Recombinant glutathione-S-transferase a major allergen from Alternaria alternata for clinical use in allergy patients.
Mol Immunol
; 43(12): 1927-32, 2006 May.
Article
em En
| MEDLINE
| ID: mdl-16430961
ABSTRACT
Recombinant proteins are used for vaccines, therapy and diagnosis of many diseases. Biological activity of these may differ from native counterpart and needs investigation. The present study aimed to compare recombinant (r) and native (n) glutathione-S-transferase (GST) from Alternaria alternata. Glutathione-S-transferase sequence showed an ORF of 696bp encoding 26-kDa protein with N-terminus conserved domain. Secondary structure of both forms was comparable with melting temperature of 57 and 59 degrees C, respectively. rGST and nGST showed similar enzymatic activity, allergenicity and potency by ELISA inhibition. Histamine release was comparable in 14/17 patients for both the GSTs. rGST and nGST induced proliferation in PBMC at different concentration. Cell supernatant revealed higher IL-4 and IL-5 levels with low levels of IFN-gamma. In summary, recombinant and native GST demonstrated similar physio-chemical, biological and immunological properties and induced comparable cell mediated and humoral response to be used for diagnosis and specific immunotherapy for the fungal allergy cases.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas Fúngicas
/
Alérgenos
/
Rinite Alérgica Sazonal
/
Alternaria
/
Glutationa Transferase
Tipo de estudo:
Observational_studies
Limite:
Adolescent
/
Adult
/
Female
/
Humans
/
Male
/
Middle aged
Idioma:
En
Revista:
Mol Immunol
Ano de publicação:
2006
Tipo de documento:
Article
País de afiliação:
Índia