Title: Direct activation of a phospholipase by cyclic GMP-AMP in El Tor Vibrio cholerae

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America
 [1];  [2];  [3]; ORCiD logo [4];  [5];  [5];  [6];  [2];  [5];  [6]; ORCiD logo [4];  [5]; ORCiD logo [2]
  1. Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824,
  2. Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA 02111,, Graduate Program in Molecular Microbiology, Tufts Sackler School of Biomedical Sciences, Boston, MA 02111,
  3. Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA 02111,
  4. Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824,, Michigan State University–Department of Energy Plant Research Laboratory, Michigan State University, East Lansing, MI 48824,
  5. Department of Microbiology and Molecular Genetics, Michigan State University, East Lansing, MI 48824,
  6. Department of Microbiology, Biochemistry, and Molecular Genetics, New Jersey Medical School, Rutgers, The State University of New Jersey, Newark, NJ 07103

Significance Second messengers are employed by all organisms to regulate fundamental behaviors, including biofilm formation, motility, metabolism, and pathogenesis in bacteria. We have identified a phospholipase in the El Tor Vibrio cholerae biotype, responsible for the current cholera pandemic, that is directly activated by the second messenger 3′, 3′-cyclic GMP-AMP (cGAMP). Discovery of this proteinaceous bacterial cGAMP effector sheds light on the functions and basic principles of cGAMP signaling. Both this phospholipase and the cGAMP synthase are encoded within the VSP-1 pathogenicity island, unique to the El Tor biotype, and our findings assign a biochemical function to VSP-1 that may contribute to the epidemiological success of El Tor V. cholerae .

Research Organization:
Michigan State Univ., East Lansing, MI (United States). MSU-DOE Plant Research Lab.
Sponsoring Organization:
National Institutes of Health (NIH); USDOE; USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
Grant/Contract Number:
FG02-91ER20021; FG02-98ER20305
OSTI ID:
1441128
Journal Information:
Proceedings of the National Academy of Sciences of the United States of America, Journal Name: Proceedings of the National Academy of Sciences of the United States of America Journal Issue: 26 Vol. 115; ISSN 0027-8424
Publisher:
Proceedings of the National Academy of SciencesCopyright Statement
Country of Publication:
United States
Language:
English

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