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Related Experiment Videos

Hemin-binding surface protein from Bartonella quintana.

J A Carroll1, S A Coleman, L S Smitherman

  • 1Microscopy Branch, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, Hamilton, Montana 59840, USA.

Infection and Immunity
|November 18, 2000
PubMed
Summary

Bartonella quintana, a bacterium with high hemin needs, utilizes HbpA, a surface-exposed outer membrane protein, for hemin acquisition. This study identifies HbpA as a key virulence factor in Bartonella quintana infections.

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Area of Science:

  • Microbiology
  • Bacterial Pathogenesis
  • Molecular Biology

Background:

  • Bartonella quintana causes trench fever, endocarditis, and bacillary angiomatosis.
  • B. quintana exhibits an exceptionally high in vitro hemin requirement.
  • Hemin acquisition is crucial for bacterial survival and virulence.

Purpose of the Study:

  • To identify and characterize hemin-binding proteins in Bartonella quintana.
  • To investigate the role of the dominant hemin-binding protein in B. quintana pathogenesis.
  • To determine the location and genetic basis of the primary hemin-binding protein.

Main Methods:

  • Triton X-114 extraction and heat modification assays to characterize membrane proteins.
  • Immunoblotting and immunoelectron microscopy to determine protein localization.

Related Experiment Videos

  • Gene cloning, sequencing, and recombinant protein expression to analyze the hbpA gene and protein.
  • Southern blotting to assess the presence of hbpA homologs in other Bartonella species.
  • Functional assays using anti-HbpA Fab fragments to evaluate hemin binding.

    • Main Results:

    • Eight membrane proteins bind hemin, with HbpA (approximately 25 kDa) being dominant.
    • HbpA is an outer membrane protein, surface-exposed, and heat-modifiable.
    • The hbpA gene was cloned and sequenced, revealing a Fur box homolog upstream.
    • HbpA homologs are present in all five pathogenic Bartonella species.
    • Antibody inhibition of HbpA significantly reduced hemin binding, confirming its role in acquisition.

    Conclusions:

    • HbpA is the primary hemin-binding protein in Bartonella quintana.
    • HbpA is a surface-exposed outer membrane protein crucial for hemin acquisition.
    • HbpA represents the first characterized virulence determinant of Bartonella quintana and a potential therapeutic target.