Nanomechanical mechanisms of Lyme disease spirochete motility enhancement in extracellular matrix

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F21%3A43903619" target="_blank" >RIV/60076658:12310/21:43903619 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60077344:_____/21:00555033

Výsledek na webu

<a href="https://www.nature.com/articles/s42003-021-01783-1" target="_blank" >https://www.nature.com/articles/s42003-021-01783-1</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1038/s42003-021-01783-1" target="_blank" >10.1038/s42003-021-01783-1</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Nanomechanical mechanisms of Lyme disease spirochete motility enhancement in extracellular matrix

Popis výsledku v původním jazyce

As opposed to pathogens passively circulating in the body fluids of their host, pathogenic species within the Spirochetes phylum are able to actively coordinate their movement in the host to cause systemic infections. Based on the unique morphology and high motility of spirochetes, we hypothesized that their surface adhesive molecules might be suitably adapted to aid in their dissemination strategies. Designing a system that mimics natural environmental signals, which many spirochetes face during their infectious cycle, we observed that a subset of their surface proteins, particularly Decorin binding protein (Dbp) A/B, can strongly enhance the motility of spirochetes in the extracellular matrix of the host. Using single-molecule force spectroscopy, we disentangled the mechanistic details of DbpA/B and decorin/laminin interactions. Our results show that spirochetes are able to leverage a wide variety of adhesion strategies through force-tuning transient molecular binding to extracellular matrix components, which concertedly enhance spirochetal dissemination through the host. Martin Strnad, Yoo Jin Oh, and colleagues use single-molecule force spectroscopy and an extracellular matrix (ECM) analog that mimics natural tick feeding to show that the surface proteins DbpA/B can enhance spirochete motility in the ECM of the host. These results show that spirochetes can tune their transient molecular binding to ECM components to enhance spirochetal dissemination through the host.

Název v anglickém jazyce

Nanomechanical mechanisms of Lyme disease spirochete motility enhancement in extracellular matrix

Popis výsledku anglicky

As opposed to pathogens passively circulating in the body fluids of their host, pathogenic species within the Spirochetes phylum are able to actively coordinate their movement in the host to cause systemic infections. Based on the unique morphology and high motility of spirochetes, we hypothesized that their surface adhesive molecules might be suitably adapted to aid in their dissemination strategies. Designing a system that mimics natural environmental signals, which many spirochetes face during their infectious cycle, we observed that a subset of their surface proteins, particularly Decorin binding protein (Dbp) A/B, can strongly enhance the motility of spirochetes in the extracellular matrix of the host. Using single-molecule force spectroscopy, we disentangled the mechanistic details of DbpA/B and decorin/laminin interactions. Our results show that spirochetes are able to leverage a wide variety of adhesion strategies through force-tuning transient molecular binding to extracellular matrix components, which concertedly enhance spirochetal dissemination through the host. Martin Strnad, Yoo Jin Oh, and colleagues use single-molecule force spectroscopy and an extracellular matrix (ECM) analog that mimics natural tick feeding to show that the surface proteins DbpA/B can enhance spirochete motility in the ECM of the host. These results show that spirochetes can tune their transient molecular binding to ECM components to enhance spirochetal dissemination through the host.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2021

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Communications Biology

ISSN

2399-3642

e-ISSN

—

Svazek periodika

4

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

9

Strana od-do

—

Kód UT WoS článku

000626076500001

EID výsledku v databázi Scopus

2-s2.0-85102223579