A major stress-inducible Mr-42000 wall glycoprotein of French bean (Phaseolus vulgaris L.)

A major wall protein of suspension-cultured cells of French bean has been isolated and characterised. It can be prepared from walls or the culture filtrate and in composition it is particularly rich in proline, valine and glutamic acid/glutamine and contains appreciable amounts of hydroxyproline. The N-terminus shows some glycosylation, while following chemical deglycosylation the first 38 residues were found to be identical to those of proline-rich proteins from soybean. However, the composition of the highly purified M_r-42000 bean protein differs considerably from the soybean proteins and must contain its own specific domains. An antibody was raised and used to demonstrate the inducibility of the M_r-42000 bean protein in response to elicitor action. The protein was found to be mainly localised in the intercellular spaces of the cortical cells of bean hypocotyls and at the wall-plasmalemma interface of xylem vessels, another potentially accessible compartment for pathogens. Following wounding, the protein was found to be generally distributed in the wall of epidermal and cortical cells of the hypocotyls. The M_r-42000 protein is cross reactive with antibodies raised to glycoproteins of the Rhizobium infection thread and the chitin-binding hydroxyproline-rich glycoprotein, potato lectin. These common epitopes together with the previously demonstrated chitin-binding properties of the bean protein indicate a role in host-microbial interactions. Furthermore, the M_r-42000 protein itself bound to the growing hyphal tips of the bean pathogen, Colletotrichum lindemuthianum.Abbreviations FITC fluorescein isothiocyanate - IgG immunoglobulin G - PAL phenylalanine ammonia-lyaseWe thank Dr Nick Brewin for advice on interpretation of immunolocalisations and for the gift of MCA 265. We thank Dudley Fernandino for carrying out the confocal microscopy. GPB thanks the Science and Engineering Research Council for funding.