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Journal of Bacteriology, February 2008, p. 1036-1044, Vol. 190, No. 3
0021-9193/08/$08.00+0     doi:10.1128/JB.01416-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Identification and Characterization of an Acinetobacter baumannii Biofilm-Associated Protein{triangledown}

Thomas W. Loehfelm,1,3 Nicole R. Luke,1,4 and Anthony A. Campagnari1,2,3,4*

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

Received 31 August 2007/ Accepted 7 November 2007

We have identified a homologue to the staphylococcal biofilm-associated protein (Bap) in a bloodstream isolate of Acinetobacter baumannii. The fully sequenced open reading frame is 25,863 bp and encodes a protein with a predicted molecular mass of 854 kDa. Analysis of the nucleotide sequence reveals a repetitive structure consistent with bacterial cell surface adhesins. Bap-specific monoclonal antibody (MAb) 6E3 was generated to an epitope conserved among 41% of A. baumannii strains isolated during a recent outbreak in the U.S. military health care system. Flow cytometry confirms that the MAb 6E3 epitope is surface exposed. Random transposon mutagenesis was used to generate A. baumannii bap1302::EZ-Tn5, a mutant negative for surface reactivity to MAb 6E3 in which the transposon disrupts the coding sequence of bap. Time course confocal laser scanning microscopy and three-dimensional image analysis of actively growing biofilms demonstrates that this mutant is unable to sustain biofilm thickness and volume, suggesting a role for Bap in supporting the development of the mature biofilm structure. This is the first identification of a specific cell surface protein directly involved in biofilm formation by A. baumannii and suggests that Bap is involved in intercellular adhesion within the mature biofilm.

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

{triangledown} Published ahead of print on 16 November 2007.

Journal of Bacteriology, February 2008, p. 1036-1044, Vol. 190, No. 3
0021-9193/08/$08.00+0     doi:10.1128/JB.01416-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



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