Uncovering the Secrets of Tularemia, the "Rabbit Fever"
Researchers at Lawrence Livermore National Laboratory Solve Structures that Shed Light on how the Bacteria May Persist in the Environment and Cause Disease
Embargo expired: 16-Feb-2014 4:45 PM EST
Source Newsroom: Biophysical Society
Newswise — WASHINGTON D.C. Feb. 16, 2014 -- Tularemia, aka "rabbit fever," is endemic in the northeastern United States, and is considered to be a significant risk to biosecurity -- much like anthrax or smallpox -- because it has already been weaponized in various regions of the world.
At the 58th Annual Biophysical Society Meeting, which takes place Feb. 15-19, 2014, in San Francisco, Calif., Geoffrey K. Feld, a Postdoctoral researcher in the Physical & Life Sciences Directorate at Lawrence Livermore National Laboratory (LLNL), will describe his work to uncover the secrets of the bacterium Francisella tularensis, which causes tularemia.
"Despite its importance for both public health and biodefense, F. tularensis pathogenesis isn't entirely understood, nor do we fully understand how the organism persists in the environment," explained Feld.
Previous efforts, funded by both the National Institutes of Health and LLNL, demonstrated that amoebae may serve as a potential reservoir for the bacteria in nature. "Specifically, we demonstrated that amoebae exposed to fully virulent F. tularensis rapidly form cysts -- dormant, metabolically inactive cells -- that allow the amoebae to survive unfavorable conditions," said Amy Rasley, the research team leader.
This encystment phenotype was rapidly induced by F. tularensis in the laboratory and was required for the long-term survival of the bacteria. Further exploration led to the identification of secreted F. tularensis proteins, which are responsible for induction of the rapid encystment phenotype (REP) observed in amoebae.
In the new work, Feld and colleagues characterized two of these REP proteins -- called REP24 and REP34 -- and began to describe their functions based on their three-dimensional crystal structures.
A big surprise finding was that these proteins resembled "proteases," which are proteins that cut other proteins in a specific manner. "Our preliminary data indicate that F. tularensis bacteria lacking these proteins are diminished in their ability to infect or survive in human immune cells, which indicates that these proteins may also contribute to F. tularensis virulence," Feld said.
Rasley and colleagues believe that careful characterization of these two novel F. tularensis proteins may shed light on how this organism persists in the environment and causes disease.
"Ultimately, this type of research could inform efforts to combat the disease, although there is much work to do. Currently, we don't know the protein targets in the host -- amoeba, human, etc. -- that the REP proteins act on, nor do we know the mechanism by which the proteins could help F. tularensis survive in the environment or cause disease," Feld said.
"Once these questions are elucidated, a broader understanding of environmental persistence and pathogenesis might lead to better diagnostics and/or novel countermeasures to combat tularemia," he added.
The presentation "Structure and Function of Two Putative Virulence Factors from Francisella tularensis" by Geoffrey K. Feld will be at 1:45 p.m. on Sunday, February 16, 2014 in Hall D in San Francisco's Moscone Convention Center.
More information about Tularemia from the CDC: http://www.cdc.gov/tularemia
ABOUT THE MEETING
Each year, the Biophysical Society Annual Meeting brings together more than 7,000 researchers working in the multidisciplinary fields representing biophysics. With more than 4,200 poster presentations, over 200 exhibits, and more than 20 symposia, the BPS Annual Meeting is the largest meeting of biophysicists in the world. Despite its size, the meeting retains its small-meeting flavor through its subgroup symposia, platform sessions, social activities, and committee programs.
The 58th Annual Meeting will be held at the Moscone Convention Center, 747 Howard Street, San Francisco, California.
The Biophysical Society invites professional journalists, freelance science writers and public information officers to attend its Annual Meeting free of charge. For press registration, contact Alisha Yocum at firstname.lastname@example.org or Jason Bardi at 240-535-4954.
ABOUT THE SOCIETY
The Biophysical Society, founded in 1958, is a professional, scientific Society established to encourage development and dissemination of knowledge in biophysics. The Society promotes growth in this expanding field through its annual meeting, monthly journal, and committee and outreach activities. Its 9000 members are located throughout the U.S. and the world, where they teach and conduct research in colleges, universities, laboratories, government agencies, and industry. For more information on the Society, or the 2014 Annual Meeting, visit www.biophysics.org