Generation of a low Immunoglobulin E-binding mutant of the timothy grass pollen major allergen Phl p 5a

2007 ◽  
Vol 37 (3) ◽  
pp. 441-450 ◽  
Author(s):  
M. Wald ◽  
H. Kahlert ◽  
B. Weber ◽  
M. Jankovic ◽  
W. Keller ◽  
...  
1999 ◽  
Vol 13 (8) ◽  
pp. 843-856 ◽  
Author(s):  
Verena Niederberger ◽  
Brigitte Hayek ◽  
Susanne Vrtala ◽  
Sylvia Laffer ◽  
Anna Twardosz ◽  
...  

2010 ◽  
Vol 2010 ◽  
pp. 1-4 ◽  
Author(s):  
R. Lucassen ◽  
J. Schulte-Pelkum ◽  
C. Csuvarszki ◽  
J. Kleine-Tebbe ◽  
M. Fooke ◽  
...  

Type I hypersensitivity is driven by allergen specific immunoglobulin E (sIgE) and thus sIgE represents a marker for modern allergy diagnosis. Recently, a rapid assay for the detection of sIgE, termed as (Allergy Lateral Flow Assay) ALFA, has been developed. The objective of our study is the evaluation of a scanner-based system for the semiquantitative interpretation of ALFA results. Agreement to Skin Prick Test (SPT, Allergopharma), ALLERG-O-LIQ System (Dr. Fooke), and ImmunoCAP (Phadia) was investigated using 50 sera tested for specific IgE to timothy grass pollen (g6). 35/50 sera were positive by SPT, ALLERG-O-LIQ, and ImmunoCAP. Excellent agreement was observed between ALFA results and SPT, ImmunoCAP, and ALLERG-O-LIQ. Area under the curve (AUC) values were found at 1.0, and 100% sensitivity and specificity was found versus all other methods. Visual- and scanner-based interpretation of the ALFA results revealed excellent agreement.


2008 ◽  
Vol 389 (7) ◽  
Author(s):  
Kristian Schweimer ◽  
Arnd Petersen ◽  
Roland Suck ◽  
Wolf-Meinhard Becker ◽  
Paul Rösch ◽  
...  

Abstract The major 97-aa timothy grass (Phleum pratense) allergen Phl p 3 was recently isolated from an extract of timothy grass pollen. Sequence comparison classifies this protein as a group 3 allergen. The solution structure of Phl p 3 as determined by nuclear magnetic resonance spectroscopy reveals that the protein consists of a core of hydrophobic amino-acid side chains from two β-sheets of five and four anti-parallel β-strands, respectively. This conformation is very similar to the crystal structure published for Phl p 2 and strongly resembles the known conformation of the carboxy-terminal domain of Phl p 1, the major difference being the loop orientations. Phl p 2 and Phl p 3 show virtually identical immunoreactivity, and comparison of the charged surface amino acids of the two proteins gives initial clues as to the IgE recognition epitopes of these proteins.


2006 ◽  
Vol 36 (6) ◽  
pp. 840-849 ◽  
Author(s):  
Arnd Petersen ◽  
Roland Suck ◽  
Buko Lindner ◽  
Dessi Georgieva ◽  
Martin Ernst ◽  
...  

2007 ◽  
Vol &NA; ◽  
pp. S263
Author(s):  
Irena Matecko ◽  
Kristian Schweimer ◽  
Arnd Petersen ◽  
Wolf-Meinhard Becker ◽  
Roland Suck ◽  
...  

2013 ◽  
Vol 1834 (1) ◽  
pp. 272-283 ◽  
Author(s):  
Danielle Baeyens-Volant ◽  
Nasiha M'Rabet ◽  
Rachida El Mahyaoui ◽  
Ruddy Wattiez ◽  
Mohamed Azarkan

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