Functional Analysis of the Mycobacterium tuberculosis Protein PE_PGRS

Authors

    Kazunori Matsumura, Hiroki Iwai, Teruo Kirikae Department of Diseases Control, Research Institute, National Center for Global Health and Medicine, Shinjuku, Tokyo 162-8655, Japan Department of Infectious Diseases, Research Institute, National Center for Global Health and Medicine, Shinjuku, Tokyo 162-8655, Japan Department of Microbiology, Juntendo University School of Medicine, Bunkyo, Tokyo 113-8421, Japan

Keywords:

Mycobacterium tuberculosis, PE_PGRS, Autophagy, Cell death

Abstract

Tuberculosis (TB) remains an important infectious disease, causing ten million new cases and 1.4 million deaths a year worldwide. Elucidating the pathogenicity of Mycobacterium tuberculosis, the causative agent of TB will contribute to the development of new drugs, vaccines, and treatments. Prolineglutamic acid (PE)/proline-proline-glutamic acid (PPE) family accounts for approximately 10% of the coding region of the M. tuberculosis genome and its functions are largely unknown. PE proteins having polymorphic GC-rich repetitive sequences (PGRS) in the carboxyl-terminal are members of the PE_PGRS family. PE_PGRS62 and PE_PGRS30 are members of the PE_PGRS family and homologs of MAG24, the virulence factor of M. marinum. We are in the process of analyzing the functions of PE_PGRS62 and PE_PGRS30 and have results suggesting that PE_PGRS62 regulates autophagy, whereas PE_PGRS30 induces cell death.

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Published

2021-12-31