Evidence map›Paper›PMID 36214577›Full record

ArticleJournal of virology2022

Dissecting Naturally Arising Amino Acid Substitutions at Position L452 of SARS-CoV-2 Spike.

Toong Seng Tan, Mako Toyoda, Hirotaka Ode, Godfrey Barabona, Hiroshi Hamana, Mizuki Kitamatsu, Hiroyuki Kishi, Chihiro Motozono, Yasumasa Iwatani, Takamasa Ueno

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Journal of virology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.4field-weighted citation impact, top 17% 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

8 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 4 institutions in 1 country.

Toong Seng TanJoint Research Center for Human Retrovirus Infection, Kumamoto Universitygrid.274841.c, Kumamoto, Japan.
Mako ToyodaJoint Research Center for Human Retrovirus Infection, Kumamoto Universitygrid.274841.c, Kumamoto, Japan.
Hirotaka OdeClinical Research Center, National Hospital Organization Nagoya Medical Center, Nagoya, Aichi, Japan.
Godfrey BarabonaJoint Research Center for Human Retrovirus Infection, Kumamoto Universitygrid.274841.c, Kumamoto, Japan.
Hiroshi HamanaDepartment of Immunology, Faculty of Medicine, Academic Assembly, University of Toyamagrid.267346.2, Toyama, Japan.
Mizuki KitamatsuDepartment of Applied Chemistry, Faculty of Science and Engineering, Kindai Universitygrid.258622.9, Osaka, Japan.
Hiroyuki KishiDepartment of Immunology, Faculty of Medicine, Academic Assembly, University of Toyamagrid.267346.2, Toyama, Japan.
Chihiro MotozonoJoint Research Center for Human Retrovirus Infection, Kumamoto Universitygrid.274841.c, Kumamoto, Japan.
Yasumasa IwataniClinical Research Center, National Hospital Organization Nagoya Medical Center, Nagoya, Aichi, Japan.ORCID 0000-0001-9269-4828
Takamasa UenoJoint Research Center for Human Retrovirus Infection, Kumamoto Universitygrid.274841.c, Kumamoto, Japan.ORCID 0000-0003-4852-4236
Kumamoto University · JPNational Hospital Organization · JPUniversity of Toyama · JPKindai University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mutations at spike protein L452 are recurrently observed in severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants of concern (VOC), including omicron lineages. It remains elusive how amino acid substitutions at L452 are selected in VOC. Here, we characterized all 19 possible mutations at this site and revealed that five mutants expressing the amino acids Q, K, H, M, and R gained greater fusogenicity and pseudovirus infectivity, whereas other mutants failed to maintain steady-state expression levels and/or pseudovirus infectivity. Moreover, the five mutants showed decreased sensitivity toward neutralization by vaccine-induced antisera and conferred escape from T cell recognition. Contrary to expectations, sequence data retrieved from the Global Initiative on Sharing All Influenza Data (GISAID) revealed that the naturally occurring L452 mutations were limited to Q, M, and R, all of which can arise from a single nucleotide change. Collectively, these findings highlight that the codon base change mutational barrier is a prerequisite for amino acid substitutions at L452, in addition to the phenotypic advantages of viral fitness and decreased sensitivity to host immunity.

Indexed as

COVID-19SARS-CoV-2Amino AcidsAmino Acid SubstitutionHumansImmune SeraMutationNucleotidesSpike Glycoprotein, CoronavirusAmino AcidsImmune SeraNucleotidesSpike Glycoprotein, CoronaviruscoronavirusfitnessL452mutational studiesSARS-CoV-2spikespike proteinsubstitution

Identifiers

PMID36214577
PMCPMC9599599
OpenAlexW4303986818

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.