2opo
From Proteopedia
(New page: 200px<br /><applet load="2opo" size="450" color="white" frame="true" align="right" spinBox="true" caption="2opo, resolution 1.75Å" /> '''Crystal structure of...) |
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| - | [[Image:2opo.gif|left|200px]]<br /><applet load="2opo" size=" | + | [[Image:2opo.gif|left|200px]]<br /><applet load="2opo" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2opo, resolution 1.75Å" /> | caption="2opo, resolution 1.75Å" /> | ||
'''Crystal structure of the calcium-binding pollen allergen Che a 3'''<br /> | '''Crystal structure of the calcium-binding pollen allergen Che a 3'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: Little is known about the molecular properties of chenopod | + | BACKGROUND: Little is known about the molecular properties of chenopod allergens. Recently, profilin and 2 EF-hand calcium-binding protein (polcalcin) have been shown to play a role in chenopod pollinosis. OBJECTIVE: We sought to analyze these panallergens in chenopod pollen and to evaluate their involvement in the allergy to this biologic source. METHODS: Profilin and polcalcin were purified to homogeneity and characterized by using spectrometric and chemical methods. Immunologic analyses were performed by means of immunoblotting, ELISA, and competitive inhibition assays with olive profilin- and polcalcin-specific rabbit polyclonal antibodies and sera from patients with chenopod allergy. cDNAs encoding these proteins were cloned by means of PCR and sequenced. RESULTS: Purified Che a 2 (profilin) and Che a 3 (polcalcin) exhibited prevalences of 55% and 46%, respectively, in patients (n=104) hypersensitive to chenopod pollen. Both purified allergens individually inhibited the IgE binding to the whole pollen extract and showed strong cross-reactivity with the corresponding olive pollen profilin (Ole e 2) and polcalcin (Ole e 3). Chenopod profilin consists of a 131-amino-acid chain that displays identities of approximately 75% and 82% with pollen and food profilins, respectively. Che a 3 (86 amino acids) displays similarity (65% to 82% identity) with polcalcins from pollens of olive, birch, alder, rapeseed, and timothy. CONCLUSION: Profilin and polcalcin are relevant panallergens in chenopod pollen and good candidates to be involved in IgE cross-reactivity with other pollen sources, thus explaining the highly frequent polysensitization of patients allergic to chenopod. |
==About this Structure== | ==About this Structure== | ||
| - | 2OPO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chenopodium_album Chenopodium album] with CA and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. This structure | + | 2OPO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chenopodium_album Chenopodium album] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1PMZ. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OPO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: ef-hand]] | [[Category: ef-hand]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:21:13 2008'' |
Revision as of 16:21, 21 February 2008
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Crystal structure of the calcium-binding pollen allergen Che a 3
Overview
BACKGROUND: Little is known about the molecular properties of chenopod allergens. Recently, profilin and 2 EF-hand calcium-binding protein (polcalcin) have been shown to play a role in chenopod pollinosis. OBJECTIVE: We sought to analyze these panallergens in chenopod pollen and to evaluate their involvement in the allergy to this biologic source. METHODS: Profilin and polcalcin were purified to homogeneity and characterized by using spectrometric and chemical methods. Immunologic analyses were performed by means of immunoblotting, ELISA, and competitive inhibition assays with olive profilin- and polcalcin-specific rabbit polyclonal antibodies and sera from patients with chenopod allergy. cDNAs encoding these proteins were cloned by means of PCR and sequenced. RESULTS: Purified Che a 2 (profilin) and Che a 3 (polcalcin) exhibited prevalences of 55% and 46%, respectively, in patients (n=104) hypersensitive to chenopod pollen. Both purified allergens individually inhibited the IgE binding to the whole pollen extract and showed strong cross-reactivity with the corresponding olive pollen profilin (Ole e 2) and polcalcin (Ole e 3). Chenopod profilin consists of a 131-amino-acid chain that displays identities of approximately 75% and 82% with pollen and food profilins, respectively. Che a 3 (86 amino acids) displays similarity (65% to 82% identity) with polcalcins from pollens of olive, birch, alder, rapeseed, and timothy. CONCLUSION: Profilin and polcalcin are relevant panallergens in chenopod pollen and good candidates to be involved in IgE cross-reactivity with other pollen sources, thus explaining the highly frequent polysensitization of patients allergic to chenopod.
About this Structure
2OPO is a Single protein structure of sequence from Chenopodium album with and as ligands. This structure supersedes the now removed PDB entry 1PMZ. Full crystallographic information is available from OCA.
Reference
Profilin (Che a 2) and polcalcin (Che a 3) are relevant allergens of Chenopodium album pollen: isolation, amino acid sequences, and immunologic properties., Barderas R, Villalba M, Pascual CY, Batanero E, Rodriguez R, J Allergy Clin Immunol. 2004 Jun;113(6):1192-8. PMID:15208604
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