Fusion of Na-ASP-2 with human immunoglobulin Fcγ abrogates histamine release from basophils sensitized with anti-Na-ASP-2 IgE

Parasite Immunology

Volumn 34, Issue 8-9, 2012, Pages 404-411

  Zhan, B ^a,b   Santiago, H ^c   Keegan, B ^a,b   Gillespie, P ^a,b   Xue, J ^d   Bethony, J ^e   De Oliveira, L M ^e   Jiang, D ^e   Diemert, D ^e   Xiao, S H ^d   Jones, K ^a,b   Feng, X ^f   Hotez, P J ^a,b   Bottazzi, M E ^a,b  

^a BAYLOR COLLEGE OF MEDICINE   (United States)

^b TEXAS CHILDREN S HOSPITAL   (United States)

^c NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES   (United States)

^d CHINESE CENTER FOR DISEASE CONTROL AND PREVENTION   (China)

^e GEORGE WASHINGTON UNIVERSITY SCHOOL OF MEDICINE AND HEALTH SCIENCES   (United States)

^f JILIN MEDICAL COLLEGE   (China)

Author keywords

Allergy; Fc RIIb; Fc RI; Hookworm; IgE; Na ASP 2; Necator americanus; Vaccine

Indexed keywords

ALUMINUM HYDROXIDE; ANCYLOSTOMA CANINUM ANCYLOSTOMA SECRETED PROTEIN 2; CHIMERIC PROTEIN; FC RECEPTOR IIB; HELMINTH PROTEIN; HYBRID PROTEIN; IMMUNOGLOBULIN E; IMMUNOGLOBULIN FC FRAGMENT; IMMUNOGLOBULIN FC GAMMA NECATOR AMERICANUS ANCYLOSTOMA SECRETED PROTEIN 2; IMMUNOGLOBULIN G; NECATOR AMERICANUS ANCYLOSTOMA SECRETED PROTEIN 2; UNCLASSIFIED DRUG;

ALLERGIC REACTION; ANCYLOSTOMIASIS; ANIMAL EXPERIMENT; ANIMAL MODEL; ANTIGENICITY; ARTICLE; BASOPHIL; CONTROLLED STUDY; DOG; DRUG DESIGN; DRUG EFFECT; DRUG FORMULARY; DRUG HYPERSENSITIVITY; GENETIC ENGINEERING; HISTAMINE RELEASE; HUMAN; HUMAN CELL; IMMUNOGENICITY; MOUSE; NECATOR AMERICANUS; NECATORIASIS; NONHUMAN; NUCLEOTIDE SEQUENCE; PICHIA PASTORIS; PRIORITY JOURNAL; PROTEIN EXPRESSION; VACCINATION;

ANIMALS; ANTIGENS, HELMINTH; BASOPHILS; CRICETINAE; DOGS; GENE EXPRESSION; HISTAMINE RELEASE; HUMANS; HYPERSENSITIVITY; IMMUNIZATION; IMMUNOGLOBULIN E; IMMUNOGLOBULIN FC FRAGMENTS; IMMUNOGLOBULINS; NECATOR AMERICANUS; PICHIA; RECOMBINANT FUSION PROTEINS; SKIN; VACCINATION;

ANCYLOSTOMATOIDEA; CANIS FAMILIARIS; CRICETINAE; NECATOR AMERICANUS; PICHIA PASTORIS;

EID: 84864772495     PISSN: 01419838     EISSN: 13653024     Source Type: Journal    
DOI: 10.1111/j.1365-3024.2012.01371.x     Document Type: Article

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