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| 1 | +--- |
| 2 | +layout: post |
| 3 | +title: 'DisProt 2025_06 - New thematic dataset of Bacterial virulence-related proteins' |
| 4 | +date: 2025-07-07 09:00:00 +0200 |
| 5 | +author: "Maria Cristina Aspromonte" |
| 6 | +headline: 'With this last DisProt thematic dataset, we explore the role of intrinsically disordered proteins (IDPs) in bacterial pathogenicity.' |
| 7 | +topic: "disprot" |
| 8 | +--- |
| 9 | + |
| 10 | + |
| 11 | +# **DisProt 2025_06 - New thematic dataset of Bacterial virulence-related proteins** |
| 12 | + |
| 13 | +*Written in July 2025 by Maria Cristina Aspromonte* |
| 14 | + |
| 15 | +With the latest thematic dataset released by DisProt, we turn our attention to a fascinating and still emerging topic: the role of **intrinsically disordered proteins (IDPs)** and **intrinsically disordered regions (IDRs)** in **bacterial pathogenicity**. |
| 16 | + |
| 17 | +This curated collection highlights disordered bacterial proteins with functional roles in **virulence, host–pathogen interaction**, and **immune evasion**. While IDPs are well recognized in eukaryotic systems, their relevance in bacteria is still under active investigation. |
| 18 | + |
| 19 | +From this dataset, we have **76 bacterial proteins**, all annotated in DisProt, revealing compelling insights into the biological significance of structural disorder in bacterial infections. |
| 20 | + |
| 21 | + |
| 22 | +### **How much disorder is there?** |
| 23 | + |
| 24 | +**Total number of proteins:** 76 \ |
| 25 | +**Minimum disorder content**: 1.15% \ |
| 26 | +**Maximum disorder content**: 75.19% |
| 27 | + |
| 28 | +### **Examples of disordered virulence proteins in bacteria** |
| 29 | + |
| 30 | + |
| 31 | +**Cholera enterotoxin subunit A** |
| 32 | + |
| 33 | + |
| 34 | + |
| 35 | +* **DisProt ID**: [DP00250](https://www.disprot.org/DP00250) |
| 36 | +* **Organism**: *Vibrio cholerae* serotype O1 |
| 37 | +* **Disorder content**: 75.19% |
| 38 | +* **Function**: This subunit plays a central role in the activity of the cholera toxin. It undergoes a **disorder-to-order transition** (IDPO:00050) upon binding, which facilitates its **activation and intracellular trafficking**, including **internalization** and **retrograde transport to the endoplasmic reticulum** — essential steps for the toxin’s cytotoxic effect. |
| 39 | + |
| 40 | + |
| 41 | +**Translocated intimin receptor (Tir)** |
| 42 | + |
| 43 | +* **DisProt ID**: [DP04161](https://disprot.org/DP04161) |
| 44 | +* **Organism**: *Escherichia coli* |
| 45 | +* **Disorder content**: 50.73% |
| 46 | +* **Function**: Tir is directly translocated into the host cell via a Type III secretion system. Its intrinsically disordered regions provide the **flexibility needed to interact with multiple host targets**, modulate host signaling pathways, and manipulate immune responses. |
| 47 | + |
| 48 | +Thanks to the effort of our expert DisProt biocurators, **[Maria Victoria Nugnes](https://apicuron.org/curators/0000-0001-8399-7907), (Federica Quaglia)[https://apicuron.org/curators/0000-0002-0341-4888]**, and the *DisProt Consortium*, the new dataset features more than **300** pieces of evidence obtained from **102** publications. |
| 49 | + |
| 50 | +Notes: Bacterial virulence-related proteins dataset icon was obtained from [The Noun Project](https://thenounproject.com/) |
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