Use of translational fusion of the MrpH fimbrial adhesin-binding domain with the cholera toxin A2 domain, coexpressed with the cholera toxin B subunit, as an intranasal vaccine to prevent experimental urinary tract infection by Proteus mirabilis

Infect Immun. 2004 Dec;72(12):7306-10. doi: 10.1128/IAI.72.12.7306-7310.2004.

Abstract

This is a follow-up to our previous study using an intranasal vaccine composed of MrpH, the tip adhesin of the MR/P fimbria, and cholera toxin to prevent urinary tract infection by Proteus mirabilis (X. Li, C. V. Lockatell, D. E. Johnson, M. C. Lane, J. W. Warren, and H. L. Mobley, Infect. Immun. 72:66-75, 2004). Here, we have expressed a cholera toxin-like chimera in which the MrpH adhesin-binding domain (residues 23 to 157) replaces the cholera toxin A1 ADP-ribosyltransferase domain. This chimera, when administered intranasally without additional adjuvant, is sufficient to induce protective immunity in mice.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adhesins, Bacterial / chemistry
  • Adhesins, Bacterial / immunology*
  • Administration, Intranasal
  • Animals
  • Bacterial Vaccines / immunology*
  • Binding Sites
  • Cholera Toxin / immunology*
  • Fimbriae Proteins / chemistry
  • Fimbriae Proteins / immunology*
  • Mice
  • Protein Biosynthesis
  • Proteus Infections / prevention & control*
  • Proteus mirabilis / immunology*
  • Recombinant Fusion Proteins / immunology*
  • Urinary Tract Infections / prevention & control*
  • Vaccination
  • Vaccines, Synthetic / immunology*

Substances

  • Adhesins, Bacterial
  • Bacterial Vaccines
  • MrpH protein, Proteus mirabilis
  • Recombinant Fusion Proteins
  • Vaccines, Synthetic
  • Fimbriae Proteins
  • Cholera Toxin