Evidence map›Paper›PMID 38783052›Full record

ArticleScientific reports2024

Detailed analysis of low temperature inactivation of respiratory syncytial virus.

Yuki Kitai, Oshi Watanabe, Suguru Ohmiya, Tomoko Kisu, Reiko Ota, Kazuyoshi Kawakami, Hiroshi Katoh, Kaori Fukuzawa, Makoto Takeda, Hidekazu Nishimura

Abstract read
In one paragraph

Article in Scientific reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
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

5 citing papers in PubMed.

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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

10 authors.

Yuki KitaiDepartment of Microbiology, Graduate School of Medicine and Faculty of Medicine, The University of Tokyo, Tokyo, Japan. y-kitai@m.u-tokyo.ac.jp.
Oshi WatanabeVirus Research Center, Clinical Research Division, Sendai Medical Center, Sendai, Miyagi, Japan.
Suguru OhmiyaVirus Research Center, Clinical Research Division, Sendai Medical Center, Sendai, Miyagi, Japan.
Tomoko KisuVirus Research Center, Clinical Research Division, Sendai Medical Center, Sendai, Miyagi, Japan.
Reiko OtaVirus Research Center, Clinical Research Division, Sendai Medical Center, Sendai, Miyagi, Japan.
Kazuyoshi KawakamiDepartment of Medical Microbiology, Mycology and Immunology, Tohoku University Graduate School of Medicine, Sendai, Miyagi, Japan.
Hiroshi KatohDepartment of Microbiology, Graduate School of Medicine and Faculty of Medicine, The University of Tokyo, Tokyo, Japan.
Kaori FukuzawaGraduate School of Pharmaceutical Sciences, Osaka University, Suita, Osaka, Japan.
Makoto TakedaDepartment of Microbiology, Graduate School of Medicine and Faculty of Medicine, The University of Tokyo, Tokyo, Japan.
Hidekazu NishimuraVirus Research Center, Clinical Research Division, Sendai Medical Center, Sendai, Miyagi, Japan. hide-nishimura@mte.biglobe.ne.jp.

Funding

Japan Agency for Medical Research and Development JP223fa627001Japan Agency for Medical Research and Development JPwm0125001Japan Society for the Promotion of Science 23K19463Japan Society for the Promotion of Science JP19K24679
6 · The paper itself

Abstract

Our previous findings indicated that many respiratory syncytial virus (RSV) isolates are unstable at 4 °C compared to 20 °C. Some of the strains completely lose infectivity after 24 h at 4 °C. This study analyzed the inactivation process at 4 °C using a representative strain, RSV/Sendai/851/13. After 24 h of storage at 4 °C, the virus was completely inactivated but retained its ability to attach to and to be taken into host cells. It suggested a reduced fusion ability between the viral and cellular membranes. During storage at 4 °C, the RSV fusion (F) protein underwent a conformational change and was no longer recognized by pre-fusion form-specific antibodies. When the RSV/Sendai/851/13 strain was passaged at 4 °C, a variant with an amino acid substitution, I148T, in the F protein fusion peptide was selected. Also, an amino acid change in G protein demonstrating stability at low temperatures was obtained. These results show that the inactivation of RSV at 4 °C is due to the loss of membrane fusion activity in the F protein, which cannot maintain its pre-fusion state at 4 °C.

Indexed as

Cold TemperatureRespiratory Syncytial Virus, HumanViral Fusion ProteinsVirus InactivationAnimalsHumansRespiratory Syncytial VirusesRespiratory Syncytial Virus InfectionsViral Fusion Proteins

Identifiers

PMID38783052
PMCPMC11116427

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Registered trials

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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.