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Proteome analysis reveals developmentally expressed rice homologues of grass group II pollen allergens

Kerim, Tursun; Imin, Nijat; Natera, Siria Helen Anna; Rolfe, Barry

Description

Three isoallergens of Ory s 2, homologues of grass group II pollen allergens, were identified from rice and characterised by proteome and immunochemical analyses. The N-terminal amino acid sequence profiles of three proteins on a 2-dimensional electrophoresis (2-DE) gel of rice pollen proteins matched 100% to the protein sequences encoded by three rice expressed sequence tags (ESTs). The deduced protein sequences from these ESTs share sequence identities of 41-43% with the protein sequences of...[Show more]

dc.contributor.authorKerim, Tursun
dc.contributor.authorImin, Nijat
dc.contributor.authorNatera, Siria Helen Anna
dc.contributor.authorRolfe, Barry
dc.date.accessioned2015-12-13T23:14:20Z
dc.date.available2015-12-13T23:14:20Z
dc.identifier.issn1445-4408
dc.identifier.urihttp://hdl.handle.net/1885/88559
dc.description.abstractThree isoallergens of Ory s 2, homologues of grass group II pollen allergens, were identified from rice and characterised by proteome and immunochemical analyses. The N-terminal amino acid sequence profiles of three proteins on a 2-dimensional electrophoresis (2-DE) gel of rice pollen proteins matched 100% to the protein sequences encoded by three rice expressed sequence tags (ESTs). The deduced protein sequences from these ESTs share sequence identities of 41-43% with the protein sequences of the group II pollen allergens of different grasses, and sequence identity of 39% with the C-terminal portion of rice group I pollen allergens. Signal peptide sequences, which are similar to the leader peptides of other major pollen allergens, are also present in the deduced amino acid sequences. Polyclonal antibodies, produced in rabbits using Ory s 2 proteins purified by 2-DE, were used to investigate the developmental-stage- and tissue-specific expression of Ory s 2 by immunochemical analysis. Results of immunochemical experiments show that Ory s 2 proteins are expressed only at the late stage of pollen development and they do not have cross-reactivity with group II pollen allergens from some other common grasses.
dc.publisherCSIRO Publishing
dc.sourceFunctional Plant Biology
dc.subjectKeywords: Amino acids; Antibodies; Electrophoresis; Gels; Immunology; Pollen development; Proteins; pollen; Oryctolagus cuniculus; Oryza sativa; Poaceae 2-dimensional gel electrophoresis; Antibody; N-terminal sequencing; Oryza sativa; Western blot
dc.titleProteome analysis reveals developmentally expressed rice homologues of grass group II pollen allergens
dc.typeJournal article
local.description.notesImported from ARIES
local.description.refereedYes
local.identifier.citationvolume30
dc.date.issued2003
local.identifier.absfor060111 - Signal Transduction
local.identifier.ariespublicationMigratedxPub18285
local.type.statusPublished Version
local.contributor.affiliationKerim, Tursun, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationImin, Nijat, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationNatera, Siria Helen Anna, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationRolfe, Barry, College of Medicine, Biology and Environment, ANU
local.bibliographicCitation.issue8
local.bibliographicCitation.startpage843
local.bibliographicCitation.lastpage852
local.identifier.doi10.1071/FP03100
dc.date.updated2015-12-12T08:38:25Z
local.identifier.scopusID2-s2.0-0141501436
CollectionsANU Research Publications

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