Characterization and functional analysis of PorB, a Chlamydia porin and neutralizing target.
A predicted protein (CT713) with weak sequence similarity to the major outer membrane protein (20.4% identity) in Chlamydia trachomatis was identified by Chlamydia genome analysis. We show that this protein is expressed, surface accessible, localized to the chlamydial outer membrane complex and functions as a porin. This protein, PorB, was highly conserved among different serovars, with nearly identical sequences between serovars D, B, C and L2. Sequence comparison between C. trachomatis and Chlamydia pneumoniae showed less conservation between species with 59.3% identity. Immunofluorescence staining with monospecific antisera to purified PorB revealed antigen localized within chlamydial inclusions and found throughout the developmental cycle. Antibodies to PorB neutralized infectivity of C. trachomatis in an in vitro neutralization assay confirming that PorB is surface exposed. As PorB was found to be in the outer membrane, as well as having weak structural characteristics similar to major outer membrane protein (MOMP) and other porins, a liposome-swelling assay was used to determine whether this protein had pore-forming capabilities. PorB had pore-forming activity and was shown to be different from MOMP porin activity.
Kubo
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Division of Infectious Diseases, School of Public Health, 140 Earl Warren Hall, University of California, Berkeley, CA 94720, USA.
Stephens
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D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000235:genetics* / Q000378:metabolism*; D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism*; D002692:Chlamydia trachomatis / Q000235:genetics* / Q000378:metabolism*; D008969:Molecular Sequence Data; D018272:Porins / Q000235:genetics* / Q000378:metabolism*; D016415:Sequence Alignment
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D018272:Porins; C057699:porin protein, Neisseria