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. 2001 May;69(5):3082–3091. doi: 10.1128/IAI.69.5.3082-3091.2001

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Copyright © 2001, American Society for Microbiology

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FIG. 4 — (A) Immunoprecipitation of intrinsically ³⁵S-labeled C. pneumoniae antigen by C. pneumoniae MAbs. Autoradiographs show immunoprecipitation results of ³⁵S-labeled C. pneumoniae-infected (lane 1) and uninfected (lane 2) HeLa cells with the GZD1E8 MAb; ³⁵S-labeled C. pneumoniae-infected (lane 3) and uninfected (lane 4) HeLa cells immunoprecipitated with anti-rickettsial MAb 8-13A4A10; ³⁵S-labeled C. psittaci GPIC-infected (lane 5) and C. trachomatis L2-infected (lane 6) HeLa cells immunoprecipitated with MAb GZD1E8; and ³⁵S-labeled C. pneumoniae-infected (lane 7) and uninfected (lane 8) HeLa cells immunoprecipitated with MAb RR-402. ∗, the ∼40-kDa protein in C. pneumoniae-infected HeLa cells detected with MAbs GZD1E8 and RR-402 (lanes 1 and 7). (B) Detection of a ∼40-kDa polypeptide with MAbs GZD1E8 and RR-402 by immunoblotting. The 40-kDa polypeptide was not detected with the RR-402 MAb (lane 1) and was weakly detected with the GZD1E8 MAb (lane 2). A very strong reaction was detected with chlamydial, genus-specific, anti-MOMP antibody (lane 3). ∗, the ∼40-kDa protein.