TY  - JOUR
A1  - Stevenson, Brian
A1  - Choy, Henry A.
A1  - Pinne, Marija
A1  - Rotondi, Matthew L.
A1  - Miller, M. Clarke
A1  - DeMoll, Edward
A1  - Kraiczy, Peter
A1  - Cooley, Anne E.
A1  - Creamer, Trevor P.
A1  - Suchard, Marc A.
A1  - Brissette, Catherine A.
A1  - Verma, Ashutosh
A1  - Haake, David A.
T1  - Leptospira interrogans endostatin-like outer membrane proteins bind host fibronectin, laminin and regulators of complement
T2  - PLoS One
N2  - 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.
Y1  - 2007
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/22659
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30-115033
SN  - 1932-6203
N1  - This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose.
VL  - 2
IS  - (11): e1188
ER  -