Leptospira interrogans endostatin-like outer membrane proteins bind host fibronectin, laminin and regulators of complement.
The pathogenic spirochete Leptospira interrogans disseminates throughout its hosts via the bloodstream, then invades and colonizes a variety of host tissues. Infectious leptospires are resistant to killing by their hosts' alternative pathway of complement-mediated killing, and interact with var...
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2007-11-01
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doaj-cf75645695ac434ebc9eb6f2120bffb22020-11-24T22:06:40ZengPublic Library of Science (PLoS)PLoS ONE1932-62032007-11-01211e118810.1371/journal.pone.0001188Leptospira interrogans endostatin-like outer membrane proteins bind host fibronectin, laminin and regulators of complement.Brian StevensonHenry A ChoyMarija PinneMatthew L RotondiM Clarke MillerEdward DemollPeter KraiczyAnne E CooleyTrevor P CreamerMarc A SuchardCatherine A BrissetteAshutosh VermaDavid A HaakeThe pathogenic spirochete Leptospira interrogans disseminates throughout its hosts via the bloodstream, then invades and colonizes a variety of host tissues. Infectious leptospires are resistant to killing by their hosts' alternative pathway of complement-mediated killing, and interact with various host extracellular matrix (ECM) components. The LenA outer surface protein (formerly called LfhA and Lsa24) was previously shown to bind the host ECM component laminin and the complement regulators factor H and factor H-related protein-1. We now demonstrate that infectious L. interrogans contain five additional paralogs of lenA, which we designated lenB, lenC, lenD, lenE and lenF. All six genes encode domains predicted to bear structural and functional similarities with mammalian endostatins. Sequence analyses of genes from seven infectious L. interrogans serovars indicated development of sequence diversity through recombination and intragenic duplication. LenB was found to bind human factor H, and all of the newly-described Len proteins bound laminin. In addition, LenB, LenC, LenD, LenE and LenF all exhibited affinities for fibronectin, a distinct host extracellular matrix protein. These characteristics suggest that Len proteins together facilitate invasion and colonization of host tissues, and protect against host immune responses during mammalian infection.http://europepmc.org/articles/PMC2063517?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Brian Stevenson Henry A Choy Marija Pinne Matthew L Rotondi M Clarke Miller Edward Demoll Peter Kraiczy Anne E Cooley Trevor P Creamer Marc A Suchard Catherine A Brissette Ashutosh Verma David A Haake |
spellingShingle |
Brian Stevenson Henry A Choy Marija Pinne Matthew L Rotondi M Clarke Miller Edward Demoll Peter Kraiczy Anne E Cooley Trevor P Creamer Marc A Suchard Catherine A Brissette Ashutosh Verma David A Haake Leptospira interrogans endostatin-like outer membrane proteins bind host fibronectin, laminin and regulators of complement. PLoS ONE |
author_facet |
Brian Stevenson Henry A Choy Marija Pinne Matthew L Rotondi M Clarke Miller Edward Demoll Peter Kraiczy Anne E Cooley Trevor P Creamer Marc A Suchard Catherine A Brissette Ashutosh Verma David A Haake |
author_sort |
Brian Stevenson |
title |
Leptospira interrogans endostatin-like outer membrane proteins bind host fibronectin, laminin and regulators of complement. |
title_short |
Leptospira interrogans endostatin-like outer membrane proteins bind host fibronectin, laminin and regulators of complement. |
title_full |
Leptospira interrogans endostatin-like outer membrane proteins bind host fibronectin, laminin and regulators of complement. |
title_fullStr |
Leptospira interrogans endostatin-like outer membrane proteins bind host fibronectin, laminin and regulators of complement. |
title_full_unstemmed |
Leptospira interrogans endostatin-like outer membrane proteins bind host fibronectin, laminin and regulators of complement. |
title_sort |
leptospira interrogans endostatin-like outer membrane proteins bind host fibronectin, laminin and regulators of complement. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS ONE |
issn |
1932-6203 |
publishDate |
2007-11-01 |
description |
The pathogenic spirochete Leptospira interrogans disseminates throughout its hosts via the bloodstream, then invades and colonizes a variety of host tissues. Infectious leptospires are resistant to killing by their hosts' alternative pathway of complement-mediated killing, and interact with various host extracellular matrix (ECM) components. The LenA outer surface protein (formerly called LfhA and Lsa24) was previously shown to bind the host ECM component laminin and the complement regulators factor H and factor H-related protein-1. We now demonstrate that infectious L. interrogans contain five additional paralogs of lenA, which we designated lenB, lenC, lenD, lenE and lenF. All six genes encode domains predicted to bear structural and functional similarities with mammalian endostatins. Sequence analyses of genes from seven infectious L. interrogans serovars indicated development of sequence diversity through recombination and intragenic duplication. LenB was found to bind human factor H, and all of the newly-described Len proteins bound laminin. In addition, LenB, LenC, LenD, LenE and LenF all exhibited affinities for fibronectin, a distinct host extracellular matrix protein. These characteristics suggest that Len proteins together facilitate invasion and colonization of host tissues, and protect against host immune responses during mammalian infection. |
url |
http://europepmc.org/articles/PMC2063517?pdf=render |
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