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Infection and Immunity, March 2001, p. 1747-1754, Vol. 69, No. 3
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.3.1747-1754.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Expression of C-Reactive Protein in the Human Respiratory Tract

Jane M. Gould1 and Jeffrey N. Weiser2,*

Division of Pediatric Infectious Diseases, The Children's Hospital of Philadelphia,1 and Departments of Microbiology and Pediatrics, University of Pennsylvania School of Medicine,2 Philadelphia, Pennsylvania 19104

Received 16 October 2000/Returned for modification 27 November 2000/Accepted 7 December 2000

C-reactive protein (CRP) is a normal constituent of human sera synthesized by hepatocytes and induced by proinflammatory cytokines. The function of this acute-phase reactant includes activation of complement and enhancement of opsonophagocytosis. CRP binds to phosphorylcholine (ChoP), a constituent of eukaryotic membranes that is also found on the cell surface of major bacterial pathogens of the human respiratory tract, including Streptococcus pneumoniae and Haemophilus influenzae. The presence of CRP on mucosal surfaces and role in innate immunity in the human respiratory tract where ChoP-containing organisms reside have not been previously studied. We have shown using a monoclonal antibody to CRP that CRP is present in inflamed (0.17 to 42 µg/ml) and uninflamed (<0.05 to 0.88 µg/ml) secretions from the human respiratory tract in sufficient quantities for an antimicrobial effect. In addition, the CRP gene was expressed in epithelial cells of the human respiratory tract using in situ hybridization on nasal polyps and reverse transcriptase PCR of pharyngeal cells in culture. The complement-dependent bactericidal activity of normal nasal airway surface fluid and sputum against ChoP-expressing H. influenzae was abolished when the secretions were pretreated to remove CRP. In summary, the results indicate that CRP is present in secretions of the human respiratory tract, that human respiratory epithelial cells are capable of CRP expression, and that this protein may contribute to bacterial clearance in the human respiratory tract.

* Corresponding author. Mailing address: 301B Johnson Pavilion, Department of Microbiology, University of Pennsylvania, Philadelphia, PA 19104-6076. Phone: (215) 573-3511. Fax: (215) 898-9557. E-mail: weiser{at}mail.med.upenn.edu.

Infection and Immunity, March 2001, p. 1747-1754, Vol. 69, No. 3
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.3.1747-1754.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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