556 Identification of two distinct allergenic sites of a rye grass pollen allergen, Lol p IV

Jaggi, Kuldeep S.; Ekramoddoullah, A.K.M.; Kisil, F.T.; Dzuba-Fischer, J.M.M.; Rector, Edward S.; Sehon, A.H.

doi:10.1016/0091-6749(88)90790-7

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“…6). This finding con firms our earlier observation that anti-site B, Mab 12 failed to bind to the tryptic digest of the CB-2 peptide fraction derived from cleavage of Lolp IV by CNBr [10]. It can therefore be speculated that lysine/arginine residues either constitute a part of site B or con tribute to its allergenic/antigenic integrity.…”

Section: Discussionsupporting

confidence: 33%

“…We have previously reported on the identification of two allergenic sites A and B on Lol p IV using mu rine anti-Lol p IV Mabs [10]. In the present study, site A was detected by Mab 90 only in HPLC peptide frac tions 92-98.…”

Section: Discussionmentioning

confidence: 53%

“…Since, the IgE antibody response to Lol p IV can differ from one individual to another [10], it is more than likely that testing of peptide fragments with other grass aller gic patients' sera would reveal an allergenic activity profile different from the one obtained in the pres ent study (fig. 3).…”

Section: Discussionmentioning

confidence: 99%

“…With the aid of murine anti-Lol p IV monoclonal antibodies (Mabs), at least two different allergenic sites recognized by human IgE antibodies have been detected and designated as sites A and B [10]. In another study, we found that cleavage of Lol p IV with cyanogen bromide (CNBr) produced peptides, of which two, CB-1 (17.4 kD) and CB-2 (22 kD) retained allergenic activity [11].…”

Section: Introductionmentioning

confidence: 94%

“…The murine anti-Lo/p IV M ab9 0 (anti-site A )and Mab ^(a n tisite B) [10] were used to identify, respectively, the presence of sites A and B in the peptide fractions separated by H PLC. An amount of approximately 1 mg of the Lol p IV peptides generated by CNBr and trypsin digestion were fractionated by HPLC as described above.…”

Section: Detection O F Sites a And B In The Peptide Fractionsmentioning

confidence: 99%

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Allergenic Fragments of Ryegrass (Lolium perenne) Pollen Allergen Lol p IV

Jaggi¹,

Ekramoddoullah²,

Kisil³

1989

Int Arch Allergy Immunol

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To facilitate studies on establishing the nature of structure/function relationships of allergens, ryegrass pollen allergen, Lol p IV, was cleaved into smaller fragments by cyanogen bromide (CNBr) and the resulting peptides were further digested with trypsin. The resulting peptides were then fractionated by high performance liquid chromatography (HPLC) on a C-18 reverse phase column. The allergenic activity of the HPLC fractions was evaluated in terms of their ability to inhibit the binding of ¹²⁵l-Lol p IV to serum IgE antibodies of a grass-allergic patient. Many of these fractions inhibited the binding between the native allergen and IgE antibodies in a dose-dependent manner. The inhibitions were specific, i.e., the fractions did not inhibit the binding between ¹²⁵l-Lol p I (a group-I ryegrass pollen allergen) and the IgE antibodies present in the allergic human serum. The possibility that the allergenic peptide fractions were contaminated by the native undegraded allergen, which might have accounted for the observed inhibition, was ruled out by the fact that the native allergen could not be detected by SDS-PAGE and the elution profiles of allergenically active peptides did not coincide with that of native allergen. One of the allergenic sites recognized by monoclonal antibody (Mab) 90, i.e., site A, was located in HPLC fractions 90–100 while another allergenic site B (recognized by Mab 12) appeared to be lost following the sequential digestion of Lol p IV with CNBr and trypsin.

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Section: Discussionsupporting

confidence: 33%

Section: Discussionmentioning

confidence: 53%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 94%

Section: Detection O F Sites a And B In The Peptide Fractionsmentioning

confidence: 99%

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