The Structural Integrity of Plasmid-Encoded Pgp3 Is Essential for Induction of Hydrosalpinx by.

Abstract

Pgp3 consists of globular N- and C-terminal domains connected by a triple-helical coiled-coil middle domain. We demonstrated previously that Pgp3 is required for induction of hydrosalpinx by. We constructedtransformants harboring deletion of the Pgp3 N-terminus (pgp3Δn), C-terminus (pgp3Δc), or middle domain (pgp3Δm). C3H/HeJ and CBA/J mice infected with pgp3Δn or pgp3Δm failed to induce hydrosalpinx in oviduct tissue. However, the pgp3Δc transformant induced mild hydrosalpinx in 20% of C3H/HeJ mice (severity score 0.2 ± 0.6) and in 40% of CBA/J mice (severity score 0.8 ± 1.3). The attenuated pathogenicity of the transformants harboring Pgp3 domain deletions was correlated with impairedgrowth and significantly reduced infectivity in the mouse lower genital tract. Moreover, the oviduct tissue of C3H/HeJ and CBA/J mice infected with the Pgp3-domain-deficient transformants displayed less inflammatory cell infiltration. Thus, the structural integrity of plasmid-encoded Pgp3 is essential for induction of hydrosalpinx by.