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Infection and Immunity, January 2007, p. 497-503, Vol. 75, No. 1
0019-9567/07/$08.00+0 doi:10.1128/IAI.00935-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Department of Microbiology and Immunology, University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, Texas 78229,1 Department of Immunology, Hebei Medical University, Shijiazhuang, Hebei, China 0500172
Received 12 June 2006/ Returned for modification 16 August 2006/ Accepted 20 October 2006
The hypothetical protein encoded by Chlamydia pneumoniae open reading frame cpn0308 was detected in inclusion membranes of C. pneumoniae-infected cells using antibodies raised with Cpn0308 fusion proteins. The anti-Cpn0308 antibodies did not cross-react with IncA, a known C. pneumoniae inclusion membrane protein, although the anti-Cpn0308 antibody staining overlapped with the anti-IncA antibody labeling. The labeling of the inclusion membrane by the anti-Cpn0308 antibody was specifically blocked by the Cpn0308 but not IncA fusion proteins. The Cpn0308 antigen was detectable 24 h after infection and remained in the inclusion membrane throughout the infection course.
Published ahead of print on 13 November 2006.
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