Human Serum Protein Interactions with Pseudomonas Aeruginosa PAO1

A 2026 study by Tania Bernabé identifies transthyretin as a novel binding partner to the opportunistic pathogen Pseudomonas aeruginosa PAO1. The dataset contains experimental results showing transthyretin binds to lipopolysaccharide via lipid A and induces bacterial agglutination. It is a small dataset (5.5 KB) shared under a CC BY 4.0 license.

Use Cases

• Analyze transthyretin binding interactions with Pseudomonas aeruginosa lipopolysaccharide to understand innate immune mechanisms.
• Investigate the bactericidal activity of synthetic peptides derived from the N-terminal region of transthyretin against Gram-negative bacteria.
• Study the agglutination and reduction in bacterial viability induced by transthyretin-bacteria complex formation.
• Examine the role of lipid A in mediating the interaction between transthyretin and bacterial membrane integrity.

Strengths

• Data is recent, last updated in March 2026.
• Provides novel findings on transthyretin as an endogenous antimicrobial factor.
• Includes results from mapping studies identifying the specific N-terminal region responsible for bacterial interaction.
• Shared under a permissive CC BY 4.0 license.

Limitations

• The dataset is very small at 5.5 KB, indicating limited scope and likely a small number of experimental observations.
• Specific data structure, column names, and row counts are unknown, complicating direct analysis.
• Focus is on a specific bacterial strain (PAO1) and a single protein interaction, limiting generalizability.

Provenance

Source

figshare, authored by Tania Bernabé.

Collection Method

Experimental study identifying protein-bacteria interactions, likely involving binding assays and viability tests.

Time Range

Study published in 2026.

Freshness

Last updated 2026-03-23.