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Infection and Immunity, April 2008, p. 1608-1616, Vol. 76, No. 4
0019-9567/08/$08.00+0     doi:10.1128/IAI.00994-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Outer Membrane Protein DsrA Is the Major Fibronectin-Binding Determinant of Haemophilus ducreyi{triangledown}

Isabelle Leduc,1 C. Dinitra White,1,{dagger} Igor Nepluev,1,{ddagger} Robert E. Throm,2,§ Stanley M. Spinola,2,3,4 and Christopher Elkins1,5*

Departments of Medicine,1 Microbiology and Immunology, School of Medicine, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599,5 Departments of Microbiology and Immunology,2 Medicine,3 Pathology and Laboratory Medicine, Indiana University, Indianapolis, Indiana 462024

Received 20 July 2007/ Returned for modification 22 August 2007/ Accepted 21 December 2007

The ability to bind extracellular matrix proteins is a critical virulence determinant for skin pathogens. Haemophilus ducreyi, the etiological agent of the genital ulcer disease chancroid, binds extracellular matrix components, including fibronectin (FN). We investigated H. ducreyi FN binding and report several important findings about this interaction. First, FN binding by H. ducreyi was greatly increased in bacteria grown on heme and almost completely inhibited by hemoglobin. Second, wild-type strain 35000HP bound significantly more FN than did a dsrA mutant in two different FN binding assays. Third, the expression of dsrA in the dsrA mutant restored FN binding and conferred the ability to bind FN to a non-FN-binding Haemophilus influenzae strain. Fourth, an anti-DsrA monoclonal antibody partially blocked FN binding by H. ducreyi. The hemoglobin receptor, the collagen-binding protein, the H. ducreyi lectin, the fine-tangle pili, and the outer membrane protein OmpA2 were not involved in H. ducreyi FN binding, since single mutants bound FN as well as the parent strain did. However, the major outer membrane protein may have a minor role in FN binding by H. ducreyi, since a double dsrA momp mutant bound less FN than did the single dsrA mutant. Finally, despite major sequence differences, DsrA proteins from both class I and class II H. ducreyi strains mediated FN and vitronectin binding. We concluded that DsrA is the major factor involved in FN binding by both classes of H. ducreyi strains.

* Corresponding author. Mailing address: Department of Medicine, Division of Infectious Diseases, University of North Carolina at Chapel Hill, 8341C MBRB, 103 Mason Farm Rd., CB#7031, Chapel Hill, NC 27599-7031. Phone: (919) 843-5521. Fax: (919) 843-1015. E-mail: chriselk{at}med.unc.edu

{triangledown} Published ahead of print on 22 January 2008.

Editor: J. N. Weiser

{dagger} Present address: Department of Biology, North Carolina Agricultural and Technical State University, Greensboro, NC 27411.

{ddagger} Present address: Department of Medicine, Division of Cardiovascular Medicine, Duke University, Durham, NC 27704.

§ Present address: Department of Hematology, St. Jude Children's Hospital, Memphis, TN 38105.

Infection and Immunity, April 2008, p. 1608-1616, Vol. 76, No. 4
0019-9567/08/$08.00+0     doi:10.1128/IAI.00994-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Leduc, I., Olsen, B., Elkins, C. (2009). Localization of the Domains of the Haemophilus ducreyi Trimeric Autotransporter DsrA Involved in Serum Resistance and Binding to the Extracellular Matrix Proteins Fibronectin and Vitronectin. Infect. Immun. 77: 657-666 [Abstract] [Full Text]  


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