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Infection and Immunity, June 2007, p. 2929-2936, Vol. 75, No. 6
0019-9567/07/$08.00+0     doi:10.1128/IAI.00396-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Identification of a Novel Two-Partner Secretion Locus in Moraxella catarrhalis{triangledown}

Pascale Plamondon,1,3 Nicole R. Luke,1,4 and Anthony A. Campagnari1,2,3,4*

Department of Microbiology and Immunology,1 Division of Infectious Disease, Department of Medicine,2 Witebsky Center for Microbial Pathogenesis and Immunology, University at Buffalo, State University of New York,3 NYS Center of Excellence in Bioinformatics and Life Sciences, Buffalo, New York4

Received 15 March 2007/ Accepted 30 March 2007

Although Moraxella catarrhalis continues to be a significant cause of disease in both children and adults, the steps involved in pathogenesis remain poorly understood. We have identified three open reading frames in the M. catarrhalis genome that encode homologues of the two-partner secretion system (TPS). The sequenced M. catarrhalis hemagglutinin-like locus of strain 7169 has a unique gene organization composed in the order of mchA1, mchB, and mchA2, where mchA1 is divergent. MchA1 and MchA2 are 74% identical at the amino acid level and diverge only in the C-terminal regions. The TPS motif identified in the common N-terminal regions of MchA1 and MchA2 was found to be homologous to the filamentous hemagglutinin of Bordetella pertussis, and MchB has homology to other TpsB transporters. The presence of MchA1 and MchA2 in outer membrane protein preparations and concentrated culture supernatants (CCSs) of strain 7169 was confirmed by immunoblotting using specific antisera. Nanoscale liquid chromatography-tandem mass spectrometry peptide sequencing of the antibody-reactive bands from the CCSs was performed and demonstrated that 13 different peptides mapped to identical regions of MchA1 and MchA2. Quantitative adherence assays revealed a decrease of binding to primary normal human bronchial epithelial cells by the mch mutants 7169mchB and 7169mchA1A2B compared to that by the wild-type strain. These studies show that MchA1, MchA2, and MchB are components of a novel TPS identified in M. catarrhalis and suggest that these proteins may be involved in colonization.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, University at Buffalo, 140 Biomedical Research Bldg., 3435 Main St., Buffalo, NY 14214. Phone: (716) 829-2673. Fax: (716) 829-3889. E-mail: AAC{at}acsu.buffalo.edu

{triangledown} Published ahead of print on 9 April 2007.

Editor: D. L. Burns

Infection and Immunity, June 2007, p. 2929-2936, Vol. 75, No. 6
0019-9567/07/$08.00+0     doi:10.1128/IAI.00396-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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