# The Role of NEU1 in Coronavirus Infection and Pathogenesis

**Authors:** Y Wu, GY Chen

PMC · DOI: 10.23880/vij-16000351 · Virology & immunology journal · 2025-08-08

## TL;DR

This paper reviews how the enzyme NEU1 may influence coronavirus infection and disease progression, highlighting its role in sialic acid modification and potential therapeutic implications.

## Contribution

The paper synthesizes existing research on NEU1's role in coronavirus infection and identifies gaps for future investigation.

## Key findings

- NEU1 is involved in modifying sialic acids, which are critical for glycoprotein and glycolipid function during viral infection.
- The N protein of coronaviruses is a key structural and immunogenic component linked to replication and virion assembly.
- Sialidases like NEU1 modulate biological pathways through desialylation, affecting both normal and disease processes.

## Abstract

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has caused the coronavirus disease 2019 (COVID-19) pandemic, resulting in millions of infections and deaths worldwide. Although vaccines are available, they appear to be less efficacious against newly emerging variants of the virus. Thus, therapeutic modalities are urgently needed. The coronavirus genome encodes four major structural proteins: the spike (S) protein, nucleocapsid (N) protein, membrane (M) protein, and envelope (E) protein, all of which are required to produce a structurally complete viral particle. N protein is one of the most abundant structural proteins, participates in the regulation of viral replication and virion assembly, and is a major immunogen in coronavirus infection-induced disease. Sialylation is the addition of sialic acids to the terminal glycans of glycoproteins and glycolipids, which act as key components for biological functions of glycoproteins or glycolipids. Sialidases (or neuraminidases) are glycosidases that remove sialic acid residues (desialylation) from glycan portions of glycoproteins or glycolipids. Through desialylation, sialidases modulate the functionality of sialic acid-containing molecules and are involved in both physiological and pathological pathways. This review aims to explore the current understanding of NEU1’s involvement in coronavirus infection and pathogenesis, synthesizing available research and identifying areas for future investigation.

## Linked entities

- **Proteins:** NEU1 (neuraminidase 1), LOC102617969 (S-protein homolog 24-like)
- **Diseases:** coronavirus disease 2019 (MONDO:0100096), COVID-19 (MONDO:0100096)

## Full-text entities

- **Genes:** NEU1 (neuraminidase 1) [NCBI Gene 4758] {aka NANH, NEU, SIAL1}
- **Diseases:** deaths (MESH:D003643), COVID-19 (MESH:D000086382), infections (MESH:D007239), Coronavirus Infection (MESH:D018352)
- **Chemicals:** glycan (MESH:D011134), sialic acid (MESH:D019158), glycolipids (MESH:D006017), sialic acids (MESH:D012794)
- **Species:** Severe acute respiratory syndrome coronavirus 2 (no rank) [taxon 2697049], Gammacoronavirus (genus) [taxon 694013]

## Full text

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## Figures

1 figure with captions in the complete paper: https://tomesphere.com/paper/PMC12333695/full.md

## References

43 references — full list in the complete paper: https://tomesphere.com/paper/PMC12333695/full.md

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Source: https://tomesphere.com/paper/PMC12333695