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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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