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Related Experiment Videos

Acidic precursor revealed in human eosinophil granule major basic protein cDNA.

R L Barker1, G J Gleich, L R Pease

  • 1Department of Immunology, Mayo Medical School, Mayo Clinic, Rochester, Minnesota 55905.

The Journal of Experimental Medicine
|October 1, 1988
PubMed
Summary

Eosinophil major basic protein (MBP) is translated as a nontoxic precursor, protecting cells during processing. This precursor is then converted to toxic MBP within eosinophil granules.

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Area of Science:

  • Immunology
  • Molecular Biology
  • Biochemistry

Background:

  • Eosinophils are key immune cells involved in defense against parasites.
  • Eosinophil granule major basic protein (MBP) is a potent cytotoxic molecule.
  • The precise mechanism of MBP synthesis and its potential precursor form were not fully elucidated.

Purpose of the Study:

  • To isolate and characterize the cDNA for human eosinophil major basic protein (MBP).
  • To investigate the precursor forms of MBP during its synthesis and processing.
  • To understand how eosinophils protect themselves from the cytotoxic effects of MBP.

Main Methods:

  • Isolation of human MBP cDNA from a HL-60 cell line library.
  • Nucleotide sequencing of the MBP cDNA.

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  • Bioinformatic analysis to predict protein structure, isoelectric points (pI), and processing pathways.

    • Main Results:

    • Human MBP is translated as a 25.2-kD preproprotein, not the mature 13.8-kD toxic form.
    • The precursor contains a 9.9-kD anionic pro-portion (pI 3.9) and a cationic mature MBP region (pI 10.9).
    • The precursor form (proMBP, pI 6.2) likely protects the eosinophil from MBP's toxicity during intracellular processing.

    Conclusions:

    • MBP is synthesized as a nontoxic precursor that is processed within the endoplasmic reticulum and granules.
    • This precursor-mediated processing mechanism protects the host eosinophil from self-damage.
    • Similar processing strategies may be employed by other cationic toxins.