Characterization of the heparin-binding site of the mycobacterial heparin-binding hemagglutinin adhesin.

@article{Pethe2000CharacterizationOT,
  title={Characterization of the heparin-binding site of the mycobacterial heparin-binding hemagglutinin adhesin.},
  author={Kevin Pethe and Marc Aumercier and Esther Fort and C. Gatot and Camille Locht and Franco Menozzi},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 19},
  pages={
          14273-80
        }
}
The mycobacterial adhesin heparin-binding hemagglutinin (HBHA) contains several lysine-rich repeats at its carboxyl-terminal end. Using truncated recombinant HBHA forms and hybrid proteins containing HBHA repeats grafted onto the Escherichia coli maltose-binding protein (MBP), we found that these repeats are responsible for heparin binding. Immunofluorescence microscopy studies revealed that their deletion abrogates binding of HBHA to human pneumocytes. Conversely, when fused to MBP, the HBHA… CONTINUE READING
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