# Development of a single-chain variable antibody fragment against a conserved region of the SARS-CoV-2 spike protein

**Authors:** Tingyu Gao, Atsushi Irie, Takahisa Kouwaki, Hiroyuki Oshiumi

PMC · DOI: 10.1038/s41598-024-64103-7 · Scientific Reports · 2024-06-22

## TL;DR

Researchers developed a new antibody fragment that can detect both original and variant strains of SARS-CoV-2.

## Contribution

A high-affinity single-chain antibody fragment (sc5G2) targeting a conserved region of the SARS-CoV-2 spike protein was developed.

## Key findings

- The sc5G2 antibody fragment effectively detects the original SARS-CoV-2 spike protein.
- The sc5G2 also detects spike proteins from variant strains of SARS-CoV-2.
- The antibody fragment was successfully expressed in both mammalian and bacterial cells.

## Abstract

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has prolonged the duration of the pandemic because of the continuous emergence of new variant strains. The emergence of these mutant strains makes it difficult to detect the virus with the existing antibodies; thus, the development of novel antibodies that can target both the variants as well as the original strain is necessary. In this study, we generated a high-affinity monoclonal antibody (5G2) against the highly conserved region of the SARS-CoV-2 spike protein to detect the protein variants. Moreover, we generated its single-chain variable antibody fragment (sc5G2). The sc5G2 expressed in mammalian and bacterial cells detected the spike protein of the original SARS-CoV-2 and variant strains. The resulting sc5G2 will be a useful tool to detect the original SARS-CoV-2 and variant strains.

## Linked entities

- **Diseases:** Severe acute respiratory syndrome coronavirus 2 (MONDO:0100096), SARS-CoV-2 (MONDO:0100096)

## Full-text entities

- **Species:** Severe acute respiratory syndrome coronavirus 2 (no rank) [taxon 2697049]

## Full text

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## Figures

7 figures with captions in the complete paper: https://tomesphere.com/paper/PMC11193732/full.md

## References

48 references — full list in the complete paper: https://tomesphere.com/paper/PMC11193732/full.md

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Source: https://tomesphere.com/paper/PMC11193732