2 research outputs found
Proteomic Analysis of Major and Minor Allergens from Isolated Pollen Cytoplasmic Granules
Grass pollen is one of the most important vectors of
aeroallergens.
Under atmospheric conditions, pollen grains can release pollen cytoplasmic
granules (PCGs). The allergens associated with these intrinsic subfractions
induce, in laboratory animals as well as in asthmatic patients, allergic
and inflammatory responses. The objectives of this study were to characterize
the PCGs' intrinsic allergens and to compare them with those of pollen
grains. The water-soluble proteins were extracted from pollen grains
and their PCGs. IgE-binding proteins were analyzed and characterized
through an allergomic strategy: 1- and 2-dimensional gel electrophoresis
(1-DE and 2-DE), immunoblotting, using grass-pollen-sensitized patient
sera, mass spectrometry (MS) analysis, and database searching. Several
of the allergens listed in the IUIS nomenclature, Phl p 1, 4, 5, 6,
and 12, were detected in pollen and PCG extracts, whereas Phl p 11
was found only in PCGs, and Phl p 2 as well as Phl p 13 were found
only in pollen extract. Some other allergens not listed in the IUIS
nomenclature were also characterized in both pollen and PCG extracts.
Since the major grass pollen allergens were found in PCGs and because
of their small size, these submicronic particles should be considered
as very potent sensitizing and challenging respirable vectors of allergens
Proteomic Analysis of Major and Minor Allergens from Isolated Pollen Cytoplasmic Granules
Grass pollen is one of the most important vectors of
aeroallergens.
Under atmospheric conditions, pollen grains can release pollen cytoplasmic
granules (PCGs). The allergens associated with these intrinsic subfractions
induce, in laboratory animals as well as in asthmatic patients, allergic
and inflammatory responses. The objectives of this study were to characterize
the PCGs' intrinsic allergens and to compare them with those of pollen
grains. The water-soluble proteins were extracted from pollen grains
and their PCGs. IgE-binding proteins were analyzed and characterized
through an allergomic strategy: 1- and 2-dimensional gel electrophoresis
(1-DE and 2-DE), immunoblotting, using grass-pollen-sensitized patient
sera, mass spectrometry (MS) analysis, and database searching. Several
of the allergens listed in the IUIS nomenclature, Phl p 1, 4, 5, 6,
and 12, were detected in pollen and PCG extracts, whereas Phl p 11
was found only in PCGs, and Phl p 2 as well as Phl p 13 were found
only in pollen extract. Some other allergens not listed in the IUIS
nomenclature were also characterized in both pollen and PCG extracts.
Since the major grass pollen allergens were found in PCGs and because
of their small size, these submicronic particles should be considered
as very potent sensitizing and challenging respirable vectors of allergens