Summary
In 2D-PAGE analysis of Bet v 1, the major birch pollen allergen, up to 12 isoforms can be demonstrated that differ in their isoelectric points from about pH 4.9 to pH 5.9. The molecular weights of these isoforms seem to be rather similar, but minor variations can also be seen. Preliminary experiments with birch leaves seem to indicate that in aging leaves some isoforms can be found that do not occur in pollen. In birch cells cultured in vitro, Bet v 1 isoforms can be induced by bacterial infection that do not occur in pollen (Swoboda et al. (1995), Pant, Cell and Environment 18, 865-874). In a recent paper (Swoboda et al (1995)., J. Biol Chem. 270, 2607-2613 ) we show that in natural Bet v 1 from pollen the isoforms are due to different protein sequences. The derived protein sequences of 10 different isoforms (corresponding to 13 different cDNAs) were determined and confirmed by plasma desorption mass spectrometry of purified natural Bet v 1 after trypsin and endoproteinase Glu-C digestion. These experiments also showed that pollen Bet v 1 isoforms were reactive to patients’ sera to different degrees and that common post-synthetic modifications (besides N-terminal methionine cleavage) did not occur on Betv 1.
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Breitenbach, M. et al. (1996). Biological and Immunological Importance of BET v 1 Isoforms. In: Sehon, A., HayGlass, K.T., Kraft, D. (eds) New Horizons in Allergy Immunotherapy. Advances in Experimental Medicine and Biology, vol 409. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5855-2_16
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