Fel d 1
| Major allergen I polypeptide chain 2 | |||||||
|---|---|---|---|---|---|---|---|
 | |||||||
| Identifiers | |||||||
| Symbol | CH2 | ||||||
| Alt. symbols | Fel d I, AG4, Allergen Cat-1 | ||||||
| NCBI gene | 677879 | ||||||
| PDB | 1PUO | ||||||
| UniProt | P30440 | ||||||
| |||||||
| Allergen Fel d I-B chain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 structural characterization of the tetrameric form of the major cat allergen fel d 1 | |||||||||
| Identifiers | |||||||||
| Symbol | Feld-I_B | ||||||||
| Pfam | PF09252 | ||||||||
| Pfam clan | CL0370 | ||||||||
| InterPro | IPR015332 | ||||||||
| SCOP2 | 1puo / SCOPe / SUPFAM | ||||||||
| |||||||||
Fel d 1 is a protein that in cats is encoded by the CH1 (chain 1/Fel d 1-A) and CH2 (chain 2/Fel d 1-B) genes.[2][3]
Fel d 1, produced largely in cat saliva and sebaceous glands, is the primary allergen present on cats and kittens.[1] Fel d 1 is also produced by cat skin itself.[4] The protein is of an unknown function to the animal but causes an IgG or IgE reaction in sensitive humans (either as an allergic or asthmatic response). Removal of soft surfaces in the home (carpet, furniture), frequent washings of bed linens, HEPA filters and even washing cats has been proven to reduce the amounts of Fel d 1 present in the home.
Female cats produce a lower level of Fel d 1 than males, and neutered males produce a lower level of Fel d 1 than unneutered males.[5]
Neutered males produce Fel d 1 in levels similar to females (both intact and spayed females produce Fel d 1 in similar levels). Even though females and neutered males produce Fel d 1 in lower levels, they still produce enough to cause allergic symptoms in sensitive individuals.
Structure
The complete quaternary structure of Fel d 1 has been determined.[1] The allergen is a tetrameric glycoprotein consisting of two disulfide-linked heterodimers of chains 1 and 2. Fel d 1 chains 1 and 2 share structural similarity with uteroglobin, a secretoglobin superfamily member; chain 2 is a glycoprotein with N-linked oligosaccharides. Both chains share an all alpha-helical structure.[1]
See also
References
- ^ a b c d PDB: 1PUO; Kaiser L, Grönlund H, Sandalova T, Ljunggren HG, van Hage-Hamsten M, Achour A, Schneider G (September 2003). "The crystal structure of the major cat allergen Fel d 1, a member of the secretoglobin family". J. Biol. Chem. 278 (39): 37730–5. doi:10.1074/jbc.M304740200. PMID 12851385.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ Morgenstern JP, Griffith IJ, Brauer AW, Rogers BL, Bond JF, Chapman MD, Kuo MC (November 1991). "Amino acid sequence of Fel dI, the major allergen of the domestic cat: protein sequence analysis and cDNA cloning". Proc. Natl. Acad. Sci. U.S.A. 88 (21): 9690–4. doi:10.1073/pnas.88.21.9690. PMC 52784. PMID 1946388.
- ^ Griffith IJ, Craig S, Pollock J, Yu XB, Morgenstern JP, Rogers BL (April 1992). "Expression and genomic structure of the genes encoding FdI, the major allergen from the domestic cat". Gene. 113 (2): 263–8. doi:10.1016/0378-1119(92)90405-E. PMID 1572548.
- ^ DABROWSKI, A; VANDERBREMPT, X; SOLER, M; SEGURET, N; LUCCIANI, P; CHARPIN, D; VERVLOET, D. "Cat skin as an important source of Fel d I allergen". Journal of Allergy and Clinical Immunology. 86 (4): 462–465. doi:10.1016/S0091-6749(05)80200-3.
- ^ Sex difference in Fel d 1 allergen production. http://www.jacionline.org/article/S0091-6749(96)70238-5/fulltext . Accessed 31 Oct 2016.