title: Complete amino acid sequence of a Lolium perenne (perennial rye grass) pollen allergen, Lol p II.
abstract: The complete amino acid sequence of a Lolium perenne (rye grass) pollen allergen, Lol p II was determined by automated Edman degradation of the protein and selected fragments. Cleavage of the protein by enzymatic and chemical techniques established an unambiguous sequence for the protein. Lol p II contains 97 amino acid residues, with a calculated molecular weight of 10,882. The protein lacks cysteine and glutamine and shows no evidence of glycosylation. Theoretical predictions by Fraga's (Fraga, S. (1982) Can. J. Chem. 60, 2606-2610) and Hopp and Woods' (Hopp, T. P., and Woods, K. R. (1981) Proc. Natl. Acad. Sci. U.S.A. 78, 3824-3828) methods indicate the presence of four hydrophilic regions, which may contribute to sequential or parts of conformational B-cell epitopes. Analysis of amphipathic regions by Berzofsky's method indicates the presence of a highly amphipathic region, which may contain, or contribute to, an Ia/T-cell epitope. This latter segment of Lol p II was found to be highly homologous with an antibody-binding segment of the major rye allergen Lol p I and may explain why immune responsiveness to both the allergens is associated with HLA-DR3.
authors: Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland 21239.
authors: A A
authors: AA
authors: Ansari
authors: P
authors: P
authors: Shenbagamurthi
authors: D G
authors: DG
authors: Marsh
mesh_terms: D000595:Amino Acid Sequence; D001402:B-Lymphocytes / Q000276:immunology; D002918:Chymotrypsin; D003488:Cyanogen Bromide; D000939:Epitopes / Q000276:immunology; D014644:Genetic Variation; D008129:Lolium; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments; D011058:Pollen / Q000276:immunology; D013601:T-Lymphocytes / Q000276:immunology; D014357:Trypsin
chemical_list: D000939:Epitopes; D010446:Peptide Fragments; D002918:Chymotrypsin; D014357:Trypsin; D003488:Cyanogen Bromide