4.5 Article

HomA and HomB, outer membrane proteins of Helicobacter pylori down-regulate activation-induced cytidine deaminase (AID) and Ig switch germline transcription and thereby affect class switch recombination (CSR) of Ig genes in human B-cells

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Biophysical characterization of the homodimers of HomA and HomB, outer membrane proteins of Helicobacter pylori

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Summary: Our study focused on exploring the structure of the HomA and HomB proteins from H. pylori using computational, biophysical, and SAXS techniques. Analysis revealed that HomA/B consist of 8 discontinuous N and C terminal beta-strands forming a small beta-barrel with a large surface-exposed globular domain. Biophysical experiments indicated that HomA and HomB are likely dimeric and that cysteine residues on surface-exposed loops may be involved in protein-protein interactions. This structural information provides insight into the pathogenesis of H. pylori.

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