Infection and Immunity, August 2005, p. 5127-5136, Vol. 73, No. 8
0019-9567/05/$08.00+0 doi:10.1128/IAI.73.8.5127-5136.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
Hag Directly Mediates the Adherence of Moraxella catarrhalis to Human Middle Ear Cells
Brian Bullard,
Serena L. Lipski, and
Eric R. Lafontaine*
Department of Medical Microbiology and Immunology, Medical College of Ohio, 3055 Arlington Ave., Toledo, Ohio 43614
Received 7 February 2005/
Returned for modification 10 March 2005/
Accepted 4 April 2005
Moraxella catarrhalis is a human pathogen that causes otitis media in young children and lung infections in patients with chronic obstructive pulmonary disease. In this study, the role of the surface protein Hag in the adherence of multiple M. catarrhalis strains was examined. The hag genes of four clinical isolates were disrupted with a spectinomycin resistance cassette, and the binding of isogenic mutants to primary cultures of human middle ear epithelial cells (HMEE), as well as A549 pneumocytes, was measured. These experiments revealed that the attachment of most mutants to both cell types was 10-fold less than that of their wild-type progenitors. To determine whether Hag directly mediates adherence to human cells, the hag genes from three M. catarrhalis isolates were cloned and expressed in a nonadherent Escherichia coli cloning strain. At least 17-fold more E. coli bacteria expressing Hag attached to HMEE cells than an adherence-negative control. Surprisingly, Hag expression did not increase the binding of recombinant E. coli to A549 monolayers. Our data demonstrate that the involvement of Hag in M. catarrhalis adherence to A549 and HMEE cells is conserved among isolates and that Hag directly mediates binding to HMEE cells.
* Corresponding author. Mailing address: Department of Medical Microbiology and Immunology, Medical College of Ohio, 3055 Arlington Ave., Health Education Bldg., Rm. 267, Toledo, OH 43614. Phone: (419) 383-6626. Fax: (419) 383-3002. E-mail: elafontaine{at}mco.edu.
Editor: D. L. Burns
Infection and Immunity, August 2005, p. 5127-5136, Vol. 73, No. 8
0019-9567/05/$08.00+0 doi:10.1128/IAI.73.8.5127-5136.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
This article has been cited by other articles:
-
Sheets, A. J., Grass, S. A., Miller, S. E., St. Geme, J. W. III
(2008). Identification of a Novel Trimeric Autotransporter Adhesin in the Cryptic Genospecies of Haemophilus. J. Bacteriol.
190: 4313-4320
[Abstract]
[Full Text]
-
Balder, R., Hassel, J., Lipski, S., Lafontaine, E. R.
(2007). Moraxella catarrhalis Strain O35E Expresses Two Filamentous Hemagglutinin-Like Proteins That Mediate Adherence to Human Epithelial Cells. Infect. Immun.
75: 2765-2775
[Abstract]
[Full Text]
-
Plamondon, P., Luke, N. R., Campagnari, A. A.
(2007). Identification of a Novel Two-Partner Secretion Locus in Moraxella catarrhalis. Infect. Immun.
75: 2929-2936
[Abstract]
[Full Text]
-
Lipski, S. L., Akimana, C., Timpe, J. M., Wooten, R. M., Lafontaine, E. R.
(2007). The Moraxella catarrhalis Autotransporter McaP Is a Conserved Surface Protein That Mediates Adherence to Human Epithelial Cells through Its N-Terminal Passenger Domain. Infect. Immun.
75: 314-324
[Abstract]
[Full Text]
-
Tan, T. T., Christensen, J. J., Dziegiel, M. H., Forsgren, A., Riesbeck, K.
(2006). Comparison of the Serological Responses to Moraxella catarrhalis Immunoglobulin D-Binding Outer Membrane Protein and the Ubiquitous Surface Proteins A1 and A2. Infect. Immun.
74: 6377-6386
[Abstract]
[Full Text]
Copyright © 2005 by the American Society for Microbiology. All rights reserved.