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Infection and Immunity, September 2002, p. 4902-4907, Vol. 70, No. 9
0019-9567/02/$04.00+0     DOI: 10.1128/IAI.70.9.4902-4907.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

The Haemophilus influenzae Hap Autotransporter Binds to Fibronectin, Laminin, and Collagen IV

Doran L. Fink,1,2 Bruce A. Green,3 and Joseph W. St. Geme III1,2*

Edward Mallinckrodt Department of Pediatrics,1 Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, Missouri 63110,2 Wyeth-Lederle Vaccines, West Henrietta, New York 145863

Received 1 March 2002/ Returned for modification 2 April 2002/ Accepted 4 June 2002

Nontypeable Haemophilus influenzae (NTHI) initiates infection by colonizing the upper respiratory tract mucosa. NTHI disease frequently occurs in the context of respiratory tract inflammation, where organisms encounter damaged epithelium and exposed basement membrane. In this study, we examined interactions between the H. influenzae Hap adhesin and selected extracellular matrix proteins. Hap is an autotransporter protein that undergoes autoproteolytic cleavage, with release of the adhesive passenger domain, Haps, from the bacterial cell surface. We found that Hap promotes bacterial adherence to purified fibronectin, laminin, and collagen IV and that Hap-mediated adherence is enhanced by inhibition of autoproteolysis. Adherence is inhibited by pretreatment of bacteria with a polyclonal antiserum recognizing Haps. Purified Haps binds with high affinity to fibronectin, laminin, and collagen IV but not to collagen II. Binding of Haps to fibronectin involves interaction with the 45-kDa gelatin-binding domain but not the 30-kDa heparin-binding domain of fibronectin. Taken together, these observations suggest that interactions between Hap and extracellular matrix proteins may play an important role in NTHI colonization of the respiratory tract.

* Corresponding author. Mailing address: Department of Pediatrics, Washington University School of Medicine, 660 South Euclid Ave., Campus Box 8208, St. Louis, MO 63110. Phone: (314) 286-2887. Fax: (314) 286-2895. E-mail: stgeme{at}borcim.wustl.edu.

Editor: D. L. Burns

Infection and Immunity, September 2002, p. 4902-4907, Vol. 70, No. 9
0019-9567/02/$04.00+0     DOI: 10.1128/IAI.70.9.4902-4907.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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