Journal
JOURNAL OF INFECTIOUS DISEASES
Volume 211, Issue 3, Pages 462-471Publisher
OXFORD UNIV PRESS INC
DOI: 10.1093/infdis/jiu460
Keywords
Borrelia burgdorferi; BB0238; BB0323; protein-protein interaction; posttranslational stability; pathogen persistence
Categories
Funding
- National Institute of Allergy and Infectious Diseases [R01AI080615]
- Grants-in-Aid for Scientific Research [25461982] Funding Source: KAKEN
Ask authors/readers for more resources
We have shown that Borrelia burgdorferi gene product BB0323 is essential for cell fission and pathogen persistence in vivo. Here we describe characterization of a conserved hypothetical protein annotated as BB0238, which specifically interacts with the N-terminal region of BB0323. We show that BB0238 is a subsurface protein, and similar to BB0323, exists in the periplasm and as a membrane-bound protein. Deletion of bb0238 in infectious B. burgdorferi did not affect microbial growth in vitro or survival in ticks, but the mutant was unable to persist in mice or transmit from ticks-defects that are restored on genetic complementation. Remarkably, BB0238 and BB0323 contribute to mutual posttranslational stability, because deletion of one causes dramatic reduction in the protein level of the other partner. Interference with the function of BB0238 or BB0323 and their interaction may provide novel strategies to combat B. burgdorferi infection.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available