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We cloned and characterized MtPRP4, a new member of the repetitive proline-rich protein gene family in Medicago truncatula. The sequence of MtPRP4 predicts a 62-kD protein consisting of a 22-amino acid N-terminal signal peptide and a 527-amino acid repetitive proline-rich domain composed of three repetitive pentapeptide motifs arranged into two decapeptide repeats: PPVEKPPVHK and PPVEKPPVYK. MtPRP4 is the largest PRP described to date and contains repeated motifs that have not previously been found together in a single polypeptide. RNA gel blot experiments detected MtPRP4 transcripts in symbiotic root nodules, but not in roots, hypocotyls, or leaves. Accumulation of MtPRP4 transcript was an early response to Rhizobium inoculation and did not depend on nodule infection. In situ hybridization experiments demonstrated that MtPRP4 was expressed early in the development of the nodule meristem and that expression was highest in the meristematic cells of mature indeterminate nodules. These data support the proposition that an important early response of legume host roots to Rhizobium involves remodeling the host extracellular matrix and that proline-rich wall proteins play an important role in this architectural modification.

The chemical investigation of n-butanol fraction (BF) from the leaves of Zanthoxylum naranjillo (Rutaceae) by open column and preparative HPLC resulted in the isolation of magnoflorine (1), apigenin-6-C-β-D-glucopyranoside (2) and apigenin-8-C-β-D-glucopyranoside (3). This is the first time that the presence of compounds 1 to 3 in Z. naranjillo has been reported. Compounds 1 to 3 and BF were screened in vitro against Schistosoma mansoni adult worms. The results indicated that BF and compound 3 were able to separate coupled S. mansoni adult worms.

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