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LASV is a class I fusion virus, and thus its fusion protein, GP2, is functionally similar to other class I fusion proteins in that it follows the six-helix bundle fusion mechanism. LASV fusion is atypical in that it requires another viral protein, stable signal peptide (SSP), that does not undergo fusion itself but is required for the fusion process. However, the exact function of SSP in fusion is unknown. We aimed to understand the role of SSP in the fusion process by examining the structural changes that occur within SSP during the fusion process. We found that SSP undergoes two distinct structural changes; the first at pH 6 that is not associated with fusion, the second at below pH 5 that is associated with fusion activity. Furthermore, we found a mutation to a key residue of SSP, K33A, does not undergo these two structural changes; in fact, K33A is seen to undergo a different conformational change at pH 6. We believe this distinct conformation change is due to the loss of favorable interactions between the lysine at the end of the transmembrane helix of SSP. This disruption of favorable interaction then causes downstream effects to the SSP structure in the event of lowering pH. The difference in conformational changes between K33A and wildtype (WT) SSP is likely why K33A abrogates the fusion activity of GP2. We conclude that the conformational changes undergone by SSP are crucial for LASV fusion activity.<\/jats:p>","DOI":"10.1021\/acs.biochem.6c00428","type":"journal-article","created":{"date-parts":[[2026,9,10]],"date-time":"2026-09-10T14:01:19Z","timestamp":1789048879000},"page":"3080-3091","source":"Crossref","is-referenced-by-count":0,"title":["Biophysical Characterization of K33A Mutation to Stable\nSignal Peptide Reveals Insights into Lassa Virus Fusion Mechanism"],"prefix":"10.1021","volume":"65","author":[{"given":"Shane D.","family":"Collins","sequence":"first","affiliation":[{"name":"University of Maryland College Park , , , ,","place":["College Park, Maryland, United States, 20740"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Idowu Moses","family":"Falomo","sequence":"additional","affiliation":[{"name":"University of Maryland College Park , , , ,","place":["College Park, Maryland, United States, 20740"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lucian Q.","family":"Cook","sequence":"additional","affiliation":[{"name":"University of Maryland College Park , , , ,","place":["College Park, Maryland, United States, 20740"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lia R.","family":"Goldstein","sequence":"additional","affiliation":[{"name":"University of Maryland College Park , , , ,","place":["College Park, Maryland, United States, 20740"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1433-2810","authenticated-orcid":true,"given":"Jinwoo","family":"Lee","sequence":"additional","affiliation":[{"name":"University of Maryland College Park , , , ,","place":["College Park, Maryland, United States, 20740"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,9,10]]},"reference":[{"key":"2026100608064345700_cit1","doi-asserted-by":"publisher","first-page":"63","DOI":"10.1016\/j.antiviral.2018.09.009","article-title":"The WHO R&D Blueprint:\n2018 review of emerging infectious diseases requiring urgent research\nand development efforts","volume":"159","author":"Mehand","year":"2018","journal-title":"Antiviral Res."},{"key":"2026100608064345700_cit2","doi-asserted-by":"publisher","DOI":"10.1042\/BSR20211930","article-title":"Lassa virus glycoprotein\ncomplex review: insights into its unique\nfusion machinery","volume":"42","author":"Pennington","year":"2022","journal-title":"Biosci. 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Virol."},{"key":"2026100608064345700_cit7","doi-asserted-by":"publisher","first-page":"7584","DOI":"10.1128\/JVI.00651-15","article-title":"Molecular Mechanism\nfor LAMP1 Recognition by Lassa Virus","volume":"89","author":"Cohen-Dvashi","year":"2015","journal-title":"J. Virol."},{"key":"2026100608064345700_cit8","doi-asserted-by":"publisher","first-page":"5979","DOI":"10.1128\/JVI.79.10.5979-5987.2005","article-title":"Characterization of the Interaction\nof Lassa Fever\nVirus with Its Cellular Receptor \u03b1-Dystroglycan","volume":"79","author":"Kunz","year":"2005","journal-title":"J. Virol."},{"key":"2026100608064345700_cit9","doi-asserted-by":"publisher","first-page":"2320","DOI":"10.1099\/vir.0.82950-0","article-title":"Amino acids\nfrom both N-terminal\nhydrophobic regions of the Lassa virus envelope glycoprotein GP-2\nare critical for pH-dependent membrane fusion and infectivity","volume":"88","author":"Klewitz","year":"2007","journal-title":"J. Gen. Virol."},{"key":"2026100608064345700_cit10","doi-asserted-by":"publisher","first-page":"2095","DOI":"10.1016\/j.jmb.2019.04.012","article-title":"Variations in Core Packing of GP2\nfrom Old World Mammarenaviruses in their Post-Fusion Conformations\nAffect Membrane-Fusion Efficiencies","volume":"431","author":"Shulman","year":"2019","journal-title":"J. Mol.\nBiol."},{"key":"2026100608064345700_cit11","doi-asserted-by":"publisher","first-page":"5189","DOI":"10.1128\/JVI.00208-06","article-title":"Role of the Stable Signal Peptide\nand Cytoplasmic Domain of G2 in Regulating Intracellular Transport\nof the Juni\u0301n Virus Envelope Glycoprotein Complex","volume":"80","author":"Agnihothram","year":"2006","journal-title":"J. Virol."},{"key":"2026100608064345700_cit12","doi-asserted-by":"publisher","DOI":"10.1128\/mBio.02063-14","article-title":"Arenavirus\nStable Signal Peptide Is the Keystone Subunit for Glycoprotein Complex\nOrganization","volume":"5","author":"Bederka","year":"2014","journal-title":"mBio"},{"key":"2026100608064345700_cit13","doi-asserted-by":"publisher","first-page":"6138","DOI":"10.1128\/JVI.07241-11","article-title":"Dissection of the Role of the Stable\nSignal Peptide of the Arenavirus Envelope Glycoprotein in Membrane\nFusion","volume":"86","author":"Messina","year":"2012","journal-title":"J. Virol."},{"key":"2026100608064345700_cit14","doi-asserted-by":"publisher","first-page":"7775","DOI":"10.1128\/JVI.00642-06","article-title":"Role of the Stable\nSignal Peptide of Juni\u0301n Arenavirus\nEnvelope Glycoprotein in pH-Dependent Membrane Fusion","volume":"80","author":"York","year":"2006","journal-title":"J. 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Acta BBA - Proteins Proteomics"},{"key":"2026100608064345700_cit32","doi-asserted-by":"publisher","first-page":"1529","DOI":"10.1016\/j.bpj.2017.03.011","article-title":"NMRbox: A Resource\nfor Biomolecular NMR Computation","volume":"112","author":"Maciejewski","year":"2017","journal-title":"Biophys. J."},{"key":"2026100608064345700_cit33","doi-asserted-by":"publisher","first-page":"1325","DOI":"10.1093\/bioinformatics\/btu830","article-title":"NMRFAM-SPARKY:\nenhanced software\nfor biomolecular NMR spectroscopy","volume":"31","author":"Lee","year":"2015","journal-title":"Bioinformatics"},{"key":"2026100608064345700_cit34","doi-asserted-by":"publisher","first-page":"277","DOI":"10.1007\/BF00197809","article-title":"NMRPipe: A multidimensional spectral\nprocessing system based on UNIX\npipes","volume":"6","author":"Delaglio","year":"1995","journal-title":"J. Biomol. 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