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Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin

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Structural variations within the transferrin binding site on transferrin-binding protein B, TbpB.

Charles Calmettes¹, Rong-hua Yu, Leslie P Silva

¹Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada.

The Journal of Biological Chemistry

|February 8, 2011

Summary

Pathogenic bacteria use transferrin-binding proteins (TbpB) to acquire iron. This study reveals conserved structural elements in TbpB despite sequence variation, crucial for binding transferrin and developing vaccines.

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Area of Science:

Microbiology
Structural Biology
Immunology

Background:

Pathogenic bacteria require iron for survival in host environments.
Gram-negative bacteria like Neisseriaceae and Pasteurellaceae utilize transferrin-binding proteins (TbpA and TbpB) to acquire iron from host transferrin (Tf).
TbpA and TbpB are surface-exposed proteins and considered crucial vaccine targets due to their role in pathogenesis.

Purpose of the Study:

To determine the structure of TbpB from two porcine pathogens: Actinobacillus pleuropneumoniae and Actinobacillus suis.
To understand how TbpB maintains transferrin binding despite significant sequence variation in the binding site.
To provide insights for developing broad-spectrum vaccines targeting TbpB.

Main Methods:

X-ray crystallography to determine TbpB structures.
Molecular docking simulations.
Surface plasmon resonance (SPR) assays.
Hydrogen/deuterium exchange mass spectrometry (HDX-MS) experiments with wild-type and mutant TbpBs.

Main Results:

The structures of TbpBs from Actinobacillus pleuropneumoniae and Actinobacillus suis were determined.
Despite sequence variations in the transferrin-binding site, structurally conserved elements within TbpB homologs were identified.
Experimental data supported the structural findings, explaining the mechanism of transferrin binding despite sequence divergence.

Conclusions:

Conserved structural features in TbpB are essential for transferrin binding, even with sequence variability.
Understanding these conserved elements is key to developing effective vaccines against bacterial pathogens.
The findings pave the way for broad-spectrum vaccines targeting TbpB.