dc.contributor.author
Kao, Wei-Chien Andrew
dc.contributor.author
Petrosova, Helena
dc.contributor.author
Ebady, Rhodaba
dc.contributor.author
Lithgow, Karen V.
dc.contributor.author
Rojas, Pablo
dc.contributor.author
Zhang, Yang
dc.contributor.author
Kim, Yae-Eun
dc.contributor.author
Kim, Yae-Ram
dc.contributor.author
Odisho, Tanya
dc.contributor.author
Gupta, Nupur
dc.contributor.author
Moter, Annette
dc.contributor.author
Cameron, Caroline E.
dc.contributor.author
Moriarty, Tara J.
dc.date.accessioned
2018-06-08T10:58:40Z
dc.date.available
2017-09-04T11:05:47.752Z
dc.identifier.uri
https://refubium.fu-berlin.de/handle/fub188/21429
dc.identifier.uri
http://dx.doi.org/10.17169/refubium-24722
dc.description.abstract
Treponema pallidum subsp. pallidum, the causative agent of syphilis, is a
highly invasive spirochete pathogen that uses the vasculature to disseminate
throughout the body. Identification of bacterial factors promoting
dissemination is crucial for syphilis vaccine development. An important step
in dissemination is bacterial adhesion to blood vessel surfaces, a process
mediated by bacterial proteins that can withstand forces imposed on adhesive
bonds by blood flow (vascular adhesins). The study of T. pallidum vascular
adhesins is hindered by the uncultivable nature of this pathogen. We overcame
these limitations by expressing T. pallidum adhesin Tp0751 (pallilysin) in an
adhesion-attenuated strain of the cultivable spirochete Borrelia burgdorferi.
Under fluid shear stress representative of conditions in postcapillary
venules, Tp0751 restored bacterial-vascular interactions to levels similar to
those observed for infectious B. burgdorferi and a gain-of-function strain
expressing B. burgdorferi vascular adhesin BBK32. The strength and stability
of Tp0751- and BBK32-dependent endothelial interactions under physiological
shear stress were similar, although the mechanisms stabilizing these
interactions were distinct. Tp0751 expression also permitted bacteria to
interact with postcapillary venules in live mice as effectively as
BBK32-expressing strains. These results demonstrate that Tp0751 can function
as a vascular adhesin.
en
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.subject.ddc
600 Technik, Medizin, angewandte Wissenschaften::610 Medizin und Gesundheit
dc.title
Identification of Tp0751 (Pallilysin) as a Treponema pallidum Vascular Adhesin
by Heterologous Expression in the Lyme disease Spirochete
dc.type
Wissenschaftlicher Artikel
dcterms.bibliographicCitation
Scientific Reports. - 7 (2017), Artikel Nr. 1538
dcterms.bibliographicCitation.doi
10.1038/s41598-017-01589-4
dcterms.bibliographicCitation.url
http://www.nature.com/articles/s41598-017-01589-4
refubium.affiliation
Charité - Universitätsmedizin Berlin
de
refubium.mycore.fudocsId
FUDOCS_document_000000027813
refubium.note.author
Der Artikel wurde in einer reinen Open-Access-Zeitschrift publiziert.
refubium.resourceType.isindependentpub
no
refubium.mycore.derivateId
FUDOCS_derivate_000000008696
dcterms.accessRights.openaire
open access