Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 105, Issue 39, Pages 15088-15093Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0805666105
Keywords
peptidoglycan recognition protein LB; Sodalis glossinidius; tsetse
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Funding
- University of Arizona, Tucson, AZ
- Institut National de la Recherche Agronomique, Villeurbanne, France
- Institute of Parsitology, Cesk Budejovice, Czech Republic
- Texas A & M University, College Station, TX
- University of California, Santa Barbara, CA [pB33OT4]
- The Saban Research Institute, Los Angeles, CA
- National Institute of Allergy and Infectious Diseases [AI51584]
- National Institute of General Medical Sciences [069449]
- Ambrose Monell Foundation
- Kirschstein-National Research Service [F32AI062680]
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Beneficial bacterial symbioses are ubiquitous in nature. However, the functional and molecular basis of host tolerance to resident symbiotic microbes, in contrast to resistance to closely related bacteria that are recognized as foreign, remain largely unknown. We used the tsetse fly (Glossina morsitans), which depends on symbiotic flora for fecundity and has limited exposure to foreign microbes, to investigate the tolerance phenomenon exhibited during symbiosis. We examined the potential role of bacterium-specific polymorphisms present in the major bacterial surface protein, outer-membrane protein A (OmpA), on host infection outcomes. Tsetse were successfully superinfected with their mutualistic facultative symbiont, Sodalis glossinidius, whereas infections with Escherichia coli K12 were lethal. In contrast, tsetse were resistant to an E. coli OmpA mutant strain, whereas recombinant Sodalis expressing E. coli OmpA became pathogenic. Profiling of tsetse immunity- related gene expression incriminated peptidoglycan recognition protein (pgrp)-Ib as a determinant of the infection outcomes we observed. RNAi-induced knockdown of tsetse pgrp-Ib significantly reduced host mortality after infection with otherwise lethal E. coli K12. Our results show that polymorphisms in the exposed loop domains of OmpA represent a microbial adaptation that mediates host tolerance of endogenous symbiotic bacteria.
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