Identification of aTreponema pallidumLaminin-Binding Protein
Open Access
- 1 May 2003
- journal article
- Published by American Society for Microbiology in Infection and Immunity
- Vol. 71 (5) , 2525-2533
- https://doi.org/10.1128/iai.71.5.2525-2533.2003
Abstract
Host extracellular matrix (ECM) components represent ideal microbial adhesion targets that many pathogens use for colonization of tissues and initiation of infection. This study investigated the interaction of the spirocheteTreponema pallidumwith the ECM component laminin. To identify candidate laminin-binding adhesins, theT. pallidumgenome was analyzed to predict open reading frames that encode putative outer membrane proteins, as these proteins interact directly with host ECM components. Subsequent recombinant expression of these proteins and analysis of their laminin-binding potential identified one protein, Tp0751, that demonstrated specific attachment to laminin. Tp0751 attached to laminin in a dose-dependent, saturable manner but did not attach to the ECM component collagen type I or IV or to the negative control proteins fetuin or bovine serum albumin. Sodium metaperiodate treatment of laminin reduced the Tp0751-laminin interaction in a concentration-dependent manner, suggesting that oligosaccharides play a role in this interaction. In addition, Tp0751-specific antibodies were detected in serum samples collected from both experimental and natural syphilis infections, indicating that Tp0751 is expressed in vivo during the course of infection. Collectively, these experiments identified Tp0751 as a laminin-binding protein that is expressed during infection and may be involved in attachment ofT. pallidumto host tissues.Keywords
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