Hello, kitty: could cat allergy be a form of intoxication?

Insights into Platypus Crural Gland Transcriptomics – Venom and Beyond

“…The inclusion of three putative toxins in this protein family suggests secretoglobins may be an important component of the platypus crural system that requires further investigation. The function of all toxic secretoglobins in vertebrates is unknown (86-88), including the role of the brachial gland exudate secretion protein (BGEsp) that is a major component in loris venom (114,115). Secretoglobins are dimeric proteins secreted within epithelial cells, glandular tissues and secretions such as sputum, with important roles in immunoregulation, anti-in ammation, tissue repair and tumourigenesis (116,117).…”

Insights into Platypus Crural Gland Transcriptomics – Venom and Beyond

“…The inclusion of three putative toxins in this protein family suggests secretoglobins may be an important component of the platypus crural system that requires further investigation. The function of all toxic secretoglobins in vertebrates is unknown (86-88), including the role of the brachial gland exudate secretion protein (BGEsp) that is a major component in loris venom (114,115). Secretoglobins are dimeric proteins secreted within epithelial cells, glandular tissues and secretions such as sputum, with important roles in immunoregulation, anti-in ammation, tissue repair and tumourigenesis (116,117).…”

A narrative review on allergy and exposure to domestic and non-domestic animals: favorable and unfavorable effects

“…Interestingly, it has been shown homology between this brachial gland protein and the main allergen of cat dander (52). Laboratory data demonstrate that Fel d 1 may satisfy some criteria to be considered a toxin and thus suggesting the possibility that cat-induced reactions could also include a form of toxic reaction (53). A similar model is provided by hymenoptera stings, possibly leading to allergic or non-allergic (e.g.…”

Slowly Making Sense: A Review of the Two-Step Venom System within Slow (Nycticebus spp.) and Pygmy Lorises (Xanthonycticebus spp.)

“…As of 2023, only one component of the brachial gland exudate has been identified in detail from a single species of slow loris ( N. javanicus )—the BGE secretion protein (BGEsp, Figure 3 ) [ 64 , 84 , 85 ]. The BGEsp is a 17.6 kDa homodimer formed of two heterodimer chains that are linked together by three disulfide bridges each.…”

“…The reason for secretoglobins resulting in so many allergies is proposed to be because they mimic lipocalins, which are an important part of the immune system [ 90 ]. Where this becomes even more striking is the structural and functional homology of BGEsp compared to Fel-d-1, the most common secretory protein produced by domestic cats ( Felis catus ) and the reason for most cat allergies within humans [ 64 , 84 , 85 , 91 ]. Indeed, we put Chain A and Chain B from [ 64 ] through BLASTP [ 92 ] to determine which sequences are homologous ( Supplementary File S1 ).…”

“…Chain A specifically displayed greater homology to all Felidae, while Chain B displayed high homology levels only with Fel-d-1 from domestic cats. This convergent evolution is highly unusual between the slow lorises and Felidae, as it brings into question a tentative link between venom and allergies [ 85 ]. The purpose of Fel-d-1 within cats is still not currently understood, but it is considered important in chemical communication between cats [ 93 ].…”

Insights into Platypus Crural Gland Transcriptomics – Venom and Beyond

“…The inclusion of three putative toxins in this protein family suggests secretoglobins may be an important component of the platypus crural system that requires further investigation. The function of all toxic secretoglobins in vertebrates is unknown (86-88), including the role of the brachial gland exudate secretion protein (BGEsp) that is a major component in loris venom (114,115). Secretoglobins are dimeric proteins secreted within epithelial cells, glandular tissues and secretions such as sputum, with important roles in immunoregulation, anti-in ammation, tissue repair and tumourigenesis (116,117).…”

A narrative review on allergy and exposure to domestic and non-domestic animals: favorable and unfavorable effects

“…Interestingly, it has been shown homology between this brachial gland protein and the main allergen of cat dander (52). Laboratory data demonstrate that Fel d 1 may satisfy some criteria to be considered a toxin and thus suggesting the possibility that cat-induced reactions could also include a form of toxic reaction (53). A similar model is provided by hymenoptera stings, possibly leading to allergic or non-allergic (e.g.…”

Slowly Making Sense: A Review of the Two-Step Venom System within Slow (Nycticebus spp.) and Pygmy Lorises (Xanthonycticebus spp.)

“…As of 2023, only one component of the brachial gland exudate has been identified in detail from a single species of slow loris ( N. javanicus )—the BGE secretion protein (BGEsp, Figure 3 ) [ 64 , 84 , 85 ]. The BGEsp is a 17.6 kDa homodimer formed of two heterodimer chains that are linked together by three disulfide bridges each.…”

“…The reason for secretoglobins resulting in so many allergies is proposed to be because they mimic lipocalins, which are an important part of the immune system [ 90 ]. Where this becomes even more striking is the structural and functional homology of BGEsp compared to Fel-d-1, the most common secretory protein produced by domestic cats ( Felis catus ) and the reason for most cat allergies within humans [ 64 , 84 , 85 , 91 ]. Indeed, we put Chain A and Chain B from [ 64 ] through BLASTP [ 92 ] to determine which sequences are homologous ( Supplementary File S1 ).…”

“…Chain A specifically displayed greater homology to all Felidae, while Chain B displayed high homology levels only with Fel-d-1 from domestic cats. This convergent evolution is highly unusual between the slow lorises and Felidae, as it brings into question a tentative link between venom and allergies [ 85 ]. The purpose of Fel-d-1 within cats is still not currently understood, but it is considered important in chemical communication between cats [ 93 ].…”

Insights into Platypus Crural Gland Transcriptomics – Venom and Beyond

“…The inclusion of three putative toxins in this protein family suggests secretoglobins may be an important component of the platypus crural system that requires further investigation. The function of all toxic secretoglobins in vertebrates is unknown (86-88), including the role of the brachial gland exudate secretion protein (BGEsp) that is a major component in loris venom (114,115). Secretoglobins are dimeric proteins secreted within epithelial cells, glandular tissues and secretions such as sputum, with important roles in immunoregulation, anti-in ammation, tissue repair and tumourigenesis (116,117).…”

A narrative review on allergy and exposure to domestic and non-domestic animals: favorable and unfavorable effects

“…Interestingly, it has been shown homology between this brachial gland protein and the main allergen of cat dander (52). Laboratory data demonstrate that Fel d 1 may satisfy some criteria to be considered a toxin and thus suggesting the possibility that cat-induced reactions could also include a form of toxic reaction (53). A similar model is provided by hymenoptera stings, possibly leading to allergic or non-allergic (e.g.…”

Slowly Making Sense: A Review of the Two-Step Venom System within Slow (Nycticebus spp.) and Pygmy Lorises (Xanthonycticebus spp.)

“…As of 2023, only one component of the brachial gland exudate has been identified in detail from a single species of slow loris ( N. javanicus )—the BGE secretion protein (BGEsp, Figure 3 ) [ 64 , 84 , 85 ]. The BGEsp is a 17.6 kDa homodimer formed of two heterodimer chains that are linked together by three disulfide bridges each.…”

“…The reason for secretoglobins resulting in so many allergies is proposed to be because they mimic lipocalins, which are an important part of the immune system [ 90 ]. Where this becomes even more striking is the structural and functional homology of BGEsp compared to Fel-d-1, the most common secretory protein produced by domestic cats ( Felis catus ) and the reason for most cat allergies within humans [ 64 , 84 , 85 , 91 ]. Indeed, we put Chain A and Chain B from [ 64 ] through BLASTP [ 92 ] to determine which sequences are homologous ( Supplementary File S1 ).…”

“…Chain A specifically displayed greater homology to all Felidae, while Chain B displayed high homology levels only with Fel-d-1 from domestic cats. This convergent evolution is highly unusual between the slow lorises and Felidae, as it brings into question a tentative link between venom and allergies [ 85 ]. The purpose of Fel-d-1 within cats is still not currently understood, but it is considered important in chemical communication between cats [ 93 ].…”