Outer Membrane Vesiculation Facilitates Surface Exchange and In Vivo Adaptation of Vibrio cholerae

Cell Host Microbe. 2020 Feb 12;27(2):225-237.e8. doi: 10.1016/j.chom.2019.12.002. Epub 2019 Dec 31.


Gram-negative bacteria release outer membrane vesicles into the external milieu to deliver effector molecules that alter the host and facilitate virulence. Vesicle formation is driven by phospholipid accumulation in the outer membrane and regulated by the phospholipid transporter VacJ/Yrb. We use the facultative human pathogen Vibrio cholerae to show that VacJ/Yrb is silenced early during mammalian infection, which stimulates vesiculation that expedites bacterial surface exchange and adaptation to the host environment. Hypervesiculating strains rapidly alter their bacterial membrane composition and exhibit enhanced intestinal colonization fitness. This adaptation is exemplified by faster accumulation of glycine-modified lipopolysaccharide (LPS) and depletion of outer membrane porin OmpT, which confers resistance to host-derived antimicrobial peptides and bile, respectively. The competitive advantage of hypervesiculation is lost upon pre-adaptation to bile and antimicrobial peptides, indicating the importance of these adaptive processes. Thus, bacteria use outer membrane vesiculation to exchange cell surface components, thereby increasing survival during mammalian infection.

Keywords: Alm pathway; Mla pathway; OMV; OmpT; OmpU; antimicrobial peptides; bile; glycination; lipid A; porin.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adhesins, Bacterial / metabolism
  • Animals
  • Antimicrobial Cationic Peptides / metabolism
  • Bacterial Outer Membrane / metabolism*
  • Bacterial Outer Membrane Proteins / metabolism
  • Bacterial Proteins / metabolism
  • Bile / metabolism
  • Host Microbial Interactions*
  • Mice
  • Porins / metabolism
  • Transport Vesicles / metabolism*
  • Vibrio cholerae / metabolism
  • Vibrio cholerae / pathogenicity*


  • Adhesins, Bacterial
  • Antimicrobial Cationic Peptides
  • Bacterial Outer Membrane Proteins
  • Bacterial Proteins
  • Porins