PMID- 15013973
OWN - NLM
STAT- MEDLINE
DCOM- 20041018
LR  - 20190509
IS  - 1071-412X (Print)
IS  - 1098-6588 (Electronic)
IS  - 1071-412X (Linking)
VI  - 11
IP  - 2
DP  - 2004 Mar
TI  - Role of C-terminal cysteine residues of Aspergillus fumigatus allergen Asp f 4 in 
      immunoglobulin E binding.
PG  - 261-5
AB  - Among the several allergens cloned and expressed from Aspergillus fumigatus, Asp 
      f 4 is a major one associated with allergic bronchopulmonary aspergillosis 
      (ABPA). The structure-function relationship of allergens is important in 
      understanding the immunopathogenesis, diagnosis, and treatment of allergic 
      diseases. These include the epitopes, conformational or linear, deletion of the N 
      or C terminus or both N and C termini, and glycosylation or nonglycosylation, all 
      of which affect immune responses. Similarly, the role of cysteine residues 
      present in allergens may yield useful information regarding the conformational 
      structure of allergens and the immunoglobulin E (IgE) epitope interaction. Such 
      information may help in developing new strategies towards immunotherapy. In order 
      to define the role of cysteine in the interaction of the antibody with Asp f 4, 
      we have constructed mutants by selectively deleting cysteine residues from the 
      C-terminal region of the Asp f 4. Immunological evaluation of these engineered 
      recombinant constructs was conducted by using sera from patients with ABPA, 
      Aspergillus skin test-positive asthmatics, and healthy controls. The results 
      demonstrate strong IgE binding with Asp f 4 and two truncated mutants, Asp f 
      4(1-234) (amino acids [aa] 1 to 234) and Asp f 4(1-241) (aa 1 to 241), while 
      another mutant, Asp f 4(1-196) (aa 1 to 196), showed reactivity with fewer 
      patients. The result suggests that deletion of cysteines and the alteration of 
      IgE epitopes at the C-terminal end resulted in conformational changes, which may 
      have a potential role in the immunomodulation of the disease.
FAU - Ramachandran, Harikrishnan
AU  - Ramachandran H
AD  - Department of Pediatrics, Allergy-Immunology Division, Medical College of 
      Wisconsin, Milwaukee, Wisconsin 53226, USA.
FAU - Banerjee, Banani
AU  - Banerjee B
FAU - Greenberger, Paul A
AU  - Greenberger PA
FAU - Kelly, Kevin J
AU  - Kelly KJ
FAU - Fink, Jordan N
AU  - Fink JN
FAU - Kurup, Viswanath P
AU  - Kurup VP
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PL  - United States
TA  - Clin Diagn Lab Immunol
JT  - Clinical and diagnostic laboratory immunology
JID - 9421292
RN  - 0 (Allergens)
RN  - 0 (Antigens, Plant)
RN  - 0 (Asp f 4 allergen)
RN  - 0 (Peptide Fragments)
RN  - 37341-29-0 (Immunoglobulin E)
RN  - K848JZ4886 (Cysteine)
SB  - IM
MH  - Allergens/*genetics/*immunology/metabolism
MH  - Amino Acid Sequence
MH  - Antigens, Plant
MH  - Aspergillus fumigatus/*genetics/*immunology
MH  - Blotting, Western
MH  - Cysteine/immunology
MH  - Immunoglobulin E/*immunology/metabolism
MH  - Molecular Sequence Data
MH  - Peptide Fragments/immunology/metabolism
PMC - PMC371203
EDAT- 2004/03/12 05:00
MHDA- 2004/10/19 09:00
PMCR- 2004/03/01
CRDT- 2004/03/12 05:00
PHST- 2004/03/12 05:00 [pubmed]
PHST- 2004/10/19 09:00 [medline]
PHST- 2004/03/12 05:00 [entrez]
PHST- 2004/03/01 00:00 [pmc-release]
AID - 0187 [pii]
AID - 10.1128/cdli.11.2.261-265.2004 [doi]
PST - ppublish
SO  - Clin Diagn Lab Immunol. 2004 Mar;11(2):261-5. doi: 
      10.1128/cdli.11.2.261-265.2004.