748 Barn allergy: Isolation and characterization of the major allergens of storage mites: L. destructor

Muthiah, R.; Miller, Marina; Kagen, Steven L.

doi:10.1016/0091-6749(91)92030-5

Cited by 2 publications

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“…The N-terminal sequence of the major L. destructor allergen has been already reported. Thus, Muthiah et al [19] identified 18 residues within the first 29 N-terminal positions, that exactly matches with those amino acids assigned by us at the same positions. Subsequently, van Hage-Hamsten et al [20] described the sequence of the first 18 residues.…”

Section: Discussionsupporting

confidence: 75%

Primary Structure of Lep D I, the Main Lepidoglyphus Destructor Allergen

Varela

Ventas

Carreira

et al. 1994

European Journal of Biochemistry

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The most relevant allergen of the storage mite Lepidoglyphus destructor (Lep d I) has been characterized. Lep d I is a monomer protein of 13273 Da. The primary structure of Lep d I was determined by N‐terminal Edman degradation and partially confirmed by cDNA sequencing. Sequence polymorphism was observed at six positions, with non‐conservative substitutions in three of them. No potential N‐glycosylation site was revealed by peptide sequencing, The 125‐residue sequence of Lep d I shows approximately 40% identity (including the six cysteines) with the overlapping regions of group II allergens from the genus Dermatophagoides, which, however, do not share common allergenic epitopes with Lep d I.

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Section: Discussionsupporting

confidence: 75%

Primary Structure of Lep D I, the Main Lepidoglyphus Destructor Allergen

Varela

Ventas

Carreira

et al. 1994

European Journal of Biochemistry

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Cloning and Sequence Analysis of a cDNA EncodingPso oII, a Mite Group II Allergen of the Sheep Scab Mite (Acari: Psoroptidae)

Temeyer¹,

Soileau²,

Pruett

2002

J Med Entomol

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Psoroptes ovis (Hering), the sheep scab mite, is responsible for psoroptic scabies of cattle and sheep. Reverse translation of 30 N-terminal amino acids of the major P. ovis allergen, previously chosen as a candidate immunogen and identified as a 16 kDa protein yielded a degenerate sequence used to design oligodeoxynucleotide polymerase chain reaction (PCR) primers. Use of the PCR primers with a P. ovis cDNA library succeeded in amplification of a 90 bp cDNA gene fragment that was cloned, sequenced, and used to select unique sequencing/PCR primers. Primer walking generated overlapping subclones which yielded the 588 nucleotide consensus sequence of the cDNA encoding the 143 amino acid P. ovis allergen precursor. Nucleotide and translated sequences of the cDNA were compared with sequences in GenBank and found to be homologous to mite group II allergens Lep d II (formerly Lep d I) of Lepidoglyphus destructor Schrank, DerfII of Dermatophagoides farinae Hughes, Der p II of Derrmatophagoides pteronyssinus (Trouessart), Tyr p II of Tyrophagus putrescentiae (Schrank), Eur m II of Euroglyphus maynei (Cooreman) and Gly d II of Glycophagus domesticus (De Geer). The mature P. ovis allergen is composed of 126 amino acids with a calculated molecular mass of 13,468 Da, three disulfide bonds, and pI of 6.06 with one potential o-glycosylation site at Thr116. We designate the P. ovis 16 kDa protein as Pso o II in conformity with nomenclature for mite group II allergens.

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748 Barn allergy: Isolation and characterization of the major allergens of storage mites: L. destructor

Cited by 2 publications

References 0 publications

Primary Structure of Lep D I, the Main Lepidoglyphus Destructor Allergen

Primary Structure of Lep D I, the Main Lepidoglyphus Destructor Allergen

Cloning and Sequence Analysis of a cDNA EncodingPso oII, a Mite Group II Allergen of the Sheep Scab Mite (Acari: Psoroptidae)

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