The Crystal Structure of the Major Cat Allergen Fel d 1, a Member of the Secretoglobin Family

Kaiser, Liselotte; Grönlund, Hans; Sandalova, T.; Ljunggren, Hans‐Gustaf; Hage, Marianne van; Achour, Adnane; Schneider, Günter

doi:10.1074/jbc.m304740200

Cited by 109 publications

(127 citation statements)

References 55 publications

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“…2) demonstrates that these share the same four ␣-helix secondary structure that has been observed in structures of rabbit uteroglobin and cat Fel dI (Mornon et al 1980;Kaiser et al 2003). They also share the three cysteine residues that form single intrachain and interchain disulfide bonds in the Fel dI heterodimer.…”

Section: Secretoglobin Protein Structurementioning

confidence: 85%

“…The detection of multiple Abpa-like and Abpbg-like genes in rodents yielded an opportunity to compare their sequences with the homologous chains of the cat allergen Fel dI (chains 1 and 2, respectively), whose protein tertiary structure has been determined (Kaiser et al 2003). ABP␣-like sequences are closely related to cat Fel dI chain 1, whereas ABP␤␥-like sequences are closely related to Fel dI chain 2.…”

Section: Secretoglobin Protein Structurementioning

confidence: 99%

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Comparative Evolutionary Genomics of Androgen-Binding Protein Genes

Emes¹,

Riley²,

Laukaitis

et al. 2004

Genome Res.

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Allelic variation within the mouse androgen-binding protein (ABP) ␣ subunit gene (Abpa) has been suggested to promote assortative mating and thus prezygotic isolation. This is consistent with the elevated evolutionary rates observed for the Abpa gene, and the Abpb and Abpg genes whose products (ABP␤ and ABP␥) form heterodimers with ABP␣. We have investigated the mouse sequence that contains the three Abpa/b/g genes, and orthologous regions in rat, human, and chimpanzee genomes. Our studies reveal extensive "remodeling" of this region: Duplication rates of Abpa-like and Abpbg-like genes in mouse are >2 orders of magnitude higher than the average rate for all mouse genes; synonymous nucleotide substitution rates are twofold higher; and the Abpabg genomic region has expanded nearly threefold since divergence of the rodents. During this time, one in six amino acid sites in ABP␤␥-like proteins appear to have been subject to positive selection; these may constitute a site of interaction with receptors or ligands. Greater adaptive variation among Abpbg-like sequences than among Abpa-like sequences suggests that assortative mating preferences are more influenced by variation in Abpbg-like genes. We propose a role for ABP␣/␤/␥ proteins as pheromones, or in modulating odorant detection. This would account for the extraordinary adaptive evolution of these genes, and surrounding genomic regions, in murid rodents.

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Section: Secretoglobin Protein Structurementioning

confidence: 85%

Section: Secretoglobin Protein Structurementioning

confidence: 99%

Comparative Evolutionary Genomics of Androgen-Binding Protein Genes

Emes¹,

Riley²,

Laukaitis

et al. 2004

Genome Res.

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“…Recent studies have revealed that almost all important mammalderived respiratory allergens are lipocalins, the one exception being Fel d 1 of cat (27,28). Despite this, human T cell epitopes of lipocalin allergens are largely unknown.…”

Section: Discussionmentioning

confidence: 99%

T Cell Epitope-Containing Peptides of the Major Dog Allergen Can f 1 as Candidates for Allergen Immunotherapy

Immonen

Farci

Taivainen

et al. 2005

The Journal of Immunology

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One prerequisite for developing peptide-based allergen immunotherapy is knowing the T cell epitopes of an allergen. In this study, human T cell reactivity against the major dog allergen Can f 1 was investigated to determine peptides suitable for immunotherapy. Seven T cell epitope regions (A–G) were found in Can f 1 with specific T cell lines and clones. The localization of the epitope regions shows similarities with those of the epitopes found in Bos d 2 and Rat n 1. On average, individuals recognized three epitopes in Can f 1. Our results suggest that seven 16-mer peptides (p15–30, p33–48, p49–64, p73–88, p107–122, p123–138, and p141–156), each from one of the epitope regions, show widespread T cell reactivity in the population studied, and they bind efficiently to seven HLA-DRB1 molecules (DRB1*0101, DRB1*0301, DRB1*0401, DRB1*0701, DRB1*1101, DRB1*1301, and DRB1*1501) predominant in Caucasian populations. Therefore, these peptides are potential candidates for immunotherapy of dog allergy.

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“…The cavity observed in the Der p 5 dimer is particularly interesting, considering the existence of many allergens with hydrophobic cavities that bind lipid-like ligands. For example, the cat allergen Fel d 1 binds steroid-like molecules (40); the horse allergen Equ c 1 and the mouse allergen Mus m 1 are lipocalins (41,42), and Der f 2 was demonstrated to bind lipopolysaccharide (43). Interestingly, the crystal structures of both Der p 2 and Bet v 1 contained apparent ligands in a hydrophobic environment with difficult to interpret electron density (44,45).…”

Section: Discussionmentioning

confidence: 99%

Der p 5 Crystal Structure Provides Insight into the Group 5 Dust Mite Allergens

Mueller

Gosavi

Krahn

et al. 2010

Journal of Biological Chemistry

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Group 5 allergens from house dust mites elicit strong IgE antibody binding in mite-allergic patients. The structure of Der p 5 was determined by x-ray crystallography to better understand the IgE epitopes, to investigate the biologic function in mites, and to compare with the conflicting published Blo t 5 structures, designated 2JMH and 2JRK in the Protein Data Bank. Der p 5 is a three-helical bundle similar to Blo t 5, but the interactions of the helices are more similar to 2JMH than 2JRK. The crystallographic asymmetric unit contains three dimers of Der p 5 that are not exactly alike. Solution scattering techniques were used to assess the multimeric state of Der p 5 in vitro and showed that the predominant state was monomeric, similar to Blo t 5, but larger multimeric species are also present. In the crystal, the formation of the Der p 5 dimer creates a large hydrophobic cavity of ϳ3000 Å 3 that could be a ligand-binding site. Many allergens are known to bind hydrophobic ligands, which are thought to stimulate the innate immune system and have adjuvant-like effects on IgE-mediated inflammatory responses.

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The Crystal Structure of the Major Cat Allergen Fel d 1, a Member of the Secretoglobin Family

Cited by 109 publications

References 55 publications

Comparative Evolutionary Genomics of Androgen-Binding Protein Genes

Comparative Evolutionary Genomics of Androgen-Binding Protein Genes

T Cell Epitope-Containing Peptides of the Major Dog Allergen Can f 1 as Candidates for Allergen Immunotherapy

Der p 5 Crystal Structure Provides Insight into the Group 5 Dust Mite Allergens

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