Traditionally used medicinal plants against uncomplicated urinary tract infections: Hexadecyl coumaric acid ester from the rhizomes of Agropyron repens (L.) P. Beauv. with antiadhesive activity against uropathogenic E. coli.

The rhizomes from Agropyron repens are traditionally used for the treatment of uncomplicated urinary tract infections. Extracts prepared with solvents of different polarity did not show any cytotoxic effects against different strains of uropathogenic E. coli (UPEC) and human T24 bladder cells under in vitro conditions. Significant antiadhesive activity against the bacterial attachment to human T24 bladder cells was found for an acetone extract (AAE) at concentrations >250µg/mL. More hydrophilic extracts did not influence the bacterial attachment to the eukaryotic host cells. Bioassay guided fractionation of AAE led to the identification of (E)-hexadecyl-3-(4-hydroxyphenyl)-acrylate (hexadecyl-coumaric acid ester) 1 as the compound responsible for inhibiting the UPEC adhesion to T24 bladder cells. 1 reduced the bacterial invasion into the bladder cells as shown by a specific invasion assay. Additionally, 1 was obtained by chemical synthesis, and also the synthetic structural analogs 2 and 3 were tested for their potential antiadhesive activity, indicating that a shorter alkyl chain at the ester function as well as the lack of hydroxylation of the phenyl moiety will abolish the antiadhesive activity.

Two quality-associated HMW glutenin subunits in a somatic hybrid line between Triticum aestivum and Agropyron elongatum.

High-molecular-weight glutenin subunits (HMW-GSs) from hybrid line II-12 between wheat (Triticum aestivum L.) and Agropyron elongatum (Host) Nivski were characterized with SDS-PAGE. Out of these HMW-GSs, two subunits, h1Bx and h1By, had mobilities similar to the subunits 1Bx13 and 1By16 from common wheat 4072, which was used as control. Polyclonal antibodies (pAbs) of h1Bx and h1By were prepared, and Western blotting showed that the pAbs had strong affinities for h1Bx and h1By, separately. The specificity of h1Bx-pAb was further checked; it preferentially recognized subunits h1Bx and 1Bx13. HMW-GS gene coding sequences were amplified by genomic polymerase chain reaction from hybrid II-12. Two of the five amplicons, marked II2a and II31b, were sequenced. Their coding sequences are clustered to Glu-1Bx7 and Glu-1By9 of common wheat. Three discrepant regions in deduced amino acid sequences of II2a and 31b repeated one time more than Glu-1Bx7 and Glu-1By9. N-terminal sequences of h1Bx and h1By were determined, which were identical to the published sequences of 1Bx13 and 1By16 and in agreement with that deduced from II2a and II31b, respectively. These results indicated that the two novel genes separated from the hybrid wheat derived from the allelic variation of 1Bx7 and 1By9 of the parent wheat. There is an additional cysteine residue positioned at 271st amino acid of the mature peptide of II2a, which may be related to the high quality of the flour.