ArticlemBio2022
Neutralizing Antibodies against Lassa Virus Lineage I.
Article in mBio, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
22 citing papers in PubMed, 27 citations in OpenAlex.
- Lassa virus live tracking and lineage assignment: how nextstrain can enhance surveillance and public health in Africa and beyond.Emerging microbes & infections · 2026Article
- Sequence to structure insights into Lassa virus population-level biophysical properties and glycoprotein structure catalogue.Npj viruses · 2026Article
- Development of a Conditional Replication System Using a Lassa Virus Glycoprotein Complex-Encoding Retroviral Vector for Isolating Resistant Variants to Inhibitors in BSL-2.International journal of molecular sciences · 2026Article
- Development and validation of a pseudotyped virus neutralization assay for quantification of anti-Lassa virus neutralizing antibodies.Frontiers in immunology · 2026Article
- Molecular organization of the New World arenavirus spike glycoprotein complex.Nature microbiology · 2025Article
- CLASV: Rapid Lassa virus lineage assignment with random forest.PLoS neglected tropical diseases · 2025Article
- Infusion of neutralization into Lassa vaccine design.Trends in immunology · 2025Review
- Article
- Structure-guided design of a prefusion GPC trimer induces neutralizing responses against LASV.NPJ vaccines · 2025Article
- Conformational ensemble-based framework enables rapid development of Lassa virus vaccine candidates.bioRxiv : the preprint server for biology · 2024Article
- Defining bottlenecks and opportunities for Lassa virus neutralization by structural profiling of vaccine-induced polyclonal antibody responses.Cell reports · 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
- The Adaptive Immune Response againstViruses · 2024Review
- Deep mutational scanning reveals functional constraints and antigenic variability of Lassa virus glycoprotein complex.bioRxiv : the preprint server for biology · 2024Article
- Entry inhibitors as arenavirus antivirals.Frontiers in microbiology · 2024Review
- Advancements and future prospects of adeno-associated virus-mediated gene therapy for sensorineural hearing loss.Frontiers in neuroscience · 2024Review
- Defining bottlenecks and opportunities for Lassa virus neutralization by structural profiling of vaccine-induced polyclonal antibody responses.bioRxiv : the preprint server for biology · 2023Article
- Article
- Structural conservation of Lassa virus glycoproteins and recognition by neutralizing antibodies.Cell reports · 2023Article
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
Abstract
Lassa virus (LASV) is the causative agent of the deadly Lassa fever (LF). Seven distinct LASV lineages circulate through western Africa, among which lineage I (LI), the first to be identified, is particularly resistant to antibody neutralization. Lineage I LASV evades neutralization by half of known antibodies in the GPC-A antibody competition group and all but one of the antibodies in the GPC-B competition group. Here, we solve two cryo-electron microscopy (cryo-EM) structures of LI GP in complex with a GPC-A and a GPC-B antibody. We used complementary structural and biochemical techniques to identify single-amino-acid substitutions in LI that are responsible for immune evasion by each antibody group. Further, we show that LI infection is more dependent on the endosomal receptor lysosome-associated membrane protein 1 (LAMP1) for viral entry relative to LIV. In the absence of LAMP1, LI requires a more acidic fusion pH to initiate membrane fusion with the host cell relative to LIV.
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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.