scholarly journals Mutational Analysis of Amino Acid Positions Crucial for IgE-Binding Epitopes of the Major Apple (Malus domestica) Allergen, Mal d 1

2005 ◽  
Vol 139 (1) ◽  
pp. 53-62 ◽  
Author(s):  
Yan Ma ◽  
Gabriele Gadermaier ◽  
Barbara Bohle ◽  
Suzanne Bolhaar ◽  
Andre Knulst ◽  
...  
Keyword(s):  
Amino Acid ◽  
Malus Domestica ◽  
Mutational Analysis ◽  
Ige Binding ◽  
Mal D 1

Mutational analysis of amino acid residues involved in IgE-binding to the Malassezia sympodialis allergen Mala s 11

2008 ◽  
Vol 46 (2) ◽  
pp. 294-303 ◽  
Author(s):  
Monica Vilhelmsson ◽  
Andreas G. Glaser ◽  
Daniel Badia Martinez ◽  
Margit Schmidt ◽  
Catharina Johansson ◽  
...  
Keyword(s):  
Amino Acid ◽  
Mutational Analysis ◽  
Amino Acid Residues ◽  
Ige Binding

Partial Amino Acid Sequence of a Cellulase-Like Component with IgE-Binding Properties from Stachybotrys chartarum

2004 ◽  
Vol 133 (2) ◽  
pp. 136-144 ◽  
Author(s):  
Marja Kärkkäinen ◽  
Päivi Raunio ◽  
Jaakko Rautiainen ◽  
Seppo Auriola ◽  
Kaj Hinke ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Stachybotrys Chartarum ◽  
Partial Amino Acid Sequence ◽  
Binding Properties ◽  
Ige Binding

scholarly journals Molecular basis of pollen-related food allergy: identification of a second cross-reactive IgE epitope on Pru av 1, the major cherry (Prunus avium) allergen

2004 ◽  
Vol 385 (1) ◽  
pp. 319-327 ◽  
Author(s):  
Regina WICHE ◽  
Michaela GUBESCH ◽  
Herbert KÖNIG ◽  
Kay FÖTISCH ◽  
Andreas HOFFMANN ◽  
...  
Keyword(s):  
Food Allergy ◽  
Amino Acid ◽  
Prunus Avium ◽  
Protein Structures ◽  
Cross Reactivity ◽  
Type I ◽  
Binding Region ◽  
Leukaemia Cell Line ◽  
Bet V 1 ◽  
Ige Binding

Birch (Betula verrucosa) pollen-associated food allergy is a well-characterized syndrome, which is due to the cross-reactivity of IgE antibodies to homologous allergens in various foods. One crossreacting area on the major birch pollen allergen Bet v 1 and its homologue in cherry (Prunus avium) Pru av 1 has already been identified. This is the so-called ‘P-loop’ region, which encompasses amino acid residues around position 45 and is found on the two virtually identical tertiary protein structures. We tried to determine an additional IgE cross-reacting patch on Pru av 1 and Bet v 1. The putative IgE-binding region on Pru av 1 was localized with a mAb (monoclonal antibody) that was generated against Bet v 1, and cross-reacts with several Bet v 1 homologues in food and inhibits the binding of patients' IgE to Pru av 1. mAb reactivity pattern was analysed and amino acid positions 28 and 108 of Pru av 1 were selected and mutated by site-directed mutagenesis. The Pru av 1 mutants were produced as recombinant proteins and characterized for their folding, mAb- and IgE-binding capacity and allergenic potency with a cellular assay using the humanized rat basophilic leukaemia cell line RBL-25/30. Amino acid position 28 is involved in a second major IgE-binding region on Pru av 1 and probably on Bet v 1. The identification of this second major IgE-binding region is an essential prerequisite to understand the phenomenon of cross-reactivity and its clinical consequences, and to produce hypoallergenic proteins for an improved immunotherapy of type I allergy.

scholarly journals Regulation of Escherichia coli RelA Requires Oligomerization of the C-Terminal Domain

2001 ◽  
Vol 183 (2) ◽  
pp. 570-579 ◽  
Author(s):  
Michal Gropp ◽  
Yael Strausz ◽  
Miriam Gross ◽  
Gad Glaser
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Catalytic Domain ◽  
Mutational Analysis ◽  
Amino Acid Starvation ◽  
E Coli ◽  
Terminal Domain ◽  
Negative Effect ◽  
And Control ◽  
Two Hybrid

ABSTRACT The E. coli RelA protein is a ribosome-dependent (p)ppGpp synthetase that is activated in response to amino acid starvation. RelA can be dissected both functionally and physically into two domains: The N-terminal domain (NTD) (amino acids [aa] 1 to 455) contains the catalytic domain of RelA, and the C-terminal domain (CTD) (aa 455 to 744) is involved in regulating RelA activity. We used mutational analysis to localize sites important for RelA activity and control in these two domains. We inserted two separate mutations into the NTD, which resulted in mutated RelA proteins that were impaired in their ability to synthesize (p)ppGpp. When we caused the CTD inrelA + cells to be overexpressed, (p)ppGpp accumulation during amino acid starvation was negatively affected. Mutational analysis showed that Cys-612, Asp-637, and Cys-638, found in a conserved amino acid sequence (aa 612 to 638), are essential for this negative effect of the CTD. When mutations corresponding to these residues were inserted into the full-length relA gene, the mutated RelA proteins were impaired in their regulation. In attempting to clarify the mechanism through which the CTD regulates RelA activity, we found no evidence for competition for ribosomal binding between the normal RelA and the overexpressed CTD. Results from CyaA complementation experiments of the bacterial two-hybrid system fusion plasmids (G. Karimova, J. Pidoux, A. Ullmann, and D. Ladant, Proc. Natl. Acad. Sci. USA 95:5752–5756, 1998) indicated that the CTD (aa 564 to 744) is involved in RelA-RelA interactions. Our findings support a model in which RelA activation is regulated by its oligomerization state.

Mapping and Mutational Analysis of the IgE-Binding Epitopes on Ara h 1, a Legume Vicilin Protein and a Major Allergen in Peanut Hypersensitivity

1997 ◽  
Vol 245 (2) ◽  
pp. 334-339 ◽  
Author(s):  
A. Wesley Burks ◽  
David Shin ◽  
Gael Cockrell ◽  
J. Steven Stanley ◽  
Ricki M. Helm ◽  
...  
Keyword(s):  
Mutational Analysis ◽  
Major Allergen ◽  
Ige Binding ◽  
Ara H 1

Lysine as a Critical Amino Acid for IgE Binding in Phl p 5b C Terminus

2006 ◽  
Vol 140 (4) ◽  
pp. 285-294 ◽  
Author(s):  
Kirsten Gehlhar ◽  
Kanagalaghata R. Rajashankar ◽  
Eckhard Hofmann ◽  
Christian Betzel ◽  
Wolfgang Weber ◽  
...  
Keyword(s):  
Amino Acid ◽  
Critical Amino Acid ◽  
Ige Binding ◽  
C Terminus

scholarly journals Identification by Mutational Analysis of Amino Acid Residues Essential in the Chaperone Function of Calreticulin

2005 ◽  
Vol 281 (4) ◽  
pp. 2338-2346 ◽  
Author(s):  
Virginie Martin ◽  
Jody Groenendyk ◽  
Simone S. Steiner ◽  
Lei Guo ◽  
Monika Dabrowska ◽  
...  
Keyword(s):  
Amino Acid ◽  
Mutational Analysis ◽  
Amino Acid Residues ◽  
Chaperone Function

scholarly journals Variation in IgE binding potencies of seven Artemisia species depending on content of major allergens

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Lan Zhao ◽  
Wanyi Fu ◽  
Biyuan Gao ◽  
Yi Liu ◽  
Shandong Wu ◽  
...  
Keyword(s):  
Amino Acid ◽  
Artemisia Annua ◽  
Binding Capacity ◽  
Sequence Similarity ◽  
Pollen Allergy ◽  
Amino Acid Sequences ◽  
Pollen Extract ◽  
Ige Binding ◽  
Major Allergens ◽  
Art V 1

Abstract Background Artemisia weed pollen allergy is important in the northern hemisphere. While over 350 species of this genus have been recorded, there has been no full investigation into whether different species may affect the allergen diagnosis and treatment. This study aimed to evaluate the variations in amino acid sequences and the content of major allergens, and how these affect specific IgE binding capacity in representative Artemisia species. Methods Six representative Artemisia species from China and Artemisia vulgaris from Europe were used to determine allergen amino acid sequences by transcriptome, gene sequencing and mass spectrometry of the purified allergen component proteins. Sandwich ELISAs were developed and applied for Art v 1, Art v 2 and Art v 3 allergen quantification in different species. Aqueous pollen extracts and purified allergen components were used to assess IgE binding by ELISA and ImmunoCAP with mugwort allergic patient serum pools and individual sera from five areas in China. Results The Art v 1 and Art v 2 homologous allergen sequences in the seven Artemisia species were highly conserved. Art v 3 type allergens in A. annua and A. sieversiana were more divergent compared to A. argyi and A. vulgaris. The allergen content of Art v 1 group in the seven extracts ranged from 3.4% to 7.1%, that of Art v 2 from 1.0% to 3.6%, and Art v 3 from 0.3% to 10.5%. The highest IgE binding potency for most Chinese Artemisia allergy patients was with A. annua pollen extract, followed by A. vulgaris and A. argyi, with A. sieversiana significantly lower. Natural Art v 1-3 isoallergens from different species have almost equivalent IgE binding capacity in Artemisia allergic patients from China. Conclusion and clinical relevance There was high sequence similarity but different content of the three group allergens from different Artemisia species. Choice of Artemisia annua and A. argyi pollen source for diagnosis and immunotherapy is recommended in China.

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