A Purified Aspartic Protease from Akkermansia Muciniphila Plays an Important Role in Degrading Muc2

Xin Meng1, Wencheng Wang1, Tianqi Lan1

  • 1Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, College of Life Science, Jilin University, 2699 Qianjin Street, Changchun 130012, China.

Insights

Akkermansia muciniphila

Area of Science:

  • Microbiology
  • Biochemistry
  • Gastroenterology

Background:

  • Akkermansia muciniphila produces mucin-degrading proteins, but their functions are not fully understood.
  • The gene Amuc_1434 encodes a hypothetical protein of interest for mucin degradation studies.

Purpose of the Study:

  • To characterize the recombinant Amuc_1434 protein (Amuc_1434*) from Akkermansia muciniphila.
  • To investigate the role of Amuc_1434* in mucin degradation and its potential impact on gut barrier function.

Main Methods:

  • Production and purification of recombinant Amuc_1434* from Escherichia coli.
  • Biochemical characterization including enzyme activity assays, optimal pH and temperature determination.
  • Inhibition assays using pepstatin A and assessment of effects on colon cancer cell line LS174T and Muc2 degradation.

Main Results:

  • Amuc_1434* exhibits hemoglobin hydrolysis activity (17.21 U/μg) with optimal conditions at pH 8.0 and 40 °C.
  • Amuc_1434* is identified as an aspartic protease sensitive to pepstatin A.
  • Amuc_1434* promotes LS174T cell adhesion and degrades Muc2, the major mucin in the colon.

Conclusions:

  • Amuc_1434* is a functional aspartic protease from Akkermansia muciniphila with mucin-degrading capabilities.
  • The findings suggest Amuc_1434 may contribute to restoring gut barrier function by reducing mucus layer thickness.

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