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The lethal cargo of Myxococcus xanthus outer membrane vesicles

Journal Article · · Frontiers in Microbiology
 [1];  [2];  [3];  [3];  [3];  [3];  [4];  [5];  [3];  [2];  [3]
  1. Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Life Sciences Division; Univ. of California, Berkeley, CA (United States). Dept. of Molecular and Cell Biology; St. Mary's College, Morgana, CA (United States). School of Biology; DOE/OSTI
  2. Univ. of California, San Francisco, CA (United States). Sandler-Moore Mass Spectrometry Core Facility. Dept. of Obstetrics, Gynecology and Reproductive Science
  3. Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Life Sciences Division
  4. Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Life Sciences Division; NASA Ames Research Center (ARC), Moffett Field, Mountain View, CA (United States). Synthetic Biology Program. Space Biosciences Division; Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Physical Biosciences Division
  5. Univ. of California, Berkeley, CA (United States). Dept. of Molecular and Cell Biology
Myxococcus xanthus is a bacterial micro-predator known for hunting other microbes in a wolf pack-like manner. Outer membrane vesicles (OMVs) are produced in large quantities by M. xanthus and have a highly organized structure in the extracellular milieu, sometimes occurring in chains that link neighboring cells within a biofilm. OMVs may be a vehicle for mediating wolf pack activity by delivering hydrolytic enzymes and antibiotics aimed at killing prey microbes. Here, both the protein and small molecule cargo of the OMV and membrane fractions of M. xanthus were characterized and compared. Our analysis indicates a number of proteins that are OMV-specific or OMV-enriched, including several with putative hydrolytic function. Secondary metabolite profiling of OMVs identifies 16 molecules, many associated with antibiotic activities. Several hydrolytic enzyme homologs were identified, including the protein encoded by MXAN_3564 (mepA), an M36 protease homolog. Genetic disruption of mepA leads to a significant reduction in extracellular protease activity suggesting MepA is part of the long-predicted (yet to date undetermined) extracellular protease suite of M. xanthus.
Research Organization:
Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science Division
Grant/Contract Number:
AC02-05CH11231
OSTI ID:
1628119
Journal Information:
Frontiers in Microbiology, Journal Name: Frontiers in Microbiology Vol. 5; ISSN 1664-302X
Publisher:
Frontiers Research FoundationCopyright Statement
Country of Publication:
United States
Language:
English

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Bacterial outer membrane vesicles, a potential vaccine candidate in interactions with host cells based journal December 2018
Kin discrimination and outer membrane exchange in Myxococcus xanthus: Experimental analysis of a natural population journal November 2019
Ecology and evolution of metabolic cross-feeding interactions in bacteria text January 2018
Bacterial predator-prey coevolution accelerates genome evolution and selects on virulence-associated prey defences text January 2019