Recombinant fusion proteins assembling Der p 1 and Der p 2 allergens from dermatophagoides pteronyssinus

International Archives of Allergy and Immunology

Volumn 153, Issue 2, 2010, Pages 141-151

  Bussières, Laetitia ^a   Bordas Le Floch, Véronique ^a   Bulder, Ingrid ^a   Chabre, Henri ^a   Nony, Emmanuel ^a   Lautrette, Aurélie ^a   Berrouet, Christelle ^a   Nguefeu, Yvette ^a   Horiot, Stéphane ^a   Baron Bodo, Véronique ^a   Van Overtvelt, Laurence ^a   De Conti, Anne Marie ^a   Schlegel, Anne ^b   Maguet, Nicolas ^b   Mouz, Nicolas ^b   Lemoine, Pierrick ^a   Batard, Thierry ^a   Moingeon, Philippe ^a  

^a Stallergenes SA   (France)

^b PX Therapeutics   (France)

Author keywords

Allergy vaccine; Der p 1; Der p 2; Fusion protein; House dust mite; Immunotherapy; Recombinant allergen

Indexed keywords

DER P 1 ALLERGEN; DER P 2 ALLERGEN; HOUSE DUST ALLERGEN; HYBRID PROTEIN; IMMUNOGLOBULIN E; MONOCLONAL ANTIBODY; MUTANT PROTEIN; POLYCLONAL ANTIBODY; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; ARTHROPOD PROTEIN; CYSTEINE PROTEINASE; DERMATOPHAGOIDES PTERONYSSINUS ANTIGEN P 1; DERMATOPHAGOIDES PTERONYSSINUS ANTIGEN P 2; VACCINE;

ARTICLE; BASOPHIL; CD4+ T LYMPHOCYTE; CIRCULAR DICHROISM; DERMATOPHAGOIDES PTERONYSSINUS; DISULFIDE BOND; DRUG CONJUGATION; DRUG SYNTHESIS; ESCHERICHIA COLI; HOUSE DUST ALLERGY; HUMAN; HUMAN CELL; IMMUNOBLOTTING; LYMPHOCYTE PROLIFERATION; NONHUMAN; PICHIA PASTORIS; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; T LYMPHOCYTE ACTIVATION; AMINO ACID SEQUENCE; ANIMAL; BIOSYNTHESIS; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; HYPERSENSITIVITY; IMMUNOLOGY; LYMPHOCYTE ACTIVATION; MOLECULAR GENETICS; PHYSIOLOGY; PICHIA; T LYMPHOCYTE;

AMINO ACID SEQUENCE; ANIMALS; ANTIGENS, DERMATOPHAGOIDES; BASOPHILS; DERMATOPHAGOIDES PTERONYSSINUS; ESCHERICHIA COLI; HUMANS; HYPERSENSITIVITY; LYMPHOCYTE ACTIVATION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PICHIA; RECOMBINANT FUSION PROTEINS; T-LYMPHOCYTES; VACCINES; ARTHROPOD PROTEINS; CYSTEINE ENDOPEPTIDASES;

EID: 77950942365     PISSN: 10182438     EISSN: None     Source Type: Journal    
DOI: 10.1159/000312631     Document Type: Article

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