Group V allergens in grass pollens: IV. Similarities in amino acid compositions and NH2-terminal sequences of the Group V allergens from Lolium perenne, Poa pratensis and Dactylis glomerata
Article first published online: 27 APR 2006
Clinical & Experimental Allergy
Volume 22, Issue 4, pages 491–497, April 1992
How to Cite
KLYSNER, S., WELINDER, K. G., LØWENSTEIN, H. and MATTHIESEN, F. (1992), Group V allergens in grass pollens: IV. Similarities in amino acid compositions and NH2-terminal sequences of the Group V allergens from Lolium perenne, Poa pratensis and Dactylis glomerata. Clinical & Experimental Allergy, 22: 491–497. doi: 10.1111/j.1365-2222.1992.tb00152.x
- Issue published online: 27 APR 2006
- Article first published online: 27 APR 2006
- Submitted 29 May 1991; revised 31 October 1991; accepted 4 November 1991.
Monoclonal antibodies (PpV4) raised against Phleum pratense group V allergen were used for immuno-affinity chromatography of cross-reacting group V allergens from related grass species. Fractions enriched in group V allergen were obtained from Lolium perenne, Poa pratense and Dactylis glomerata extracts. The major components in these fractions were found in the Mwr range 25–28 kD. IgE binding to these components was shown using a pool of grass allergic sera, by SDS-PAGE immunoblotting. These fractions were electroblotted from tricine SDS-PAGE gels onto a polyvinylidenedifluoride membrane and selected group V bands were directly cut out and used for amino acid analysis and NH2-terminal sequencing.
Both the amino acid compositions and the NH2-terminal sequences obtained for each group V allergen were almost similar to each other and to the sequence and composition of the previously described allergen Phl p V from Phleum pratense. A common trait of the investigated allergens, is the very high contents of alanine (25–32%) and the presence of the modified amino acid, hydroxyproline.