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Related Experiment Videos

Mycobacterial protein HbhA binds human complement component C3.

S L Mueller-Ortiz1, A R Wanger, S J Norris

  • 1Graduate School of Biomedical Sciences and Department of Pathology and Laboratory Medicine, Medical School, University of Texas Health Science Center at Houston, 77030, USA.

Infection and Immunity
|November 14, 2001
PubMed
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Mycobacterium tuberculosis and Mycobacterium avium utilize the heparin-binding hemagglutinin (HbhA) protein to bind human complement component C3. This interaction enhances bacterial adherence and phagocytosis by immune cells, aiding pathogen survival.

Area of Science:

  • Microbiology
  • Immunology
  • Molecular Biology

Background:

  • Mycobacterium tuberculosis and Mycobacterium avium are intracellular pathogens that infect mononuclear phagocytes.
  • Human complement component C3 facilitates the attachment and phagocytosis of these bacteria.

Purpose of the Study:

  • To identify and characterize C3-binding proteins on M. tuberculosis and M. avium.
  • To investigate the role of these proteins in bacterial-host cell interactions.

Main Methods:

  • C3 ligand affinity blot to identify C3-binding proteins.
  • Biochemical fractionation (Triton X-114) and purification (cation exchange chromatography).
  • Amino acid sequencing and recombinant protein analysis.

Main Results:

Related Experiment Videos

  • A 30-kDa C3-binding protein in M. tuberculosis and a 31-kDa protein in M. avium were identified.
  • These proteins were identified as heparin-binding hemagglutinin (HbhA).
  • Recombinant HbhA bound human C3 and enhanced bead adherence/phagocytosis in a C3-dependent manner.

Conclusions:

  • HbhA mediates C3 binding on M. tuberculosis and M. avium.
  • HbhA likely enhances bacterial adherence and phagocytosis by interacting with complement receptors on host cells.
  • HbhA is a potential virulence factor for these mycobacteria.