466<\/p>\n<p><strong># # # # # #<\/strong><\/p>\n<p>Jiao Guo, Yalan Du and Guangshun Zhang et al. Functional Characterization of a Lassa Virus Fusion Inhibitor Adaptive Mutant.\u00a0<em>Zoonoses.\u00a0<\/em>2025. Vol. 5(1). DOI: 10.15212\/ZOONOSES-2024-0051<\/p>\n","protected":false},"excerpt":{"rendered":"<p>Announcing a new article publication for Zoonoses journal. Lassa virus (LASV) glycoprotein complex (GPC) contains retained stable-signal peptide (SSP), glycoprotein 1 (GP1), and glycoprotein 2 (GP2). Through serial passaging of LASV with inhibitors, adaptive mutants were obtained, most of which had mutations in the transmembrane (TM) domain of GP2. Characterizing the fusion inhibitor target within [&hellip;]<\/p>\n","protected":false},"author":6,"featured_media":1642,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"footnotes":""},"categories":[6],"tags":[557,556,555,554,559,558],"class_list":["post-1641","post","type-post","status-publish","format-standard","has-post-thumbnail","hentry","category-news-and-events","tag-adaptive-mutant","tag-fusion-inhibitor","tag-glycoprotein-complex-gpc","tag-lassa-virus-lasv","tag-lassa-virus-fusion-inhibitor","tag-membrane-fusion"],"yoast_head":"<!-- This site is optimized with the Yoast SEO plugin v27.4 - https:\/\/yoast.com\/product\/yoast-seo-wordpress\/ -->\n<title>Functional Characterization of a Lassa Virus Fusion Inhibitor Adaptive Mutant<\/title>\n<meta name=\"description\" content=\"Characterizing the F446L mutation in Lassa virus fusion inhibitors offers new insights for vaccine and drug development.\" \/>\n<meta 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