e101 rCan f 1 Dog

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• Latin name: Canis familiaris
• Family: Canidae
• Common names: Dog, Ag13
• Source material: An E. coli strain carrying a cloned cDNA encoding Canis familiaris allergen

Dog allergen components

Available ImmunoCAP®:

• e101 rCan f 1 »
• e102 rCan f 2 »
• e221 nCan f 3 »

Summary

The Dog is a relative of the Wolf, the Jackal, and the Fox, all belonging to the family Canidae. Two characteristics distinguish the Dog from other canids: its worldwide distribution in close association with humans, and its huge variety as a result of adaptation and breeding for specific purposes. Dogs through the centuries have acquired the body types and dispositions to pursue and retrieve game, and to be draught animals, guides (e.g., for the blind), guards, companions, and so on.

Dogs are found in almost every human environment. Some Dogs are feral, but not in such large numbers as Cats.

As with Cat, major Dog allergens can be found in hair, dander, pelt, saliva and serum, and are considered epithelial allergens; unlike with Cat, however, Dog urine and faeces do not have any significant allergenic activity (1-5). The concentration of allergens varies within breeds and among them (2,6). Although allergen differences occur according to the origin of the allergen (e.g., epithelium or saliva), no breed-specific allergens occur (7-8. This is contrary to reports of much earlier studies (9-10).

Dog allergens are ubiquitous in the environment. They may be found, for example, on automobile seats in concentrations well above the thresholds for both sensitisation and symptoms, regardless of the presence of a pet in the home (11). Dog allergens are also prevalent on walls, smooth floors, and finished furniture in homes with and without pets (12), as well as on furnishings and textiles in classrooms (13-14). The concentration of Dog (Can f 1) allergen may even be higher in dust collected in schools than in homes (15). High Dog allergen levels can be found in households without a pet if the former occupants had a pet or if Dogs often visit the building (16).

Upholstered chairs in hospitals constitute a significant reservoir of Cat and Dog allergens, and inhalation of airborne allergen by patients attending their hospital appointments may exacerbate asthma in those highly allergic to Cats or Dogs (17).

The association between pet exposure and asthma or allergic sensitisation can be very confusing, and many conflicting findings have been published (18). Recent studies can be used to support nearly any viewpoint on the issue: Dog exposure decreases (19-20) or has no effect (21) on the risk of sensitisation; asthma is negatively (21) or positively (22) associated with Dog exposure. What makes certainly impossible is that Dog (and Cat) allergen is ubiquitous in human society and may affect sensitisation in predisposed individuals regardless of pet ownership (18,23,24).

Nevertheless, Dog dander clearly represents an important source of inhalant allergens, and many studies report that Dog may frequently induce symptoms in sensitised individuals (1, 25-27). Symptoms include asthma, allergic rhinitis and allergic conjunctivitis. Thirty percent to 35% of atopic individuals display type I allergic symptoms on exposure to Cat and/or Dog allergens (28-30). Furthermore, occupational allergy to Dog allergens may occur in animal workers, animal pelt workers, and laboratory workers (31).

Early studies reported that over 28 Dog antigens were detected, 11 of which were found in Dog serum. IgE antibody in the sera of Dog-sensitive patients was reported to bind to 21 of these antigens to varying degrees (3-4).

The following allergens have been characterised:

• Can f 1, a lipocalin (2,32-34).
• Can f 2, a lipocalin (2,32,33) .
• Can f 3, Dog serum albumin (28,35).
• Can f 4 (36).

Two serum proteins, alpha-1-antitrypsin and IgG, have been identified as minor allergens (8).

Can f 1 was originally named Ag13 and was found to be identical to Ag8 (2). Can f 1 is a 22 - 25 kDa protein found in hair, dander and saliva but not serum, and is a lipocalin family member (32).

The amount of Dog allergens produced appears to have wide variability among Dog breeds. Hair length or hormonal status does not influence the production of Can f 1 (except that males produce more than females), whereas seborrhoea strongly influences the presence of Can f 1 on hair (2). Older animals produce more dander than younger ones, because their skin is drier. Also, epidermal turnover is more rapid in Dog breeds that are prone to the various forms of dry and oily seborrhoea. Instead of the normal 21-day cycle, the epidermal turnover time of seborrhoeic Dogs is 3 to 4 days.

Can f 2, a 19 kDa protein found in dander and saliva, previously known as Can d 2, is a lipocalin family member and has homology with Mouse urinary protein (MUP) (32, 37). In the majority of studies, it is shown to be a minor allergen.

Can f 3, Dog serum albumin, a 69 kDa protein, is found in dander, epithelia, saliva, and serum (35). It has also been found in salivary glands (parotid and submandibular) and liver (38). Dog albumin represents an important allergen for up to 35% of patients who are allergic to Dogs (28).

Can f 4 is an allergen found in Dog dander.

Shared IgE epitopes of the major Cat and Dog allergens may provide an explanation for the clinical observation that allergies to Cats and Dogs are frequently associated (39). However, several studies report that actual common allergens are responsible for the cross-reactivity, and that these allergens appear to be serum albumin and lipocalin. Furthermore, in a study of 36 cat-allergic patients, in 25% of Fel d 1-reactive patients, more than 50% inhibition of IgE reactivity to Dog allergens was achieved with recombinant Fel d 1. A Fel d 1 cross-reactive 20 kDa allergen was detected in dander extracts of several different Dog breeds, which may be responsible for double positivity to Cat and Dog in serology. However, the clinical relevance of this cross-sensitisation was not clinically evaluated (40).

Importantly, Dog-allergic individuals are sensitised to a heterogenous range of Dog allergens. For example, in a study of such individuals, 52% were shown to be sensitised to Can f 1, about 33% to Can f 2, 60% to an 18 kDa protein, 44% to a 40 kDa protein, and 48% to a 70 kDa protein (probably serum albumin, now known as Can f 3 (33).

Allergens from Canis familiaris listed by IUIS*

e101 rCan f 1

Recombinant non-glycosylated protein produced in an E. coli strain carrying a cloned cDNA encoding Canis familiaris allergen Can f 1

Common name: Ag 13
Biological function: Lipocalin
Mw: 21-25 kDa

Allergen description

rCan f 1 (32-33,41-43), originally designated Can d 1, is a lipocalin. Can f 1 is a major allergen and the most important Dog allergen, and Dog dander and saliva have a high content of it (but serum has none). The protein is produced in the canine Von Ebner’s glands, which are small salivary glands opening in the lingual epithelium. This protein ranges in size from 21 kDa to 25 kDa (44-45). Can f 1 has demonstrated greater heat resistance than Mite allergens after 60 minutes at 140 °C (16). The protein is also relatively stable in house dust (26).

Major respiratory allergens of Dogs, Mice, Rats, Horses and Cows belong to the lipocalin group of proteins. The amino acid sequence identity among lipocalins is often less than 20%, but they contain between 1 and 3 structurally conserved regions, and their 3-dimensional structures are similar. Lipocalins share certain biological functions, predominantly related to the transport of small hydrophobic molecules such as vitamins and pheromones. Immune reactivity to lipocalin allergens is not well understood. In Bos d 5, the IgE-binding epitopes are spread along the molecule, whereas in Bos d 2, the C terminus appears to contain the human B cell epitopes. Bos d 5 contains several murine T cell epitopes. To explain these observations, it has been proposed that the allergenicity of lipocalins may be a consequence of molecular mimicry between lipocalin allergens and endogenous lipocalins at the T cell level (45).

Can d 1 and Can d 2 are found in sera of approximately 74% of Dog-allergic individuals (38). More than 90% of Dog-allergic patients have been shown to have specific IgE antibodies directed to Can f 1 alone (2, 32, 46-47). In another study, sera from 96% of patients with Dog allergy demonstrated allergen-specific IgE to Can f 1 and Can f 2. Can f 1 was preferentially detected in dander and saliva, but not in skin, salivary gland, serum and liver extracts. Can f 2 was strongly expressed in skin, but not in dander, serum and liver (1,25). However, not all studies have found a high prevalence of IgE reactivity in Dog-allergic patients; one study reported that, according to ELISA determination, 52% of Dog-allergic patients recognised recombinant Can f 1 (33). The authors postulated that this may have been due to their selection of patients, but whether certain populations are less frequently sensitised to Can f 1 has not been determined.

Recombinant Can f 1 and Can f 2 are immunologically concordant with natural Can f 1 in skin prick test and IgE antibody analysis. The concordance is slightly lower with recombinant Can f 2. Fifty-two percent of Dog-allergic patients reacted against
Can f 1, and about a third of the patients reacted to Can f 2 (33).

As the amount of important allergens in commercial Dog extracts can vary extensively, and as natural preparations may be contaminated with Mite allergens, potentially causing false-positive skin test results, recombinant Can f 1 and recombinant Can f 2 have a role to play in assessing allergy to Dog (48).

Can f 1 and 2 are two important and useful tools identified so far, but further components are needed for diagnosing Dog allergy (33).

e102 rCan f 2

Recombinant non-glycosylated protein produced in an E. coli strain carrying a cloned cDNA encoding Canis familiaris allergen Can f 2

Biological function: Lipocalin
Mw: 19 kDa or 27 kDa

Allergen description

Can f 2 (32-33,42-43), previously known as Can d 2, is a protein with a molecular weight of 19 kDa (38) or 27 kDa (4). It is a lipocalin and has homology with Mouse urinary protein (MUP) (2). It was found to react with IgE antibodies of 66% of Dog-allergic patients, and to bind 23% of the IgE antibodies directed against Dog dander extract, both of which findings confirm its role as a minor allergen (2). Can f 1 and Can f 2 share epitopes (44).

A study evaluated the recombinant Dog allergens Can f 1 and Can f 2 in clinically diagnosed Dog-allergic patients’ and healthy non-atopic Dog owners. These allergens were compared to commercial Dog epithelial extract, and it was found that patients’ IgE reactivity to natural Can f 1 and to the recombinant allergen were perfectly concordant, but the concordance was slightly lower with recombinant Can f 2. About one-third of the patients reacted to Can f 2. The study concluded that the recombinant allergens can be used reliably to identify Can f 1 and Can f 2-sensitised individuals, but that on their own the 2 allergens were insufficient as reagents for diagnosing Dog allergy (33).

e221 nCan f 3

Native serum albumin purified from Dog (Canis familiaris)

Common name: DSA
Biological function: Serum albumin
Mw: 69-70 kDa

Allergen description

Can f 3 (3,8,10,28,35-36,48-52), also known as Dog Serum Albumin (DSA), is a protein with a molecular weight of 69-70 kDa. It is a serum albumin. It is found in Dog serum, saliva, dander, hair and epithelia, and it is also synthesised in the Dog salivary gland and Dog liver (35). Dog serum albumin has been reported to be particularly abundant allergen in Dog epithelia extracts (50). Dog and Cat serum albumins are also very common allergens present in house dust (38). A recombinant Can f 3 has been produced (35).

Sensitisation to Dog serum albumin has been previously documented as varying from around 35-48% although early studies reported even lower frequencies (5,28,33,53). The importance and frequency of sensitisation to DSA also varies among different populations (3).

In a study, 51 patients with a clinical history of Dog allergy were evaluated for skin reactivity for 8 individual standardised Dog breed allergen preparations, and for 1 mixed-breed allergen preparation, Dog serum albumin, and histamine hydrochloride. The sensitivity rate shown by skin prick test was 67% to 88% for the various Dog breed allergen preparations, but only 18% for DSA (10).

The deduced amino acid sequence of DSA was shown to be highly homologous to the sequences of albumins from both other animals and humans, which explained the perceived extensive cross-reactivity among albumins, and was corroborated by the demonstration of the presence of similar epitopes on Dog, Cat, and human albumin (35). In immunoblot inhibition studies and histamine release tests, it was demonstrated that patients who react to Dog albumin exhibit IgE reactivity with purified albumins from Cat, Mouse, Chicken, and Rat. The deduced amino acid sequence of DSA was found to have significant sequence homology with albumins from human (82.6%), Pig (81.8%), Beef (77.3%), Sheep (78.8%), Mouse (75.8%), and Rat (76.2%) (28).

Cross-reactivity between DSA and albumins from other animals was demonstrated in other studies. In a study aimed at assessing the importance of albumin as a cross-reactive allergen in patients sensitised to Cat, Dog and Horse, 117 patients sensitised to Cat were tested for the presence of skin reactivity allergen specific IgE. Twenty-two percent of patients were found to have IgE antibodies to Cat albumin, and 41% of these patients were also sensitised to Dog and Horse. Of this group, 21% had IgE to all 3 albumins and 17% to 2. However, inhibition studies demonstrated variable degrees of inhibition, suggesting that albumins from these 3 animals share some epitopes that account for the cross-reactivity observed in around a third of patients sensitised to Cat, Dog and Horse, but that more than 50% of allergen-specific IgE that cross-reacts among these 3 animals is directed to allergens other than albumin (54).

Similarly, in a study evaluating the degree and significance of IgE-cross-reactivity to various albumins in 200 patients allergic to animals, it was found that approximately 30% of those allergic to animal hair/dander extracts reacted to albumins from various animals. Although a high degree of sequence homology existed among different animal albumins, a remarkable variability of IgE cross-reactivity was observed, indicating that some patients were sensitised preferentially against certain albumins. Most of the patients allergic to albumins reacted to Dog, Cat, and Horse albumin, which also bound a high percentage of albumin-specific IgE. Recombinant dog albumin fragment, representing 265 amino acids of the mature protein, bound IgE from all 15 patients allergic to albumin tested (55).

An association between allergy to epithelia and allergy to mammalian meat has also been reported, and most authors ascribed this to serum albumin as the responsible cross-reacting allergen. For example, a 28-year-old asthmatic male cook sensitised to Dog epithelium who developed wheezing and contact urticaria when handling raw Beef in an occupational setting was reported. Skin reactivity was found to raw and cooked Beef and raw Lamb, and to Cat and Dog. Dog-specific IgE was positive. The secondary cross-reactivity was attributed to Bovine Serum Albumin (BSA) (56).

Furthermore, patients with persistent Milk allergy and IgE antibodies to BSA were reported to be at greater risk of rhinoconjunctivitis and asthma because of cross-reactivity with serum albumin present in animal dander. In a study evaluating the cross-reactivity among serum albumin of various mammals in milk, meat, and epithelia, sera from all but 1 patient recognised serum albumin in Cow’s milk, in meat from Beef, Lamb, Deer, and Pork, and in epithelia from Dog, Cat, and Cow. Some patients were sensitised only to serum albumin in meat and epithelia. Patients allergic only to dander recognised other proteins in epithelia but not serum albumin. The authors concluded that serum albumin is an important allergen in Cow’s milk, meat, and epithelia allergy. The authors proposed that sensitisation first occurs with contact with serum albumin in Cow’s milk and that patients develop sensitisation to serum albumin present on animal epithelia even without direct contact with animals. The authors cautioned that patients with both BSA and Cow’s milk allergy must avoid raw meats and furry pets (57).

Although studies have demonstrated a high degree of homology among serum albumins from various mammals, epitope diversity results in different clinical expressions of cross-reactivity. This is particularly well described in Pork-Cat cross-reactivity, where cross-reactivity has been demonstrated between Pork meat and Cat epithelia as a result of serum albumin, but not to Dog (58-59).

Dog serum albumin may be used for diagnostic purposes to identify patients who are cross-sensitised to many animal species, and perhaps may be used for specific immunotherapy of sensitised individuals (35).

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• References