Botanical immunocytochemistry: a review with special reference to pollen antigens and allergens

Knox, R. B.; Vithanage, H. I. M. V.; Howlett, Barbara J.

doi:10.1007/bf01006951

Cited by 39 publications

(16 citation statements)

References 46 publications

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“…Thus, alternative preparation techniques had to be developed. Grass pollen grains were fixed in absolute methanol [5] or a combination of freezing techniques and direct embedding into plastic was used [6, 7] thus avoiding aqueous fixatives and graded ethanol series. These studies localized pollen antigens and allergens in the wall and occasionally in the cytoplasm of the pollen grains.…”

Section: Introductionmentioning

confidence: 99%

In situ Localization of Pollen Allergens by Immunogold Electron Microscopy: Allergens at Unexpected Sites

Grote¹

1999

Int Arch Allergy Immunol

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The windborne pollen grains of many trees and grasses contain a number of highly water–soluble (glyco)proteins which upon moistening, e.g. on the human respiratory mucosa, rapidly diffuse out of the pollen grain. In susceptible individuals, they may cause allergic reactions. Because of their rapid release from the pollen, pollen allergens were expected to be located in the outermost layers of the pollen grain, i.e. on the surface and in the wall (exine, intine). First attempts to localize allergens by microscopic methods in the pollen grain supported this view. However, since conventional preparation methods were used, artificial mobilization of allergens could not be excluded. Based on new, completely anhydrous preparation protocols and on the immunogold–labeling technique, pollen allergens were electron–microscopically shown to be located in the interior of the pollen grain, i.e. in the cytoplasm, often within ribosome–rich areas. This unexpected result was obtained in all strictly anhydrously prepared pollen species. The biological function of these allergens is largely unknown, however, clues as to possible cellular functions have been obtained for the birch pollen major allergen Bet v 1.

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Section: Introductionmentioning

confidence: 99%

In situ Localization of Pollen Allergens by Immunogold Electron Microscopy: Allergens at Unexpected Sites

Grote¹

1999

Int Arch Allergy Immunol

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“…tvall proteins are located in the intine of grass pollen as inclusions of a tubular aspect (Heslop-Harrison 1979) and seem to include allergenic proteins (Knox et al 1980, Grote et al 1991. When hydratation of the membranes occurs, inclusions arc dissolved and proteins diffuse principally through the Zwischenkorper (Knox & Heslop-Harrison 1970, Heslop-Hamson 1979.…”

Section: Discussionmentioning

confidence: 99%

“…When hydratation of the membranes occurs, inclusions arc dissolved and proteins diffuse principally through the Zwischenkorper (Knox & Heslop-Harrison 1970, Heslop-Hamson 1979. Knox et al 1980.…”

Section: Discussionmentioning

confidence: 99%

Secale Cereale Pollen: Botanical Reasons for Variability in the Quality of Allergenic Extracts

Vga¹,

Cuevas

López

et al. 1995

Grana

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“…In contrast, Pex protein extracted from pollen and detected by protein gel blot analysis may represent a soluble pool of Pex molecules accumulated in the intine, the site of Pex proteins in mature pollen (Figure 7). The intine is a protein-rich extracellular matrix that contains readily extractable proteins, such as hydrolytic enzymes and some allergens (Knox and Heslop-Harrison, 1976;Knox et al, 1980). It is possible that the intine is also the site of proteins stored in preparation for pollen tube germination and growth.…”

Section: Association Of Pex Proteins With the Pollen Tube Wallmentioning

confidence: 99%

Extensin-like Glycoproteins in the Maize Pollen Tube Wall.

et al. 1995

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We recently described the cloning and characterization of Pexl, a maize pollen-specific gene with an extensin-like domain. Here, we report that antibodies raised against a Pex fusion protein and a Pex synthetic peptide recognize a protein doublet with an apparent molecular mass of -300 kD as well as larger proteins in pollen extracts. These proteins were not detected in extracts of seedling, endosperm, ear, silk, root, leaf, wounded leaf, meiotic tassel, or young microspore.After deglycosylation, only the protein doublet was detected by the anti-Pex antiserum, suggesting that the higher molecular m a s proteins represent a glycosylated form of the Pex proteins. The anti-Pex antiserum was also used in immunolocalization experiments with in vitro-germinated pollen. With

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Botanical immunocytochemistry: a review with special reference to pollen antigens and allergens

Cited by 39 publications

References 46 publications

In situ Localization of Pollen Allergens by Immunogold Electron Microscopy: Allergens at Unexpected Sites

In situ Localization of Pollen Allergens by Immunogold Electron Microscopy: Allergens at Unexpected Sites

Secale Cereale Pollen: Botanical Reasons for Variability in the Quality of Allergenic Extracts

Extensin-like Glycoproteins in the Maize Pollen Tube Wall.

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