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Infection and Immunity, May 2005, p. 2828-2834, Vol. 73, No. 5
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.5.2828-2834.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Identification and Characterization of Human Surfactant Protein A Binding Protein of Mycoplasma pneumoniae

T. R. Kannan,1 D. Provenzano,1,{dagger} J. R. Wright,2 and J. B. Baseman1*

Department of Microbiology and Immunology, University of Texas Health Science Center at San Antonio, San Antonio, Texas,1 Department of Cell Biology, Duke University Medical Center, Durham, North Carolina2

Received 3 November 2004/ Returned for modification 15 December 2004/ Accepted 5 January 2005

Mycoplasma pneumoniae infections represent a major primary cause of human respiratory diseases, exacerbate other respiratory disorders, and are associated with extrapulmonary pathologies. Cytadherence is a critical step in mycoplasma colonization, aided by a network of mycoplasma adhesins and cytadherence accessory proteins which mediate binding to host cell receptors. Furthermore, the respiratory mucosa is enriched with extracellular matrix components, including surfactant proteins, fibronectin, and mucin, which provide additional in vivo targets for mycoplasma parasitism. In this study we describe interactions between M. pneumoniae and human surfactant protein-A (hSP-A). Initially, we found that viable M. pneumoniae cells bound to immobilized hSP-A in a dose- and calcium (Ca2+)-dependent manner. Mild trypsin treatment of intact mycoplasmas reduced binding markedly (80 to 90%) implicating a surface-associated mycoplasma protein(s). Using hSP-A-coupled Sepharose affinity chromatography and polyacrylamide gel electrophoresis, we identified a 65-kDa hSP-A binding protein of M. pneumoniae. The presence of Ca2+ enhanced binding of the 65-kDa protein to hSP-A, which was reduced by the divalent cation-chelating agent, EDTA. The 65-kDa hSP-A binding protein of M. pneumoniae was identified by sequence analysis as a novel protein (MPN372) possessing a putative S1-like subunit of pertussis toxin at the amino terminus (amino acids 1 to 226), with the remaining amino acids (227 to 591) exhibiting no homology with other subunits of pertussis toxin, other known toxins, or any reported proteins. Recombinant MPN372 (MPN372) bound to hSP-A in a dose-dependent manner, which was markedly reduced by preincubation with mouse recombinant MPN372 antisera. Also, adherence of viable M. pneumoniae cells to hSP-A was inhibited by recombinant MPN372 antisera, demonstrating that MPN372, a previously designated hypothetical protein, is surface exposed and mediates mycoplasma attachment to hSP-A.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, The University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, Texas 78229-3900. Phone: 210-567-3939. Fax: 210-567-6491. E-mail: baseman{at}uthscsa.edu.

Editor: A. D. O'Brien

{dagger} Present address: Department of Biological Sciences, University of Texas at Brownsville, Brownsville, TX 78520.

Infection and Immunity, May 2005, p. 2828-2834, Vol. 73, No. 5
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.5.2828-2834.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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