Affiliation:
1. Department of Microbiology and Immunology, Medical College of Ohio, Toledo, Ohio 43614-5806
Abstract
ABSTRACT
The outer membrane protein CD (OMPCD) of
Moraxella catarrhalis
is an outer membrane protein with several attributes of a potential vaccine antigen. We isolated four transposon mutants of strain O35E on the basis of their reduced binding to A549 human lung cells in microcolony formation assays, and we determined that they contain a transposon in
ompCD
. We also found that these transposon insertions had pleiotropic effects: mutants grew slower, became serum sensitive, bound ∼10-fold less to A549 cells, and appeared transparent when grown on solid medium. We confirmed that these various phenotypes could be attributed solely to disruption of
ompCD
by constructing the isogenic strain O35E.CD1. O35E-
ompCD
was cloned, and recombinant
Escherichia coli
bacteria expressing the gene product exhibited a 10-fold increase in adherence to A549 cells. This is the first report of
M. catarrhalis ompCD
mutants, and our findings demonstrate that this gene product is an adhesin for human lung cells.
Publisher
American Society for Microbiology
Subject
Infectious Diseases,Immunology,Microbiology,Parasitology
Cited by
77 articles.
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