IAI FigSearch
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Bullard, B.
Right arrow Articles by Lafontaine, E. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bullard, B.
Right arrow Articles by Lafontaine, E. R.
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:




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. J. Virol. Eukaryot. Cell
Microbiol. Mol. Biol. Rev. Clin. Vaccine Immunol. All ASM Journals

Copyright © 2005 by the American Society for Microbiology. All rights reserved.