Species-Specific Major Outer Membrane Protein Domain

摘要

The major outer membrane (MOMP) of Chlamydia trachomatis has important biological and antigenic properties. The MOMP is quantitatively and predominant protein of the outer membrane and is essential element for the maintenance of cell wall stability for the elementary body. The protein has also been shown to possess porin functions. These activities appear to be modulated by disulfide bond interactions. The Chlamydia MOMP is an antigenically complex protein with both conserved domains and divergent domains. This has been demonstrated by peptide analysis and by the diverge spectrum of monoclonal antibodies specific to MOMP. In vitro inhibition of infectivity assays using MOMP monospecific antisera or monoclonal antibodies demonstrate significant neutralization activities. In spite of the immunodomiant nature of this protein, its role in eliciting effective immune mechanisms in the host is unclear. Because an understanding of the molecular components for pathogenesis are of considerable interest, and because chlamydiae are difficult to cultivate, several groups have cloned various chlamydial components in Escherichia coli. Recently, Stephens et. al. expressed an antigenic portion of MOMP in E. coli that reacts wth monoclonal antibodies. The authors will describe here an antigenic domain which displays species-specific reactivities.