Targeting protein biotinylation enhances tuberculosis chemotherapy

Author:

Tiwari Divya1ORCID,Park Sae Woong1ORCID,Essawy Maram M.2ORCID,Dawadi Surendra2,Mason Alan3ORCID,Nandakumar Madhumitha4ORCID,Zimmerman Matthew3ORCID,Mina Marizel3ORCID,Ho Hsin Pin3ORCID,Engelhart Curtis A.1ORCID,Ioerger Thomas5ORCID,Sacchettini James C.6ORCID,Rhee Kyu4,Ehrt Sabine1,Aldrich Courtney C.2ORCID,Dartois Véronique37ORCID,Schnappinger Dirk1ORCID

Affiliation:

1. Department of Microbiology and Immunology, Weill Cornell Medical College, New York, NY 10021, USA.

2. Department of Medicinal Chemistry, University of Minnesota, 308 Harvard Street Southeast, 8-174 WDH, Minneapolis, MN 55455, USA.

3. Public Health Research Institute, New Jersey Medical School, Rutgers, State University of New Jersey, Newark, NJ 07103, USA.

4. Weill Department of Medicine, Weill Cornell Medical College, New York, NY 10021, USA.

5. Department of Computer Science and Engineering, Texas A&M University, College Station, TX 77843, USA.

6. Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, USA.

7. Department of Medicine, New Jersey Medical School, Rutgers, State University of New Jersey, Newark, NJ 07103, USA.

Abstract

Inhibitors of biotin protein ligase and protein biotinylation in Mycobacterium tuberculosis act synergistically with the drug rifampicin, potentially shortening tuberculosis treatment.

Funder

National Institute of Allergy and Infectious Diseases

Publisher

American Association for the Advancement of Science (AAAS)

Subject

General Medicine

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