# Optimally fixed F protein on the surface of RSV-infected cells for RSV binding and neutralizing assays

**Authors:** Hongsheng Qiang, Yujin Shi, Zemin Jiang, Yuhao Fu, Xiaobin Zhang, Li Chen, Yongpeng Sun, Yangling Wu, Zizheng Zheng, Ningshao Xia

PMC · DOI: 10.3389/fmicb.2026.1771336 · Frontiers in Microbiology · 2026-03-04

## TL;DR

This paper introduces a new cell-based ELISA method to evaluate RSV vaccine effectiveness by measuring antibody responses to different F protein conformations.

## Contribution

A novel cell-based ELISA platform using fixed RSV-infected cells to assess vaccine-induced antibody responses.

## Key findings

- Formaldehyde stabilizes pre-fusion F proteins on RSV-infected cells.
- Methanol stabilizes post-fusion F proteins on RSV-infected cells.
- The platform effectively evaluates binding and neutralizing antibody activities.

## Abstract

Respiratory syncytial virus (RSV) presents a significant global public health challenge, contributing substantially to the disease burden worldwide. As numerous F protein-based vaccine candidates advance into clinical trials, robust evaluation methods are essential. Here, we developed a cell-based ELISA platform to rapidly evaluate serum antibody responses to these vaccines. By treating RSV-infected cells with 4% formaldehyde or 60% methanol, the cell-surface F proteins were stabilized in the pre-fusion (pre-F) or post-fusion (post-F) conformations, respectively. This platform efficiently determines the binding and neutralizing activities of post-immunization serum antibodies, providing an effective method for evaluating the efficacy of RSV vaccine candidates.

## Linked entities

- **Proteins:** f-protein (F-protein)
- **Chemicals:** formaldehyde (PubChem CID 712), methanol (PubChem CID 887)

## Full-text entities

- **Chemicals:** methanol (MESH:D000432), formaldehyde (MESH:D005557)
- **Species:** Respiratory syncytial virus (no rank) [taxon 12814]

## Full text

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## Figures

5 figures with captions in the complete paper: https://tomesphere.com/paper/PMC12996122/full.md

## References

28 references — full list in the complete paper: https://tomesphere.com/paper/PMC12996122/full.md

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Source: https://tomesphere.com/paper/PMC12996122