ArticleVirologica Sinica2021
Characterizing the Lassa Virus Envelope Glycoprotein Membrane Proximal External Region for Its Role in Fusogenicity.
Article in Virologica Sinica, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 19 citations in OpenAlex.
- The Biological Characteristics and Mouse Model of Lassa Virus From the First Imported Case in China.MedComm · 2025Article
- The Lassa Virus Stable Signal Peptide Undergoes a Conformational Change to Aid Viral Fusion.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- A novel BSL-2 Lassa virus reverse genetics system modelling the complete viral life cycle.Emerging microbes & infections · 2024Article
- Identification of residues in Lassa virus glycoprotein 1 involved in receptor switch.Virologica Sinica · 2024Article
- Spatio-temporal spread and evolution of Lassa virus in West Africa.BMC infectious diseases · 2024Article
- Deletion of the first glycosylation site promotes Lassa virus glycoprotein-mediated membrane fusion.Virologica Sinica · 2023Article
- Screening and Identification of Lassa Virus Entry Inhibitors from a Fragment-Based Drug Discovery Library.Viruses · 2022Article
- Lassa virus glycoprotein complex review: insights into its unique fusion machinery.Bioscience reports · 2022Review
- Screening and Identification of Lujo Virus Entry Inhibitors From an Food and Drug Administration-Approved Drugs Library.Frontiers in microbiology · 2021Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The membrane-proximal external region (MPER) of Lassa virus (LASV) glycoprotein complex (GPC) is critical in modulating its functionality. Till now, the high-resolution structure of the intact GPC, including MPER is not available. In this study, we used alanine substitution to scan all 16 residues located in LASV MPER. Western blotting and quantification fusion assay showed that the residues located at the C terminus of the HR2 (M414 and L415) and N terminus of the MPER (K417 and Y419) are critical for GPC-mediated membrane fusion function. Furthermore, cell surface biotinylation experiments revealed that M414A, K417A and Y419A expressed similar levels as WT, whereas L415A mutant led to a reduction of mature GPC on the cell surface. Moreover, substitution of these residues with the similar residue such as M414L, L415I, K417R and Y419F would partly compensate the loss of the fusion activity caused by the alanine mutant in these sites. Results from this study showed that several key residues in the MPER region are indispensable to promote the conformational changes that drive fusion events and shed light on the structure analysis of LASV GPC and anti-LASV therapeutics.
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