Purification and partial characterization of the major outer membrane protein of Chlamydia trachomatis.

摘要: Elementary bodies (EB) of Chlamydia trachomatis serotypes C, E, and L2 were extrinsically radioiodinated, whole-cell lysates these compared by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Autoradiography the polypeptide profiles identified a major surface protein with an apparent subunit molecular weight 39,500 that was common to each C. serotype. The abilities nonionic (Triton X-100), dipolar ionic (Zwittergent TM-314), mild (sodium deoxycholate N-lauroyl sarcosine), strongly anionic (SDS) detergents extract this from intact EB serotype investigated SDS-PAGE analysis soluble insoluble fractions obtained after detergent treatment. Only SDS readily extracted EB. Sarkosyl treatment selectively solubilized majority other proteins, leaving 39,500-dalton associated Sarkosyl-insoluble fraction. Ultrastructural studies pellet showed it consist empty particles possessing apparently outer membrane. No structural evidence for peptidoglycan-like cell wall found. Morphologically chlamydial membrane complexes (COMC) resembled membranes. quantitatively COMC treating them 2% at 60 degrees This accounted 61% total COMC-associated protein, its extraction resulted in concomitant loss structure morphology. SDS-treated adsorbed hydroxylapatite column eluted linear phosphate gradient. as single peak concentration approximately 0.3 M. nearly homogeneous appeared free contaminating carbohydrate, glycolipid, nucleic acid. Hyperimmune mouse antiserum prepared against reacted Ba, D, K, L1, L2, L3 indirect immunofluorescence but failed react A, B, F, G, H, I, J, pneumonitis strain, or psittaci feline pneumonitis, guinea pig inclusion conjunctivitis, 6BC strains. Thus, is serogroup antigen organisms.