Purification, identification and preliminary crystallographic studies of an allergenic protein from<i>Lathyrus sativus</i>

Qureshi, Insaf Ahmed; Sethi, Dhruv; Salunke, Dinakar M.

doi:10.1107/s1744309106028077

Cited by 13 publications

(19 citation statements)

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“…Crystallization and preliminary characterization of LS-24 have been reported earlier (Qureshi et al, 2006). LS-24 crystals were obtained in P2 1 2 1 2 1 space group, with the unit cell dimensions a = 83.2 Å , b = 88.1 Å , and c = 154.5 Å , and four molecules in the asymmetric unit accounting for 56.3% solvent content.…”

Section: Resultsmentioning

confidence: 99%

“…Protein Characterization, Crystallization, and Structure Determination LS-24 was identified as a close homolog of albumin 2 from garden pea, exhibiting 85% sequence identity with it, while functionally screening the grass pea seed proteome (Qureshi et al, 2006;Fig. 1A).…”

Section: Resultsmentioning

confidence: 99%

“…We had earlier isolated LS-24, a protein from the albumin fraction of seed proteins from grass pea (Qureshi et al, 2006). LS-24 shows significant sequence identity with albumin 2 from garden pea (Croy et al, 1984;Harris and Croy, 1985;Gruen et al, 1987;Higgins et al, 1987;Jenne, 1991) and chickpea (Cicer arietinum; Kolberg et al, 1983;Vioque et al, 1998).…”

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confidence: 99%

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Crystal Structure and Functional Insights of Hemopexin Fold Protein from Grass Pea

et al. 2010

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A regulatory protein from grass pea (Lathyrus sativus), LS-24, a close homolog of albumin 2 from garden pea (Pisum sativum) that is associated with polyamine biosynthesis, was characterized and the structure of a hemopexin-type fold among plant proteins illustrated. Crystal structure of LS-24 determined at 2.2 Å resolution by multiple isomorphous replacement phasing showed four-bladed b-propeller structure having a pseudo 4-fold molecular symmetry along a metal ion-binding central channel. The structure represents typical mammalian hemopexin fold with discernible features correlated with the possible functional variations. The protein was found to exist in the dimeric state. While LS-24 dimer binds to spermine in the crystal structure as well as in solution, binding of heme in solution resulted in the dissociation of the dimer into monomers with concomitant release of bound spermine. Interactions of heme and spermine with LS-24 bear physiological implications. While binding of spermine to LS-24 can be linked with polyamine biosynthesis that of heme correlates with oxidative stress. Mutually exclusive binding of heme and spermine in different oligomeric states suggest a role for LS-24 in sensing oxidative stress through a ligand-regulated monomer-dimer transition switch.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Crystal Structure and Functional Insights of Hemopexin Fold Protein from Grass Pea

et al. 2010

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“…As part of our continuing efforts to identify and characterize proteins with allergenic potential from seeds, our group has previously reported the purification and crystallization of novel proteins from Vigna unguiculata (Chanana et al, 2004) and Lathyrus sativus (Qureshi et al, 2006). Here, we report the identification, purification and crystallization of Pru du amandin.…”

Section: Introductionmentioning

confidence: 99%

Purification, identification and preliminary crystallographic studies of Pru du amandin, an allergenic protein fromPrunus dulcis

2007

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Food allergies appear to be one of the foremost causes of hypersensitivity reactions. Nut allergies account for most food allergies and are often permanent. The 360 kDa hexameric protein Pru du amandin, a known allergen, was purified from almonds (Prunus dulcis) by ammonium sulfate fractionation and ionexchange chromatography. The protein was identified by a BLAST homology search against the nonredundant sequence database. Pru du amandin belongs to the 11S legumin family of seed storage proteins characterized by the presence of a cupin motif. Crystals were obtained by the hanging-drop vapour-diffusion method. The crystals belong to space group P4 1 (or P4 3 ), with unit-cell parameters a = b = 150.7, c = 164.9 Å .

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“…Such studies have also been initiated involving other seed proteomes (Chanana et al, 2004;Gaur et al, , 2010Gupta et al, 2008;Qureshi et al, 2006). Here, we report the identification, purification and crystallization of a 45 kDa protein from S. melongena which may have allergenic properties.…”

Section: Introductionmentioning

confidence: 99%

Purification, identification and preliminary crystallographic studies of an allergenic protein fromSolanum melongena

Jain

Salunke

2015

Acta Cryst Sect F

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Solanum melongena (eggplant), a member of the Solanaceae family, is a widely cultivated vegetable crop and is commonly used as a food throughout the world. Allergic reactions caused by members of this family are well known. However, mechanistic analyses to understand their molecular basis have not been adequately explored. In order to address this issue, the 7S vicilin protein (SM80.1) of size 45 kDa was purified from seeds of S. melongena by ammonium sulfate fractionation and size-exclusion chromatography. Significant homology of SM80.1 to an allergy-related protein from S. lycopersicum was identified through a BLAST search. Crystallization attempts with purified protein using the hanging-drop vapour-diffusion method led to hexagonal-shaped crystals. The crystals diffracted to 2.21 Å resolution and belonged to space group P6 3 22, with unit-cell parameters a = 117.9, c = 123.5 Å .

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Purification, identification and preliminary crystallographic studies of an allergenic protein fromLathyrus sativus

Cited by 13 publications

References 14 publications

Crystal Structure and Functional Insights of Hemopexin Fold Protein from Grass Pea

Crystal Structure and Functional Insights of Hemopexin Fold Protein from Grass Pea

Purification, identification and preliminary crystallographic studies of Pru du amandin, an allergenic protein fromPrunus dulcis

Purification, identification and preliminary crystallographic studies of an allergenic protein fromSolanum melongena

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