Partial Complementation of Sinorhizobium meliloti bacA Mutant Phenotypes by the Mycobacterium tuberculosis BacA Protein

Author:

Arnold M. F. F.1,Haag A. F.1,Capewell S.2,Boshoff H. I.3,James E. K.4,McDonald R.1,Mair I.2,Mitchell A. M.5,Kerscher B.1,Mitchell T. J.5,Mergaert P.6,Barry C. E.3,Scocchi M.7,Zanda M.89,Campopiano D. J.2,Ferguson G. P.1

Affiliation:

1. School of Medicine & Dentistry, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen, United Kingdom

2. EastChem School of Chemistry, University of Edinburgh, Edinburgh, United Kingdom

3. Tuberculosis Research Section, NIAID, Bethesda, Maryland, USA

4. The James Hutton Institute, Invergowrie, Dundee, United Kingdom

5. School of Immunity and Infection, College of Medical and Dental Sciences, University of Birmingham, Edgbaston, Birmingham, United Kingdom

6. Institut des Sciences du Végétal, Centre National de la Recherche Scientifique, Gif-sur-Yvette, France

7. Department of Life Sciences, University of Trieste, Trieste, Italy

8. School of Medical Sciences, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen, United Kingdom

9. C.N.R. Istituto di Chimica del Riconoscimento Molecolare, Milan, Italy

Abstract

ABSTRACT The Sinorhizobium meliloti BacA ABC transporter protein plays an important role in its nodulating symbiosis with the legume alfalfa ( Medicago sativa ). The Mycobacterium tuberculosis BacA homolog was found to be important for the maintenance of chronic murine infections, yet its in vivo function is unknown. In the legume plant as well as in the mammalian host, bacteria encounter host antimicrobial peptides (AMPs). We found that the M. tuberculosis BacA protein was able to partially complement the symbiotic defect of an S. meliloti BacA-deficient mutant on alfalfa plants and to protect this mutant in vitro from the antimicrobial activity of a synthetic legume peptide, NCR247, and a recombinant human β-defensin 2 (HBD2). This finding was also confirmed using an M. tuberculosis insertion mutant. Furthermore, M. tuberculosis BacA-mediated protection of the legume symbiont S. meliloti against legume defensins as well as HBD2 is dependent on its attached ATPase domain. In addition, we show that M. tuberculosis BacA mediates peptide uptake of the truncated bovine AMP, Bac7 1-16 . This process required a functional ATPase domain. We therefore suggest that M. tuberculosis BacA is important for the transport of peptides across the cytoplasmic membrane and is part of a complete ABC transporter. Hence, BacA-mediated protection against host AMPs might be important for the maintenance of latent infections.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

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