Immunochemical characterization of pollen

The effectiveness of Cocos nucifera pollen extract immunotherapy (CPE-IT) was studied in 96 patients allergic to C. nucifera pollen. A placebo-controlled study was performed at random for a period of 6–12 months. The clinical status of the patients measured by the symptom-medication scores demonstrated that C. nucifera pollen-allergic patients had significant (p < 0.005) clinical improvement after CPE-IT in comparison to placebo treatment. Serological study resulted a significant reduction (p < 0.001) of specific IgE and significant elevation (p < 0.01) of specific IgG in post-therapeutic patients’ sera which were correlated significantly (r = 0.45, p < 0.001); the changes of the above immunoglobulin levels in the placebo-treated patients were nonsignificant. However, there was no correlation between symptom-medication scores and changes in specific serum IgE or IgG levels.

Section: Discussionsupporting

confidence: 70%

“…It flowers round the year and releases a large quantity of pollen [13], which is one of the sources of inhalant al lergens responsible for immediate type I allergic reaction in humans [14], However, IT with C. mtcifera pollen ex tract has not been attempted so far.…”

Section: Introductionmentioning

confidence: 99%

Placebo-Controlled Immunotherapy with Cocos nucifera Pollen Extract

Karmakar

Chatterjee

1994

“…Thus, a major allergenic protein, Bras 2a MW 90 kD, has been isolated and identified in BC pollen extract. In India, studies with Amaranthusspinosus, Xanthium strumarium (weed pollen) and Cocos nucifera (tree pollen) have revealed the glycoproteins of higher MW (128, 103, 116-200 kD, respectively) as major allergenic proteins [18][19][20]. However, with other pollen antigens, such as Ageratum conyzoides, Artemisia scoparia, Cynodon dactylon and Prosopis julijlora, low MW proteins of 10-32 kD have been recorded as major allergenic components [21 24].…”

Section: Discussionmentioning

confidence: 99%

Immunobiochemical Characterization of Brassica campestris Pollen Allergen

Singh

Verma²,

Rai³

et al. 1995

Brαssica campestris (BC), Eng. Mustard, is an important source of pollen allergen, responsible for type I hypersensitivity disorders. In the present study, BC pollen extract was characterized by TLIEF, SDS-PAGE and immunoprinting. The extract separated into 50 silver stained bands of pi 3-9 on isoelectric focusing whereas it resolved into 14 Coomassie blue stained protein bands of 14–100 kD on SDS-PAGE. Immunoblot analysis with individual patient sera detected four allergenic proteins of 90, 67, 60 and 14 kD. BC separated into 8 peaks (Bras 1–8) on DEAE Sephadex A-50 column. Bras 2 was found to be most potent by IgE specific ELISA, hence further fractionated on Sephadex G-200. A protein of 90 kD (Bras 2a) isolated by gel filtration was found to be most allergenic protein by ELISA inhibition. The findings shall be applicable in standardization of future batches of BC pollen extract to be used for allergy diagnosis and immunotherapy.

“…3a, b). Previous studies in India with Cocos nucifera (MWs 10-200 kD), Holoptelea integrifolia (MWs 50-70 kD) and Prosopisjuliflora (MWs 10-20 kD) tree pollen have shown the presence of wide range of allergenically active proteins [23][24][25]. In case of weeds viz.…”

Section: Putranjiva Roxburghii Pollen Allergensmentioning

confidence: 99%

“…The IgE binding capacity of each fraction (4 ml) o f PR obtained from DEAF. Scphadex A-50 column was determined by direct ELISA following the protocol of Jaggi et al [23], A volume of 50 til of each fraction was mixed with 50 pi of carbonate buffer and coated on ELISA plate (Dynatech). The plate was incubated overnight at 4°C.…”

Section: Aterials and M Ethodsmentioning

confidence: 99%

Immunobiochemical Characterization of Putranjiva roxburghii Pollen Extract and Cross-Reactivity with Ricinus communis

Singh

Verma²,

Sridhara³

et al. 1997

Putranjiva roxburghii (PR) pollen has been found to be an important aeroallergen for type I hypersensitivity. In the present study, the IgE binding proteins of PR pollen have been characterized and compared with pollen allergens of Ricinus communis (RC) belonging to family Euphorbiaceae. On isoelectric focusing, PR pollen extract resolved into 35 bands (pI 3–9), whereas SDS-PAGE separated it into 18 protein components (MW 14–100 kD). Pooled patient’s sera (ID +ve to PR) recognized 12 allergenic proteins in Putranjiva and five of them (MWs 92, 80, 55,43 and 30 kD) showed immunologic reactivity to most of the sera samples tested individually by immunoblot. A number of shared allergenic proteins (MWs 92, 80, 66, 50, 43 and 14 kD) were observed between PR and RC pollen extracts on immunoblot using Putranjiva allergic serum pool. Inhibition in the binding for most of PR pollen allergenic proteins was obtained with higher concentration of RC extract than PR itself, depicting the presence of cross-reacting allergens in both. Putranjiva pollen extract was fractionated by a combination of DEAE Sephadex-A 50 and Sephadex-G 200 column chromatography. Periodate deglycosylation of western blotted PR extract and Put I fraction indicated the involvement of carbohydrate moieties in the allergenic activity. Of the two fractions from Put I (la and lb), Put lb was found to be the most allergenic protein by ELISA inhibition. Dot blot analysis with individual patients sera identified it as a major allergen of PR.