TY - JOUR
T1 - Cladosporium herbarum translationally controlled tumor protein (TCTP) is an IgE-binding antigen and is associated with disease severity
AU - Rid, Raphaela
AU - Simon-Nobbe, Birgit
AU - Langdon, Jacqueline
AU - Holler, Claudia
AU - Wally, Verena
AU - Pöll, Verena
AU - Ebner, Christof
AU - Hemmer, Wolfgang
AU - Hawranek, Thomas
AU - Lang, Roland
AU - Richter, Klaus
AU - MacDonald, Susan
AU - Rinnerthaler, Mark
AU - Laun, Peter
AU - Mari, Adriano
AU - Breitenbach, Michael
N1 - Funding Information:
We are grateful to the Austrian Science Fund FWF (Vienna, Austria) for grants S9302-B05 (to M.B.) and S8812-MED (to B.S.-N.), to the EC (Brussels, Europe) for project MIMAGE (contract no. 512020; to M.B.) as well as to Peter Sheffield for providing us the fusion vectors pHIS parallel 2 and pGST parallel 2.
PY - 2008/1
Y1 - 2008/1
N2 - Cladosporium herbarum represents one of the most important world-wide occurring allergenic fungal species. The prevalence of IgE reactivity to C. herbarum in patients suffering from allergy varies between 5 and 30% in the different climatic zones. Since mold allergy has often been associated with severe asthma, along with other allergic symptoms, it is important to define more comprehensively the allergen repertoire of this ascomycete. In this context we are reporting our successful approach to identify, clone, produce as a recombinant protein, purify and further characterize a new C. herbarum allergen which is a close homolog of the human translationally controlled tumor protein (TCTP, also called histamine releasing factor, HRF). The immunoreactivity of both pure recombinant molecules was investigated by means of immunoblot analyses, enzyme-linked immunosorbent assays as well as histamine release studies. To summarize, IgE antibodies from five out of nine individuals recognized both the human and the fungal protein in immunoblots. The latter was able to cause histamine release from human basophils with about half the efficiency compared to its human homolog HRF. Cross-inhibition assays showed that the patients' IgEs recognize common epitopes on both the human and C. herbarum proteins, but however, only pre-incubation with C. herbarum TCTP could completely inhibit reactivity with HRF. Furthermore, it appears that patients reactive to TCTP have a higher probability to suffer from asthma than other allergic patients.
AB - Cladosporium herbarum represents one of the most important world-wide occurring allergenic fungal species. The prevalence of IgE reactivity to C. herbarum in patients suffering from allergy varies between 5 and 30% in the different climatic zones. Since mold allergy has often been associated with severe asthma, along with other allergic symptoms, it is important to define more comprehensively the allergen repertoire of this ascomycete. In this context we are reporting our successful approach to identify, clone, produce as a recombinant protein, purify and further characterize a new C. herbarum allergen which is a close homolog of the human translationally controlled tumor protein (TCTP, also called histamine releasing factor, HRF). The immunoreactivity of both pure recombinant molecules was investigated by means of immunoblot analyses, enzyme-linked immunosorbent assays as well as histamine release studies. To summarize, IgE antibodies from five out of nine individuals recognized both the human and the fungal protein in immunoblots. The latter was able to cause histamine release from human basophils with about half the efficiency compared to its human homolog HRF. Cross-inhibition assays showed that the patients' IgEs recognize common epitopes on both the human and C. herbarum proteins, but however, only pre-incubation with C. herbarum TCTP could completely inhibit reactivity with HRF. Furthermore, it appears that patients reactive to TCTP have a higher probability to suffer from asthma than other allergic patients.
KW - Allergy
KW - Autoreactivity
KW - Cladosporium herbarum
KW - Histamine releasing factor
KW - Mold
KW - TCTP
UR - https://www.scopus.com/pages/publications/34548314102
UR - https://www.scopus.com/pages/publications/34548314102#tab=citedBy
U2 - 10.1016/j.molimm.2007.06.002
DO - 10.1016/j.molimm.2007.06.002
M3 - Article
C2 - 17645945
AN - SCOPUS:34548314102
SN - 0161-5890
VL - 45
SP - 406
EP - 418
JO - Molecular Immunology
JF - Molecular Immunology
IS - 2
ER -