Chlamydiae are prokaryotic obligate intracellular parasites that undergo a biphasic life cycle involving an infectious, extracellular form known as elementary bodies and an intracellular, replicating form termed reticulate bodies. We have purified from Chlamydia trachomatis a very basic elementary body-specific protein with an apparent molecular mass of 18 kDa, determined its N-terminal amino acid sequence, and cloned the encoding gene. Sequence analysis of the cloned gene revealed some remarkable properties for its expressed product, including a high lysine content (29%), a correspondingly high pl, and significant homology to the Hi class of eukaryotic histones. Furthermore, a monoclonal antibody to this chlamydial histone analog, termed Hc1, displayed immunoblot and antinuclear specificity suggestive of cross-reactivity to Hi histones. The gene was expressed only during the late stages of the chlamydial life cycle concomitant with the reorganization of chlamydial reticulate bodies into elementary bodies, suggesting that the Hc1 protein plays a role in the condensation of chlamydial chromatin during intracellular differentiation.Chlamydiae are bacterial obligate intracellular parasites that possess several characteristics making them unique among prokaryotes. During their intracellular development they undergo dramatic morphological and functional changes (1). Infection of susceptible cells is initiated by a small, dense, and relatively metabolically inert elementary body (EB). By about 8 hr after infection, EBs differentiate to larger, more pleomorphic, and metabolically active reticulate bodies (RBs). Ultrastructurally, the EBs appear as spheres about 0.3