LPS structure influences protein secretion in

M. Crhanova (1) , M. Malcova (1) , M. Mazgajova (1) , D. Karasova (2) , A. Sebkova (2) , A. Fucikova (2) , Z. Bortlicek (3) , L. Pilousova (1) , K. Kyrova (1) , M. Dekanova (1) , I. Rychlik (1)

1 Veterinary Research Institute
2 Faculty of Military Health Sciences
3 Faculty of Medicine and Faculty of Science

In this study we have compared protein secretion in the wild type of Typhimurium and the mutant. We found out that the mutant was defective in protein secretion. In addition, the mutant was defective in its invasion into an IPEC-J2 porcine epithelial cell line and also in motility in semisolid agar. Consistent with this, reduced flagella numbers were observed in the mutant. In the mutant, there were no defects in flagellin expression as detected by western blot and immune electron microscopy which demonstrated equal amounts of flagellin in the cytoplasm of both the mutant and the wild-type . Typhimurium. However, in the wild-type strain only, the flagellin was assembled to spatially restricted areas on the inner side of cytoplasmic membrane. The oligosaccharide core of LPS is therefore required for the assembly of flagella and T3SS secretion machinery followed by protein secretion.

Mots clés: LPS; protein secretion; motility; SPI-1

Domaines: Médecine vétérinaire et santé animale

M. Crhanova, M. Malcova, M. Mazgajova, D. Karasova, A. Sebkova, et al.. LPS structure influences protein secretion in. Veterinary Microbiology, 2011, 152 (1-2), pp.131. ⟨10.1016/j.vetmic.2011.04.018⟩. ⟨hal-00719079⟩