Evidence map›Paper›PMID 37468582›Full record

ArticleScientific reports2023

Activation of SARS-CoV-2 by trypsin-like proteases in the clinical specimens of patients with COVID-19.

Emiko Yamazaki, Shunsuke Yazawa, Takahisa Shimada, Kosuke Tamura, Yumiko Saga, Masae Itamochi, Noriko Inasaki, Sumiyo Hasegawa, Yoshitomo Morinaga, Kazunori Oishi and 1 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed, 1 pooled it
1.2field-weighted citation impact, top 23% 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

3 citing papers in PubMed, 1 synthesis or guideline pooled it, 6 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
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

11 authors at 3 institutions in 1 country.

Emiko YamazakiDepartment of Virology, Toyama Institute of Health, 17-1 Nakataikoyama, Imizu-Shi, Toyama, 939-0363, Japan.
Shunsuke YazawaDepartment of Virology, Toyama Institute of Health, 17-1 Nakataikoyama, Imizu-Shi, Toyama, 939-0363, Japan.
Takahisa ShimadaDepartment of Virology, Toyama Institute of Health, 17-1 Nakataikoyama, Imizu-Shi, Toyama, 939-0363, Japan.
Kosuke TamuraDepartment of Research Planning, Toyama Institute of Health, Toyama, Japan.
Yumiko SagaDepartment of Virology, Toyama Institute of Health, 17-1 Nakataikoyama, Imizu-Shi, Toyama, 939-0363, Japan.
Masae ItamochiDepartment of Virology, Toyama Institute of Health, 17-1 Nakataikoyama, Imizu-Shi, Toyama, 939-0363, Japan.
Noriko InasakiDepartment of Virology, Toyama Institute of Health, 17-1 Nakataikoyama, Imizu-Shi, Toyama, 939-0363, Japan.
Sumiyo HasegawaDepartment of Virology, Toyama Institute of Health, 17-1 Nakataikoyama, Imizu-Shi, Toyama, 939-0363, Japan.
Yoshitomo MorinagaDepartment of Microbiology, Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama, Toyama, Japan.
Kazunori OishiToyama Institute of Health, Toyama, Japan.
Hideki TaniDepartment of Virology, Toyama Institute of Health, 17-1 Nakataikoyama, Imizu-Shi, Toyama, 939-0363, Japan. toyamaeiken3@juno.ocn.ne.jp.
Toyama Institute of Health · JPOsaka Prefectural Institute of Public Health · JPUniversity of Toyama · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SARS-CoV-2 enters host cells through the angiotensin converting enzyme 2 (ACE2) receptor and/or transmembrane protease, serine 2 (TMPRSS2). In this study, we investigated whether proteases increased SARS-CoV-2 infectivity using pseudotyped viruses and clinical specimens from patients with COVID-19. First, we investigated how trypsin increased infectivity using the pseudotyped virus. Our findings revealed that trypsin increased infectivity after the virus was adsorbed on the cells, but no increase in infectivity was observed when the virus was treated with trypsin. We examined the effect of trypsin on SARS-CoV-2 infection in clinical specimens and found that the infectivity of the SARS-CoV-2 delta variant increased 36,000-fold after trypsin treatment. By contrast, the infectivity of SARS-CoV-2 omicron variant increased to less than 20-fold in the clinical specimens. Finally, using five clinical specimens containing delta variants, enhancement of viral infectivity was evaluated in the presence of the culture supernatant of several anaerobic bacteria. As a result, viral infectivities of all the clinical specimens containing culture supernatants of Fusobacterium necrophorum were significantly increased from several- to tenfold. Because SARS-CoV-2 infectivity increases in the oral cavity, which may contain anaerobic bacteria, keeping the oral cavities clean may help prevent SARS-CoV-2 infection.

Indexed as

COVID-19HumansPeptide HydrolasesPeptidyl-Dipeptidase ASARS-CoV-2TrypsinPeptide HydrolasesPeptidyl-Dipeptidase ATrypsin

Identifiers

PMID37468582
PMCPMC10356862
OpenAlexW4384819860

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.