Biochemical interaction of human neutrophil peptide-1 with Mycobacterium tuberculosis H37Ra.
The biochemical mechanism of action of human neutrophil peptide-1 (HNP-1) against Mycobacterium tuberculosis H37Ra was studied. Mycobacteria grown in the presence of a subinhibitory concentration (IC50) of HNP-1 showed a significant decrease in the biosynthesis of vital macromolecules, as shown by the incorporation of various radiolabeled precursors. Mycobacterial cells grown in the presence of HNP-1 exhibited surface changes, as was evident from the increased number of binding sites for L-anilinonaphthalene 8-sulfonate. Permeability studies carried out with spheroplasts showed a significantly high permeability to a fluorescent probe, N-phenyl naphthylamine, in the presence of HNP-1. Significant changes in the cell wall and cell membrane were observed when HNP-1-grown cells were analysed by transmission electron microscopy. Our results suggest the mycobacterial cell wall/membrane to be the major target(s) of HNP-1.
Sharma
S
S
Department of Biochemistry, Postgraduate Institute of Medical Education and Research, Chandigarh, India.
Verma
I
I
Khuller
G K
GK
D000817:Anilino Naphthalenesulfonates / Q000378:metabolism; D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D002463:Cell Membrane Permeability / Q000187:drug effects; D023082:Defensins; D005453:Fluorescence; D006801:Humans; D008854:Microscopy, Electron; D009169:Mycobacterium tuberculosis / Q000187:drug effects* / Q000378:metabolism / Q000648:ultrastructure; D011506:Proteins / Q000494:pharmacology*; D023084:alpha-Defensins
D000817:Anilino Naphthalenesulfonates; D000900:Anti-Bacterial Agents; D023082:Defensins; D011506:Proteins; D023084:alpha-Defensins; C406413:human neutrophil peptide 1