ReviewBioscience reports2022
Lassa virus glycoprotein complex review: insights into its unique fusion machinery.
Review in Bioscience reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
29 citing papers in PubMed, 41 citations in OpenAlex.
- Harnessing conserved epitopes and multivalent antigen strategies for vaccine design: Lessons learned and opportunities.Human vaccines & immunotherapeutics · 2026Review
- Deadbolt Drug Discovery: Locking the Door to Class 1 Viral Entry by Small Molecules.ACS infectious diseases · 2026Review
- Article
- Design of a global population-covering multi-epitope mRNA vaccine against Lassa virus using immunoinformatics.Scientific reports · 2026Article
- The Lassa virus fusion domain has structural plasticity and exploits bis(monoacylglycero)phosphate for fusion.Biophysical journal · 2026Article
- Development of a Rapid and Sensitive AlphaLISA-Based Assay for Lassa Virus Glycoprotein Detection.Pathogens (Basel, Switzerland) · 2026Article
- Prediction of pre- and postfusion conformations of class I fusion proteins with AlphaFold2.PloS one · 2026Article
- Framework-mediated binding of foreign and self-glycans by IGHV4-34 antibodies.Frontiers in immunology · 2026Review
- A Mutation-Based Reverse Vaccinology Approach Considering Variability in Epitopes to Combat Multi-Strains: A Study Using Glycoprotein of LASV.Journal of cellular and molecular medicine · 2025Article
- The Biological Characteristics and Mouse Model of Lassa Virus From the First Imported Case in China.MedComm · 2025Article
- Genomic changes of Lassa virus associated with mammalian host adaptation.BMC genomics · 2025Article
- The Lassa Virus Stable Signal Peptide Undergoes a Conformational Change to Aid Viral Fusion.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Machine and deep learning to predict viral fusion peptides.Computational and structural biotechnology journal · 2025Article
- Conformational ensemble-based framework enables rapid development of Lassa virus vaccine candidates.bioRxiv : the preprint server for biology · 2024Article
- Architectural organization andJournal of virology · 2024Article
- Characterization of bi-segmented and tri-segmented recombinant Pichinde virus particles.Journal of virology · 2024Article
- Deep mutational scanning reveals functional constraints and antibody-escape potential of Lassa virus glycoprotein complex.Immunity · 2024Article
- Strategies of rational and structure-driven vaccine design for Arenaviruses.Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases · 2024Review
- Hexestrol, an estrogen receptor agonist, inhibits Lassa virus entry.Journal of virology · 2024Article
- Disruption of Transmembrane Phosphatidylserine Asymmetry by HIV-1 Incorporated SERINC5 Is Not Responsible for Virus Restriction.Biomolecules · 2024Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lassa virus (LASV), an arenavirus endemic to West Africa, causes Lassa fever-a lethal hemorrhagic fever. Entry of LASV into the host cell is mediated by the glycoprotein complex (GPC), which is the only protein located on the viral surface and comprises three subunits: glycoprotein 1 (GP1), glycoprotein 2 (GP2), and a stable signal peptide (SSP). The LASV GPC is a class one viral fusion protein, akin to those found in viruses such as human immunodeficiency virus (HIV), influenza, Ebola virus (EBOV), and severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). These viruses are enveloped and utilize membrane fusion to deliver their genetic material to the host cell. Like other class one fusion proteins, LASV-mediated membrane fusion occurs through an orchestrated sequence of conformational changes in its GPC. The receptor-binding subunit, GP1, first engages with a host cell receptor then undergoes a unique receptor switch upon delivery to the late endosome. The acidic pH and change in receptor result in the dissociation of GP1, exposing the fusion subunit, GP2, such that fusion can occur. These events ultimately lead to the formation of a fusion pore so that the LASV genetic material is released into the host cell. Interestingly, the mature GPC retains its SSP as a third subunit-a feature that is unique to arenaviruses. Additionally, the fusion domain contains two separate fusion peptides, instead of a standard singular fusion peptide. Here, we give a comprehensive review of the LASV GPC components and their unusual features.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.