Borrelia burgdorferi enolase is a surface-exposed plasminogen binding protein.

Borrelia burgdorferi is the causative agent of Lyme disease, the most commonly reported arthropod-borne disease in the United States. B. burgdorferi is a highly invasive bacterium, yet lacks extracellular protease activity. In order to aid in its dissemination, B. burgdorferi binds plasminogen, a co...

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Autores principales:	Angela M Floden, John A Watt, Catherine A Brissette
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/a3d4ab4226744076bc00ba7b732c6b5c
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spelling	oai:doaj.org-article:a3d4ab4226744076bc00ba7b732c6b5c2021-11-18T07:34:43ZBorrelia burgdorferi enolase is a surface-exposed plasminogen binding protein.1932-620310.1371/journal.pone.0027502https://doaj.org/article/a3d4ab4226744076bc00ba7b732c6b5c2011-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22087329/?tool=EBIhttps://doaj.org/toc/1932-6203Borrelia burgdorferi is the causative agent of Lyme disease, the most commonly reported arthropod-borne disease in the United States. B. burgdorferi is a highly invasive bacterium, yet lacks extracellular protease activity. In order to aid in its dissemination, B. burgdorferi binds plasminogen, a component of the hosts' fibrinolytic system. Plasminogen bound to the surface of B. burgdorferi can then be activated to the protease plasmin, facilitating the bacterium's penetration of endothelial cell layers and degradation of extracellular matrix components. Enolases are highly conserved proteins with no sorting sequences or lipoprotein anchor sites, yet many bacteria have enolases bound to their outer surfaces. B. burgdorferi enolase is both a cytoplasmic and membrane associated protein. Enolases from other pathogenic bacteria are known to bind plasminogen. We confirmed the surface localization of B. burgdorferi enolase by in situ protease degradation assay and immunoelectron microscopy. We then demonstrated that B. burgdorferi enolase binds plasminogen in a dose-dependent manner. Lysine residues were critical for binding of plasminogen to enolase, as the lysine analog εaminocaproic acid significantly inhibited binding. Ionic interactions did not play a significant role in plasminogen binding by enolase, as excess NaCl had no effects on the interaction. Plasminogen bound to recombinant enolase could be converted to active plasmin. We conclude that B. burgdorferi enolase is a moonlighting cytoplasmic protein which also associates with the bacterial outer surface and facilitates binding to host plasminogen.Angela M FlodenJohn A WattCatherine A BrissettePublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 11, p e27502 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Angela M Floden John A Watt Catherine A Brissette Borrelia burgdorferi enolase is a surface-exposed plasminogen binding protein.
description	Borrelia burgdorferi is the causative agent of Lyme disease, the most commonly reported arthropod-borne disease in the United States. B. burgdorferi is a highly invasive bacterium, yet lacks extracellular protease activity. In order to aid in its dissemination, B. burgdorferi binds plasminogen, a component of the hosts' fibrinolytic system. Plasminogen bound to the surface of B. burgdorferi can then be activated to the protease plasmin, facilitating the bacterium's penetration of endothelial cell layers and degradation of extracellular matrix components. Enolases are highly conserved proteins with no sorting sequences or lipoprotein anchor sites, yet many bacteria have enolases bound to their outer surfaces. B. burgdorferi enolase is both a cytoplasmic and membrane associated protein. Enolases from other pathogenic bacteria are known to bind plasminogen. We confirmed the surface localization of B. burgdorferi enolase by in situ protease degradation assay and immunoelectron microscopy. We then demonstrated that B. burgdorferi enolase binds plasminogen in a dose-dependent manner. Lysine residues were critical for binding of plasminogen to enolase, as the lysine analog εaminocaproic acid significantly inhibited binding. Ionic interactions did not play a significant role in plasminogen binding by enolase, as excess NaCl had no effects on the interaction. Plasminogen bound to recombinant enolase could be converted to active plasmin. We conclude that B. burgdorferi enolase is a moonlighting cytoplasmic protein which also associates with the bacterial outer surface and facilitates binding to host plasminogen.
format	article
author	Angela M Floden John A Watt Catherine A Brissette
author_facet	Angela M Floden John A Watt Catherine A Brissette
author_sort	Angela M Floden
title	Borrelia burgdorferi enolase is a surface-exposed plasminogen binding protein.
title_short	Borrelia burgdorferi enolase is a surface-exposed plasminogen binding protein.
title_full	Borrelia burgdorferi enolase is a surface-exposed plasminogen binding protein.
title_fullStr	Borrelia burgdorferi enolase is a surface-exposed plasminogen binding protein.
title_full_unstemmed	Borrelia burgdorferi enolase is a surface-exposed plasminogen binding protein.
title_sort	borrelia burgdorferi enolase is a surface-exposed plasminogen binding protein.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/a3d4ab4226744076bc00ba7b732c6b5c
work_keys_str_mv	AT angelamfloden borreliaburgdorferienolaseisasurfaceexposedplasminogenbindingprotein AT johnawatt borreliaburgdorferienolaseisasurfaceexposedplasminogenbindingprotein AT catherineabrissette borreliaburgdorferienolaseisasurfaceexposedplasminogenbindingprotein
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Borrelia burgdorferi enolase is a surface-exposed plasminogen binding protein.

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