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

dc.contributor.author

Zingl, Franz G

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Kohl, Paul

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Cakar, Fatih

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Leitner, Deborah R

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Mitterer, Fabian

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Bonnington, Katherine E

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Rechberger, Gerald N

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Kuehn, Meta J

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Guan, Ziqiang

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Reidl, Joachim

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Schild, Stefan

dc.date.accessioned

2020-02-01T15:16:27Z

dc.date.available

2020-02-01T15:16:27Z

dc.date.issued

2019-12-23

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2020-02-01T15:16:24Z

dc.description.abstract

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.

dc.identifier

S1931-3128(19)30631-6

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1931-3128

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1934-6069

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https://hdl.handle.net/10161/19898

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eng

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Elsevier BV

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Cell host & microbe

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10.1016/j.chom.2019.12.002

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Alm pathway

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Mla pathway

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OMV

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OmpT

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OmpU

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antimicrobial peptides

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bile

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glycination

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lipid A

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porin

dc.title

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

dc.type

Journal article

duke.contributor.orcid

Kuehn, Meta J|0000-0003-0519-3019

duke.contributor.orcid

Guan, Ziqiang|0000-0002-8082-3423

pubs.organisational-group

School of Medicine

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Duke

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Biochemistry

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Basic Science Departments

pubs.publication-status

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