Evidence map›Paper›PMID 33154165›Full record

ArticleThe Journal of biological chemistry

Design of a highly thermotolerant, immunogenic SARS-CoV-2 spike fragment.

Sameer Kumar Malladi, Randhir Singh, Suman Pandey, Savitha Gayathri, Kawkab Kanjo, Shahbaz Ahmed, Mohammad Suhail Khan, Parismita Kalita, Nidhi Girish, Aditya Upadhyaya and 12 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed, 1 pooled it
1.2field-weighted citation impact, top 12% 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

38 citing papers in PubMed, 1 synthesis or guideline pooled it, 59 citations in OpenAlex.

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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

22 authors at 4 institutions in 1 country.

Sameer Kumar MalladiMolecular Biophysics Unit (MBU), Indian Institute of Science, Bengaluru, India.
Randhir SinghMynvax Private Limited, ES12, Entrepreneurship Centre, SID, Indian Institute of Science, Bengaluru, India.
Suman PandeyMynvax Private Limited, ES12, Entrepreneurship Centre, SID, Indian Institute of Science, Bengaluru, India.
Savitha GayathriMynvax Private Limited, ES12, Entrepreneurship Centre, SID, Indian Institute of Science, Bengaluru, India.
Kawkab KanjoMolecular Biophysics Unit (MBU), Indian Institute of Science, Bengaluru, India.
Shahbaz AhmedMolecular Biophysics Unit (MBU), Indian Institute of Science, Bengaluru, India.
Mohammad Suhail KhanMolecular Biophysics Unit (MBU), Indian Institute of Science, Bengaluru, India.
Parismita KalitaMolecular Biophysics Unit (MBU), Indian Institute of Science, Bengaluru, India.
Nidhi GirishMynvax Private Limited, ES12, Entrepreneurship Centre, SID, Indian Institute of Science, Bengaluru, India.
Aditya UpadhyayaMynvax Private Limited, ES12, Entrepreneurship Centre, SID, Indian Institute of Science, Bengaluru, India.
Poorvi ReddyMynvax Private Limited, ES12, Entrepreneurship Centre, SID, Indian Institute of Science, Bengaluru, India.
Ishika PramanickMolecular Biophysics Unit (MBU), Indian Institute of Science, Bengaluru, India.
Munmun BhasinMolecular Biophysics Unit (MBU), Indian Institute of Science, Bengaluru, India.
Shailendra ManiTranslational Health Science and Technology Institute, NCR Biotech Science Cluster, Faridabad, India.
Sankar BhattacharyyaTranslational Health Science and Technology Institute, NCR Biotech Science Cluster, Faridabad, India.
Jeswin JosephVirology Scientific Research (VSR) Laboratory, School of Biology, Indian Institute of Science Education and Research Thiruvananthapuram (IISER TVM), Kerala, India.
Karthika ThankamaniVirology Scientific Research (VSR) Laboratory, School of Biology, Indian Institute of Science Education and Research Thiruvananthapuram (IISER TVM), Kerala, India.
V Stalin RajVirology Scientific Research (VSR) Laboratory, School of Biology, Indian Institute of Science Education and Research Thiruvananthapuram (IISER TVM), Kerala, India.
Somnath DuttaMolecular Biophysics Unit (MBU), Indian Institute of Science, Bengaluru, India.
Ramandeep SinghTranslational Health Science and Technology Institute, NCR Biotech Science Cluster, Faridabad, India.
Gautham NadigMynvax Private Limited, ES12, Entrepreneurship Centre, SID, Indian Institute of Science, Bengaluru, India.
Raghavan VaradarajanMolecular Biophysics Unit (MBU), Indian Institute of Science, Bengaluru, India; Jawaharlal Nehru Centre for Advanced Scientific Research, Bengaluru, India. Electronic address: varadar@iisc.ac.in.
Indian Institute of Science Bangalore · INTranslational Health Science and Technology Institute · INIndian Institute of Science Education and Research Thiruvananthapuram · INJawaharlal Nehru Centre for Advanced Scientific Research · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Virtually all SARS-CoV-2 vaccines currently in clinical testing are stored in a refrigerated or frozen state prior to use. This is a major impediment to deployment in resource-poor settings. Furthermore, several of them use viral vectors or mRNA. In contrast to protein subunit vaccines, there is limited manufacturing expertise for these nucleic-acid-based modalities, especially in the developing world. Neutralizing antibodies, the clearest known correlate of protection against SARS-CoV-2, are primarily directed against the receptor-binding domain (RBD) of the viral spike protein, suggesting that a suitable RBD construct might serve as a more accessible vaccine ingredient. We describe a monomeric, glycan-engineered RBD protein fragment that is expressed at a purified yield of 214 mg/l in unoptimized, mammalian cell culture and, in contrast to a stabilized spike ectodomain, is tolerant of exposure to temperatures as high as 100 °C when lyophilized, up to 70 °C in solution and stable for over 4 weeks at 37 °C. In prime:boost guinea pig immunizations, when formulated with the MF59-like adjuvant AddaVax, the RBD derivative elicited neutralizing antibodies with an endpoint geometric mean titer of ∼415 against replicative virus, comparing favorably with several vaccine formulations currently in the clinic. These features of high yield, extreme thermotolerance, and satisfactory immunogenicity suggest that such RBD subunit vaccine formulations hold great promise to combat COVID-19.

Indexed as

Angiotensin-Converting Enzyme 2AnimalsAntibodies, NeutralizingAntibodies, ViralBinding SitesCOVID-19COVID-19 VaccinesEscherichia coliFemaleGuinea PigsHEK293 CellsHot TemperatureHumansImmunogenicity, VaccineModels, MolecularProtein BindingACE2 protein, humanAngiotensin-Converting Enzyme 2Antibodies, NeutralizingAntibodies, ViralCOVID-19 VaccinesReceptors, VirusRecombinant ProteinsSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2ACE2glycosylationmicrobialPichiathermostable

Identifiers

PMID33154165
PMCPMC7832000
OpenAlexW3094688801

What OpenQuestion holds

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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.