Fel d 1

Last updated
Allergen Fel d 1, chain 1 ( P30438 )
Identifiers
SymbolAllergen_Fel_d_I_chain1
InterPro IPR006178
Allergen Fel d 1, chain 2 ( P30440 )
Fel d 1.png
Crystallographic structure of the Fel d 1 dimer, the primary allergen present in cat saliva [1]
Identifiers
SymbolFeld-I_B
Pfam PF09252
Pfam clan CL0370
InterPro IPR015332
SCOP2 1puo / SCOPe / SUPFAM
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

Fel d 1 is a secretoglobin protein complex 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] Circa 1971

Contents

Among cats, Fel d 1 is produced largely in their saliva and by the sebaceous glands located in their skin. It is the primary allergen present on cats and kittens. [1] [4] The function of the protein for cats is unknown, but it causes an IgG or IgE reaction in sensitive humans (either as an allergic or asthmatic response).

Variation in cats

Kittens produce less Fel d 1 than adult cats. Female cats produce a lower level of Fel d 1 than (unneutered) males, [5] while neutered males produce levels similar to those of females. Both intact and spayed females produce similar levels. Although females and neutered males produce Fel d 1 in lower levels, they still produce enough to cause allergic symptoms in sensitive individuals.

Researchers have been investigating reports from cat owners that certain breeds of cats either do not produce Fel d 1 or are thought to do so at significantly lower levels than other breeds. For instance, individual cats from the naturally occurring Siberian breed, native to the Siberian region for which the breed is named, have been shown to have genetic variants that result in a lower production of Fel d 1. [6] Another breed thought to have a possible genetic disposition not to produce this allergen or to produce less of it is the Balinese, an offshoot of the Siamese breed. [7] Several other breeds are widely referenced as causing a diminished immune reaction in cat allergy sufferers, including Sphynx, Russian Blue, Cornish Rex, Devon Rex, Siamese, Javanese, Oriental shorthair, Burmese, and Laperm.

Fairly reliable tests for their Fel d 1 protein production is available for individual cats, but research regarding entire breeds continues, hampered by the lack of a thoroughly accessible and accurate genetic test for production of the antigen.

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]

Presence in other species

Proteins matching the InterPro family signature for Fel d 1 parts is widespread among Theria, a subclass of mammals [8] amongst the Theriiformes (the sister taxon to Yinotheria.) Theria includes the eutherians that includes the placental mammals and the metatherians that includes the marsupials. More specifically, the InterPro profiles link the two components of Fel d 1 to the rodent androgen-binding protein (ABP; not to be confused with the human SHBG), a salivary pheromone. [9] [10]

A homolog of Fel d 1 protein is also present in the venom of the slow loris ( Primate: Nycticebus). Slow lorises are one of only a few venomous mammals and the only known venomous primate. They possess a dual-composite venom of saliva and brachial gland exudate (BGE). [11] The BGE possesses a protein resembling Fel d 1, which may affect host species as an allergen as a constituent of the venom. It possess a communicative function.

See also

Related Research Articles

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Hypoallergenic, meaning "below average" or "slightly" allergenic, is a term meaning that something causes fewer allergic reactions. The term was first used in 1953 in an advertising campaign for cosmetics or perhaps as early as 1940. A 2017 study of the top-selling skin moisturizers from Amazon, Target, and Walmart found 83% of those marketed as "hypoallergenic" contained at least one potentially allergenic chemical.

<span class="mw-page-title-main">Immunoglobulin E</span> Immunoglobulin E (IgE) Antibody

Immunoglobulin E (IgE) is a type of antibody that has been found only in mammals. IgE is synthesised by plasma cells. Monomers of IgE consist of two heavy chains and two light chains, with the ε chain containing four Ig-like constant domains (Cε1–Cε4). IgE is thought to be an important part of the immune response against infection by certain parasitic worms, including Schistosoma mansoni, Trichinella spiralis, and Fasciola hepatica. IgE is also utilized during immune defense against certain protozoan parasites such as Plasmodium falciparum. IgE may have evolved as a defense to protect against venoms.

<span class="mw-page-title-main">Siberian cat</span> Variety of cat

The Siberian is a centuries-old landrace of domestic cat in Russia, and recently developed as a formal breed with standards promulgated the world over since the late-1980s. Since 2006, the breed is recognised for registry and championship status with all major cat registries.

<span class="mw-page-title-main">Food allergy</span> Hypersensitivity reaction to a food

A food allergy is an abnormal immune response to food. The symptoms of the allergic reaction may range from mild to severe. They may include itchiness, swelling of the tongue, vomiting, diarrhea, hives, trouble breathing, or low blood pressure. This typically occurs within minutes to several hours of exposure. When the symptoms are severe, it is known as anaphylaxis. A food intolerance and food poisoning are separate conditions, not due to an immune response.

<span class="mw-page-title-main">Latex allergy</span> Medical condition

Latex allergy is a medical term encompassing a range of allergic reactions to the proteins present in natural rubber latex. It generally develops after repeated exposure to products containing natural rubber latex. When latex-containing medical devices or supplies come in contact with mucous membranes, the membranes may absorb latex proteins. In some susceptible people, the immune system produces antibodies that react immunologically with these antigenic proteins. Many items contain or are made from natural rubber, including shoe soles, pen grips, hot water bottles, elastic bands, rubber gloves, condoms, baby-bottle nipples, and balloons; consequently, there are many possible routes of exposure that may trigger a reaction. People with latex allergies may also have or develop allergic reactions to some fruits, such as bananas.

Apitoxin or bee venom is the venom produced by the honey bee. It is a cytotoxic and hemotoxic bitter colorless liquid containing proteins, which may produce local inflammation. It may have similarities to sea nettle toxin.

<span class="mw-page-title-main">Hypoallergenic dog breed</span> Type of dog

A hypoallergenic dog breed is a dog breed that is purportedly more compatible with allergic people than are other breeds. However, prominent allergen researchers have determined that there is no basis to the claims that certain breeds are hypoallergenic and, while allergen levels vary among individual dogs, the breed is not a significant factor.

<span class="mw-page-title-main">Venomous mammal</span> Venom-producing animals of the class Mammalia

Venomous mammals are animals of the class Mammalia that produce venom, which they use to kill or disable prey, to defend themselves from predators or conspecifics or in agonistic encounters. Mammalian venoms form a heterogeneous group with different compositions and modes of action, from three orders of mammals: Eulipotyphla, Monotremata, and Chiroptera. It has been proposed that some members of a fourth order, Primates, are venomous. To explain the rarity of venom delivery in Mammalia, Mark Dufton of the University of Strathclyde has suggested that modern mammalian predators do not need venom because they are able to kill quickly with their teeth or claws, whereas venom, no matter how sophisticated, requires time to disable prey.

Allergies to cats are one of the most common allergies among human individuals. Among the eight known cat allergens, the most prominent allergen is secretoglobin Fel d 1, which is produced in the anal glands, salivary glands, and, mainly, in sebaceous glands of cats, and is ubiquitous in the United States, even in households without cats. The second most common is Fel d 2, this type is triggered by the cats dead skin flakes (dander) that are floating in the air as well as in the smell of cat urine.

<span class="mw-page-title-main">Milk allergy</span> Type of food allergy caused by milk

Milk allergy is an adverse immune reaction to one or more proteins in cow's milk. Symptoms may take hours to days to manifest, with symptoms including atopic dermatitis, inflammation of the esophagus, enteropathy involving the small intestine and proctocolitis involving the rectum and colon. However, rapid anaphylaxis is possible, a potentially life-threatening condition that requires treatment with epinephrine, among other measures.

<span class="mw-page-title-main">Tree nut allergy</span> Medical condition

A tree nut allergy is a hypersensitivity to dietary substances from tree nuts and edible tree seeds causing an overreaction of the immune system which may lead to severe physical symptoms. Tree nuts include almonds, Brazil nuts, cashews, chestnuts, filberts/hazelnuts, macadamia nuts, pecans, pistachios, shea nuts and walnuts.

Secretoglobins (SCGBs) are a family of small, alpha-helical, disulfide linked, dimeric proteins found only in mammals. This family was formerly known as the Uteroglobin/Clara cell 10-kDa family, after the two aliases of its founding member Uteroglobin.

<span class="mw-page-title-main">Lipocalin</span>

The lipocalins are a family of proteins which transport small hydrophobic molecules such as steroids, bilins, retinoids, and lipids, and most lipocalins are also able to bind to complexed iron as well as heme. They share limited regions of sequence homology and a common tertiary structure architecture. This is an eight stranded antiparallel beta barrel with a repeated + 1 topology enclosing an internal ligand binding site.

<span class="mw-page-title-main">Major urinary proteins</span> Proteins found in the urine and other secretions of many animals

Major urinary proteins (Mups), also known as α2u-globulins, are a subfamily of proteins found in abundance in the urine and other secretions of many animals. Mups provide a small range of identifying information about the donor animal, when detected by the vomeronasal organ of the receiving animal. They belong to a larger family of proteins known as lipocalins. Mups are encoded by a cluster of genes, located adjacent to each other on a single stretch of DNA, that varies greatly in number between species: from at least 21 functional genes in mice to none in humans. Mup proteins form a characteristic glove shape, encompassing a ligand-binding pocket that accommodates specific small organic chemicals.

Laboratory animal allergy (LAA) is an occupational disease of laboratory animal technicians and scientists. It manifests as an allergic response to animal urine, specifically the major urinary proteins (Mups) of rodents, and can lead to the development of asthma. A study of 5641 workers in Japan who were exposed to laboratory animals found 23.1% had one or more allergic symptoms; globally the prevalence among at risk workers is estimated between 11 and 30% According to the National Institutes of Health, prevention of animal allergy depends on the control of allergens in the work environment. This involves a combination of measures to eliminate or control allergen exposure, including engineering controls, administrative controls, and personal protective equipment.

<span class="mw-page-title-main">Pro-hevein</span>

Pro-hevein is a wound-induced and a lectin-like protein from Hevea brasiliensis where it is involved in the coagulation of latex.

<span class="mw-page-title-main">Human interaction with cats</span>

Hundreds of millions of cats are kept as pets around the world.

The toxicology of fire ant venom is relatively well studied. The venom plays a central role in the biology of Red imported fire ants, such as in capturing prey, and in defending itself from competitors, assailants, and diseases. Some 14 million people are stung annually in the United States, suffering reactions that vary from mild discomfort, to pustule formation, swelling, and in rare cases, systemic reactions followed by anaphylactic shock. Fire ant venoms are mainly composed (>95%) of a complex mixture of insoluble alkaloids added to a watery solution of toxic proteins. For the Red imported fire ant Solenopsis invicta Buren there are currently 46 described proteins, of which four are well-characterised as potent allergens.

References

  1. 1 2 3 4 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". The Journal of Biological Chemistry. 278 (39): 37730–5. doi: 10.1074/jbc.M304740200 . PMID   12851385.
  2. 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". Proceedings of the National Academy of Sciences of the United States of America. 88 (21): 9690–4. Bibcode:1991PNAS...88.9690M. doi: 10.1073/pnas.88.21.9690 . PMC   52784 . PMID   1946388.
  3. 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.
  4. Dabrowski AJ, Van der Brempt X, Soler M, Seguret N, Lucciani P, Charpin D, Vervloet D (October 1990). "Cat skin as an important source of Fel d I allergen". The Journal of Allergy and Clinical Immunology. 86 (4 Pt 1): 462–5. doi: 10.1016/S0091-6749(05)80200-3 . PMID   2229808.
  5. Jalil-Colome J, de Andrade AD, Birnbaum J, Casanova D, Mège JL, Lanteaume A, Charpin D, Vervloet D (July 1996). "Sex difference in Fel d 1 allergen production". The Journal of Allergy and Clinical Immunology. 98 (1): 165–8. doi:10.1016/s0091-6749(96)70238-5. PMID   8765830.
  6. Sartore S, Landoni E, Maione S, Tarducci A, Borrelli A, Soglia D, et al. (December 2017). "Polymorphism Analysis of Ch1 and Ch2 Genes in the Siberian Cat". Veterinary Sciences. 4 (4): 63. doi: 10.3390/vetsci4040063 . PMC   5753643 . PMID   29194349.
  7. "Allergy to Cats - Cat DNA Test Kit | Basepaws". Allergy to Cats - Cat DNA Test Kit | Basepaws. Retrieved 2018-08-07.
  8. Myers, P.; R. Espinosa; C. S. Parr; T. Jones; G. S. Hammond & T. A. Dewey. "Subclass Theria". Animal Diversity Web.
  9. InterPro taxonomy view, IPR006178 and IPR015332
  10. Durairaj R, Pageat P, Bienboire-Frosini C (2018). "Another cat and mouse game: Deciphering the evolution of the SCGB superfamily and exploring the molecular similarity of major cat allergen Fel d 1 and mouse ABP using computational approaches". PLOS ONE. 13 (5): e0197618. Bibcode:2018PLoSO..1397618D. doi: 10.1371/journal.pone.0197618 . PMC   5957422 . PMID   29771985.
  11. Nekaris KA, Moore RS, Rode EJ, Fry BG (September 2013). "Mad, bad and dangerous to know: the biochemistry, ecology and evolution of slow loris venom". The Journal of Venomous Animals and Toxins Including Tropical Diseases. 19 (1): 21. doi: 10.1186/1678-9199-19-21 . PMC   3852360 . PMID   24074353.

Further reading

This article incorporates text from the public domain Pfam and InterPro: IPR015332