Studies on the biochemical structure of the major cat allergen Felis domesticus I

Duffort, Oscar; Carreira, J.; Nitti, Gianpaolo; Polo, F.; Lombardero, M.

doi:10.1016/0161-5890(91)90141-6

Cited by 77 publications

(91 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The difference in molecular mass to the cat dander-derived 35-38-kDa nFel d 1 may be explained by the presence of 10 -20% N-linked carbohydrates (16,22) in the natural allergen. We further investigated the possible homodimer formation via rechromatography of the isolated 30-kDa fraction by SEC under dissociating conditions.…”

Section: Discussionmentioning

confidence: 99%

“…Fel d 1, (formerly Cat 1) was first described 25 years ago as the dominant cat allergen (13), and several subsequent studies have characterized the biochemical and immunological nature of Fel d 1 (14 -23). The allergen, a 35-39-kDa acidic glycoprotein containing 10 -20% N-linked carbohydrates (15,16,22), is found in the pelt, saliva, and lacrimal glands of cats (24 -26). It is formed by two non-covalently linked heterodimers (16), each consisting of one 70-residue peptide and one 85- (22), 90-, or 92-residue peptide (17) (i.e.…”

mentioning

confidence: 99%

“…The allergen, a 35-39-kDa acidic glycoprotein containing 10 -20% N-linked carbohydrates (15,16,22), is found in the pelt, saliva, and lacrimal glands of cats (24 -26). It is formed by two non-covalently linked heterodimers (16), each consisting of one 70-residue peptide and one 85- (22), 90-, or 92-residue peptide (17) (i.e. chain 1 and chain 2, respectively) encoded by separate genes (22,27).…”

mentioning

confidence: 99%

“…(35) or manufacturers' protocols were used for DNA manipulations. From published amino acid sequences of Fel d 1 chains 1 and 2 (15)(16)(17), synthetic genes were made by PCR-amplification (Eppendorf Mastercycler, Hamburg, Germany) using overlapping DNA primers from DNA Technology A/S (Århus, Denmark) (Table I). PCR reactions (10 l) containing 1 pmol of each primer, primers 1-4 for chain 1 and 5-10 for chain 2, using AmpliTaq DNA polymerase (Applied Biosystems, Foster City, CA), were used.…”

mentioning

confidence: 99%

See 3 more Smart Citations

Formation of Disulfide Bonds and Homodimers of the Major Cat Allergen Fel d 1 Equivalent to the Natural Allergen by Expression in Escherichia coli

Grönlund

Bergman

Sandström

et al. 2003

Journal of Biological Chemistry

102

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Formation of Disulfide Bonds and Homodimers of the Major Cat Allergen Fel d 1 Equivalent to the Natural Allergen by Expression in Escherichia coli

Grönlund

Bergman

Sandström

et al. 2003

Journal of Biological Chemistry

102

View full text Add to dashboard Cite

“…Each subunit comprises ␣-and ␤-chains that are encoded by two separate genes (15,16). Natural Fel d 1 isolated from cat dander is composed of a mixture of variants comprising both full-length and truncated versions of ␤-chain (17)(18)(19). The folding of the polypeptide chains results in an anti-parallel orientation of the ␣-and ␤-chain(s) held together with three disulfide bridges (20).…”

mentioning

confidence: 99%

Molecular Characterization of Major Cat Allergen Fel d 1

Seppälä

Hägglund

Würtzen

et al. 2005

Journal of Biological Chemistry

View full text Add to dashboard Cite

Localisation of a carbohydrate epitope recognised by human IgE in pollen of Cupressaceae

Canini

Giovinazzi

Iacovacci

et al. 2004

Journal of Plant Research

View full text Add to dashboard Cite

The objectives of the present study were: (1) to localise, at the subcellular level, the allergens in pollen of Cupressaceae species, using a monoclonal antibody (mAb 5E6) that is specific for carbohydrate epitopes of allergenic components of Cupressus arizonica pollen extract; (2) to determine whether the glycidic epitope recognised by mAb 5E6 was present in pollen of allergenic species taxonomically unrelated to Cupressaceae; and (3) to determine whether human IgE purified from monosensitive patients recognises the same epitope as mAb 5E6 in Cupressaceae pollen. Immunogold labelling of mAb 5E6 showed a high density of gold particles on the orbicules, supporting the hypothesis that they are important vectors of allergens. A high density was also found on the exine and in the cytoplasm, with the latter finding confirming that fragments of pollen ruptured under humid conditions can represent a vector. The glycidic epitope recognised by mAb 5E6 was detected in all of the species taxonomically unrelated to Cupressaceae, although with varying density. Human IgE recognised the same epitope as mAb 5E6. These findings are consistent with observations of diffuse allergenic cross-reactivity among various allergens. The in situ localisation of a common epitope recognised by both a monoclonal antibody and human IgE could be of importance in immunotherapy.

show abstract

Studies on the biochemical structure of the major cat allergen Felis domesticus I

Cited by 77 publications

References 35 publications

Formation of Disulfide Bonds and Homodimers of the Major Cat Allergen Fel d 1 Equivalent to the Natural Allergen by Expression in Escherichia coli

Formation of Disulfide Bonds and Homodimers of the Major Cat Allergen Fel d 1 Equivalent to the Natural Allergen by Expression in Escherichia coli

Molecular Characterization of Major Cat Allergen Fel d 1

Localisation of a carbohydrate epitope recognised by human IgE in pollen of Cupressaceae

Contact Info

Product

Resources

About