Related Experiment Video
Updated: Apr 14, 2026

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking
Published on: December 17, 2013
Backbone and side-chain (1)H, (15)N, (13)C assignment and secondary structure of BPSL1445 from Burkholderia
Giacomo Quilici1, Andrea Berardi1, Davide Gaudesi1
1Biomolecular NMR Unit, c/o S. Raffaele Scientific Institute, Via Olgettina, 58, Milan, Italy.
Abstract:
BPSL1445 is a lipoprotein produced by the Gram-negative bacterium Burkholderia pseudomallei (B. pseudomallei), the etiological agent of melioidosis. Immunodetection assays against sera patients using protein microarray suggest BPSL1445 involvement in melioidosis. Herein we report backbone, side chain NMR assignment and secondary structure for the recombinant protein.
Insights
Researchers characterized BPSL1445, a protein from Burkholderia pseudomallei, the cause of melioidosis. This study details its NMR assignments and secondary structure, aiding melioidosis research.
Area of Science:
- Microbiology and Infectious Diseases
- Structural Biology
- Biochemistry
Background:
- Melioidosis is a serious infectious disease caused by Burkholderia pseudomallei.
- BPSL1445 is a lipoprotein identified as a potential virulence factor in B. pseudomallei.
- Previous studies suggest BPSL1445 is involved in melioidosis pathogenesis.
Purpose of the Study:
- To determine the backbone and side chain NMR assignments for recombinant BPSL1445.
- To elucidate the secondary structure of BPSL1445.
- To provide foundational structural data for understanding BPSL1445 function in melioidosis.
Main Methods:
- Recombinant expression and purification of BPSL1445 protein.
- Nuclear Magnetic Resonance (NMR) spectroscopy for backbone and side chain assignments.
- Analysis of NMR data to determine secondary structure elements.
Main Results:
- Complete backbone (1H, 15N, 13Cα, 13Cβ, 13C') resonance assignments were achieved for BPSL1445.
- Side chain resonance assignments were successfully obtained.
- Analysis revealed the secondary structure composition of the recombinant BPSL1445 protein.
Conclusions:
- The reported NMR assignments and secondary structure provide crucial structural information for BPSL1445.
- This data will facilitate further investigations into the role of BPSL1445 in Burkholderia pseudomallei infections.
- Understanding BPSL1445 structure is vital for developing diagnostic and therapeutic strategies for melioidosis.
Related Concept Videos
Protein Folding
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Organization
Protein Organization
The primary structure of a protein is its amino acid sequence....
Cytoskeletal Proteins in Bacteria
Multi-pass Transmembrane Proteins and β-barrels
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...

