Previous Article | Next Article ![]()
Infection and Immunity, February 2009, p. 657-666, Vol. 77, No. 2
0019-9567/09/$08.00+0 doi:10.1128/IAI.00819-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

and
Christopher Elkins*
Department of Medicine, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599
Received 2 July 2008/ Returned for modification 13 August 2008/ Accepted 4 November 2008
Resisting the bactericidal activity of naturally occurring antibodies and complement of normal human serum is an important element in the evasion of innate immunity by bacteria. In the gram-negative mucosal pathogen Haemophilus ducreyi, serum resistance is mediated primarily by the trimeric autotransporter DsrA. DsrA also functions as an adhesin for the extracellular matrix proteins fibronectin and vitronectin and mediates attachment of H. ducreyi to keratinocytes. We sought to determine the domain(s) of the 236-residue DsrA protein required for serum resistance and extracellular matrix protein binding. A 140-amino-acid truncated protein containing only the C-terminal portion of the passenger domain and the entire translocator domain of DsrA exhibited binding to fibronectin and vitronectin and conferred serum resistance to an H. ducreyi serum-sensitive strain. A shorter DsrA construct consisting of only 128 amino acids was unable to bind to extracellular matrix proteins but was serum resistant. We concluded that neither fibronectin binding nor vitronectin binding is required for high-level serum resistance in H. ducreyi.
Published ahead of print on 17 November 2008.
Present address: Department of Pediatrics, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599.
This article has been cited by other articles:
Copyright © 2009 by the American Society for Microbiology. For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»