1998
DOI: 10.1016/s0014-5793(98)00174-4
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Molecular cloning of a cDNA encoding a pollen extracellular protein as a potential source of a pollen allergen in Brassica rapa

Abstract: A polyclonal antiserum was raised against the extracellular pollen proteins of Brassica rapa and used for screening the expression cDNA libraries made from immature anthers. We obtained five groups of cDNA clones, including cDNAs similar to PCP1, thioredoxin, and lipid transfer protein (LTP). Recombinant protein of the cDNA clone showing sequence similarity to LTP was demonstrated to bind IgE of a patient allergic to Brassica pollen. The cDNA clone reported here, therefore, represents a novel pollen allergen o… Show more

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Cited by 42 publications
(20 citation statements)
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“…Finally, thioredoxin-like molecules have been found on extracellular pollen and detected in self-incompatibility reactions (88,156). A thioredoxin activity linked to the C terminus of the S gene product seems to be responsible for selfincompatibility.…”
Section: New Functions For Thioredoxins In Plantsmentioning
confidence: 99%
“…Finally, thioredoxin-like molecules have been found on extracellular pollen and detected in self-incompatibility reactions (88,156). A thioredoxin activity linked to the C terminus of the S gene product seems to be responsible for selfincompatibility.…”
Section: New Functions For Thioredoxins In Plantsmentioning
confidence: 99%
“…The PCP-A1 was a cysteine-rich basic protein, and a member of a large protein family, the PCP family (Doughty et al 1998). A cDNA clone homologous to the PCP-A1 gene was also isolated from a cDNA library of immature anthers with polyclonal antiserum against the PCPs (Toriyama et al 1998). By using a surface plasmon resonance sensor (BIAcore) along with chromatographic methods, many PCP-like molecules, which can interact with SLG, were identified in the proteins extracted from the pollen coat, though their interaction was not S haplotype-specific, like PCP-A1 ).…”
Section: Identification and Functional Characterization Of Male S Detmentioning
confidence: 99%
“…Analysis of PCPs, successfully lead to identification of the male S determinant (Heslop-Harrison 1975). Initially, SLG-interactive PCPs were searched (Doughty et al 1993), and these interactive molecules were then characterized as cysteine-rich small proteins (Hiscock et al 1995;Stanchev et al 1996;Toriyama et al 1998;Doughty et al 1998;Takayama et al 2000a). The cysteinerich small proteins were shown to be a < 10kDa basic pollen coat proteins (PCP) by an elegant in vitro bioassay in which PCPs were isolated and fractionated (Stephenson et al 1997).…”
Section: Si Recognition Genes Identified From Anthermentioning
confidence: 99%