Evidence map›Paper›PMID 27605678›Full record

ArticleJournal of virology2016

Role of LAMP1 Binding and pH Sensing by the Spike Complex of Lassa Virus.

Hadas Cohen-Dvashi, Hadar Israeli, Orly Shani, Aliza Katz, Ron Diskin

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
6.5field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

54 citing papers in PubMed, 76 citations in OpenAlex.

  1. Review
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  8. Strategies of rational and structure-driven vaccine design for Arenaviruses.Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases · 2024
    Review
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  13. Entry inhibitors as arenavirus antivirals.Frontiers in microbiology · 2024
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Lassa Virus Genetics.Current topics in microbiology and immunology · 2023
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Hadas Cohen-DvashiDepartment of Structural Biology, Weizmann Institute of Science, Rehovot, Israel.
Hadar IsraeliDepartment of Structural Biology, Weizmann Institute of Science, Rehovot, Israel.
Orly ShaniDepartment of Structural Biology, Weizmann Institute of Science, Rehovot, Israel.
Aliza KatzDepartment of Structural Biology, Weizmann Institute of Science, Rehovot, Israel.
Ron DiskinDepartment of Structural Biology, Weizmann Institute of Science, Rehovot, Israel ron.diskin@weizmann.ac.il.
Weizmann Institute of Science · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To effectively infect cells, Lassa virus needs to switch in an endosomal compartment from its primary receptor, α-dystroglycan, to a protein termed LAMP1. A unique histidine triad on the surface of the receptor-binding domain from the glycoprotein spike complex of Lassa virus is important for LAMP1 binding. Here we investigate mutated spikes that have an impaired ability to interact with LAMP1 and show that although LAMP1 is important for efficient infectivity, it is not required for spike-mediated membrane fusion per se Our studies reveal important regulatory roles for histidines from the triad in sensing acidic pH and preventing premature spike triggering. We further show that LAMP1 requires a positively charged His230 residue to engage with the spike complex and that LAMP1 binding promotes membrane fusion. These results elucidate the molecular role of LAMP1 binding during Lassa virus cell entry and provide new insights into how pH is sensed by the spike. IMPORTANCE: Lassa virus is a devastating disease-causing agent in West Africa, with a significant yearly death toll and severe long-term complications associated with its infection in survivors. In recent years, we learned that Lassa virus needs to switch receptors in a pH-dependent manner to efficiently infect cells, but neither the molecular mechanisms that allow switching nor the actual effects of switching were known. Here we investigate the activity of the viral spike complex after abrogation of its ability to switch receptors. These studies inform us about the role of switching receptors and provide new insights into how the spike senses acidic pH.

Indexed as

Africa, WesternAnimalsCell LineChlorocebus aethiopsDystroglycansEndosomesHEK293 CellsHumansHydrogen-Ion ConcentrationLassa FeverLassa virusLysosomal-Associated Membrane Protein 1Membrane FusionProtein BindingReceptors, VirusVero CellsDystroglycansLysosomal-Associated Membrane Protein 1Receptors, VirusViral Envelope Proteins

Identifiers

PMID27605678
PMCPMC5105667
OpenAlexW2516578340

What OpenQuestion holds

Textmetadata
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Registered trials

None linked

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.