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The search for Brachyspira outer membrane proteins that interact with the host

Published online by Cambridge University Press:  28 February 2007

Darren J. Trott ,
David P. Alt ,
Richard L. Zuerner ,
Michael J. Wannemuehler  and
Thaddeus B. Stanton
Darren J. Trott*
Affiliation:
Bacterial Diseases of Livestock Research Unit, National Animal Disease Center, Ames, Iowa, USA
David P. Alt
Affiliation:
Bacterial Diseases of Livestock Research Unit, National Animal Disease Center, Ames, Iowa, USA
Richard L. Zuerner
Affiliation:
Bacterial Diseases of Livestock Research Unit, National Animal Disease Center, Ames, Iowa, USA
Michael J. Wannemuehler
Affiliation:
Veterinary Medical Research Institute, Iowa State University, Ames, Iowa, USA
Thaddeus B. Stanton
Affiliation:
Bacterial Diseases of Livestock Research Unit, National Animal Disease Center, Ames, Iowa, USA
*
*Department of Veterinary Pathology and Anatomy School of Veterinary Science, Seddon Building, University of Queensland, Queensland St Lucia 4072, Australia. E-mail: d.trott@mailbox.uq.edu.au
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Abstract

Little is known about the outer membrane structure of Brachyspira hyodysenteriae and Brachyspira pilosicoli or the role of outer membrane proteins (OMPs) in host colonization and the development of disease. The isolation of outer membrane vesicles from B. hyodysenteriae has confirmed that cholesterol is a significant outer membrane constituent and that it may impart unique characteristics to the lipid bilayer structure, including a reduced density. Unique proteins that have been identified in the B. hyodysenteriae outer membrane include the variable surface proteins (Vsp) and lipoproteins such as SmpA and BmpB. While the function of these proteins remains to be determined, there is indirect evidence to suggest that they may be involved in immune evasion. These data may explain the ability of the organism to initiate chronic infection. OMPs may be responsible for the unique attachment of B. pilosicoli to colonic epithelial cells; however, the only B. pilosicoli OMPs that have been identified to date are involved in metabolism. In order to identify further B. pilosicoli OMPs we have isolated membrane vesicle fractions from porcine strain 95–1000 by osmotic lysis and isopycnic centrifugation. The fractions were free of contamination by cytoplasm and fla-gella and contained outer membrane. Inner membrane contamination was minimal but could not be completely excluded. An abundant 45-kDa, heat-modifiable protein was shown to have significant homology with B. hyodysenteriae Vsp, and monoclonal antibodies were produced that reacted with five B. pilosicoli-specific membrane protein epitopes. The first of these proteins to be characterized is a unique surface-exposed lipoprotein.

Type
Research Article
Information
Animal Health Research Reviews , Volume 2 , Issue 1 , June 2001 , pp. 19 - 30
Copyright
Copyright © CAB International 2001

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