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Bursting the elementary bodies


The protein coat which surrounds and protects the chlamydial elementary body relies on disulphide bonds within and between macromolecules to maintain its conformity. Reduction of these bonds disrupts the conformational integrity: such disruption would be expected to be irreversible. Penicillamine, and amoxycillin (whose major metabolite is penicillamine) have been demonstrated to inactivate EBs in vitro. [Chuck Stratton, personal communication.]

As the EB attaches to the host cell a number of different mechanisms seem able to allow entry. [Reynolds, D. J., and J. H. Pearce. Endocytic mechanisms utilized by chlamydiae and their influence on induction of productive infection. Infect. Immun. 1991; 59: 3033–3039.] Raulston and co-workers have shown that the disulphide bonds between the chlamydial surface proteins must be opened up just prior to or during attachment to the host cell. [Raulston JE et al., Surface accessibility of the 70-kilodalton Chlamydia trachomatis heat shock protein following reduction of outer membrane protein disulfide bonds. Infect Immun. 2002; 70(2): 535-43.] It is reasonable to think that, were the EB coat to be opened up before achieving attachment to a host cell, the unprotected EB would perish...........................................