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

Rajesh, Durairaj; Pageat, Patrick; Bienboire-Frosini, Cécile

doi:10.1371/journal.pone.0197618

Cited by 18 publications

(31 citation statements)

References 75 publications

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“…It is spread throughout the cat's hair during grooming and shed into the environment with hair and dander . Fel d 1's biological function for the cat is as yet unknown, but a pheromone/chemical signaling role has been proposed …”

Section: Fel D1 the Major Cat Allergenmentioning

confidence: 99%

“…Fel d 1 is a four‐subunit (tetrameric) protein composed of two covalently linked heterodimers, each of which contains two distinct chains (Chain 1, a polypeptide, and Chain 2, a glycopeptide with N‐linked oligosaccharides) that are encoded by separate genes and linked with disulfide bridges . (Figure ) Despite variation in Fel d 1 due to differential gene expression for the two chains, core fragments are preserved and the structural variation in Fel d 1 has a low impact on its allergenicity …”

Section: Neutralizing Fel D 1 At Its Sourcementioning

confidence: 99%

“…2,17 Fel d 1's biological function for the cat is as yet unknown, but a pheromone/chemical signaling role has been proposed. 2,5,22,24 Fel d 1 easily becomes and remains airborne in dander and dust particles; up to 60% of Fel d 1 is carried by particles <5 microns in diameter. 2 9 It is passively transferred on clothing 2,5,19 ; as a result, the allergen is ubiquitous and has been documented in homes without cats, private vehicles, and public transportation and buildings at levels (≥8 µg Fel d 1 per gram of dust) that exceed threshold value associated with sensitization.…”

Section: Fel D1 the Ma Jor C At Allerg Enmentioning

confidence: 99%

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Keep the cat, change the care pathway: A transformational approach to managing Fel d 1, the major cat allergen

Satyaraj¹,

Wedner

Bousquet

2019

Allergy

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Background Allergies to cats are the most common animal‐origin allergy, and affect approximately 1 in 5 adults worldwide. The prevalence of allergy to furry animals has been increasing, and allergy to cats is a major risk factor for the development of asthma and rhinitis. The diagnosis of cat allergy is now well established. The exact significance of component‐resolved diagnosis in the diagnosis of cat allergy remains to be fully understood. Allergen avoidance is effective but often has a psychologic impact. Allergen immunotherapy is not well demonstrated. There is a need for innovative approaches to better manage cat allergens. Next‐generation care pathways for asthma and rhinitis will define the place of cat allergen avoidance. Methods and Results This manuscript, based on content presented at the European Academy of Allergy and Clinical Immunology Congress 2019, provides information on the prevalence and impact of cat allergies and the molecular biology of Fel d 1, the major cat allergen. Discussion The authors present the scientific basis of a novel care pathway that utilizes anti‐Fel d 1 IgY antibodies to safely and effectively neutralize Fel d 1 after its production by the cat but before human exposure. Conclusion Efficacy of a feline diet with an egg product ingredient containing anti‐Fel d 1 IgY antibodies was demonstrated in vitro, ex vivo, and in vivo, and further validated by a pilot exposure study involving cat‐allergic human participants.

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Section: Fel D1 the Major Cat Allergenmentioning

confidence: 99%

Section: Neutralizing Fel D 1 At Its Sourcementioning

confidence: 99%

Section: Fel D1 the Ma Jor C At Allerg Enmentioning

confidence: 99%

See 1 more Smart Citation

Keep the cat, change the care pathway: A transformational approach to managing Fel d 1, the major cat allergen

Satyaraj¹,

Wedner

Bousquet

2019

Allergy

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“…Binding of some steroids to members of the secretoglobin family was previously reported, involving interactions with their central hydrophobic cavity [19,23,26]. In particular, a recent paper extensively describes the evolutionary divergence, functional sites, and surface structural resemblance between Fel d 1 and ABP, suggesting that the first protein could be involved in semiochemical transport/processing in intra-species communication [25]. However, so far, no experimental evidence has been provided on the capability of Fel d 1 to bind semiochemicals.…”

Section: Introductionmentioning

confidence: 97%

“…From a structural perspective, Fel d 1 also displays interesting features regarding ligand binding capabilities due to the presence of two internal cavities [23]. Structural similarities between Fel d 1 and another secretoglobin involved in mice mate selection and communication, the mouse salivary androgen-binding protein (ABP) [18], have been previously described [24,25]. Binding of some steroids to members of the secretoglobin family was previously reported, involving interactions with their central hydrophobic cavity [19,23,26].…”

Section: Introductionmentioning

confidence: 98%

The Major Cat Allergen Fel d 1 Binds Steroid and Fatty Acid Semiochemicals: A Combined In Silico and In Vitro Study

Bienboire-Frosini

Rajesh

Pelosi

et al. 2020

IJMS

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The major cat allergen Fel d 1 is a tetrameric glycoprotein of the secretoglobin superfamily. Structural aspects and allergenic properties of this protein have been investigated, but its physiological function remains unclear. Fel d 1 is assumed to bind lipids and steroids like the mouse androgen-binding protein, which is involved in chemical communication, either as a semiochemical carrier or a semiochemical itself. This study focused on the binding activity of a recombinant model of Fel d 1 (rFel d 1) towards semiochemical analogs, i.e., fatty acids and steroids, using both in silico calculations and fluorescence measurements. In silico analyses were first adopted to model the interactions of potential ligands, which were then tested in binding assays using the fluorescent reporter N-phenyl-1-naphthylamine. Good ligands were fatty acids, such as the lauric, oleic, linoleic, and myristic fatty acids, as well as steroids like androstenone, pregnenolone, and progesterone, that were predicted by in silico molecular models to bind into the central and surface cavities of rFel d 1, respectively. The lowest dissociation constants were shown by lauric acid (2.6 µM) and androstenone (2.4 µM). The specific affinity of rFel d 1 to semiochemicals supports a function of the protein in cat’s chemical communication, and highlights a putative role of secretoglobins in protein semiochemistry.

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Chemical Synthesis of Secretoglobin 3A2 Covalent Homodimer and Photocaged Monomeric Variants

Gazzi,

Heinke,

Landolt

et al. 2024

Angewandte Chemie

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Secretoglobin (SCGB) 3A2 belongs to an intriguing family of small, secreted proteins present only in mammals. Although members of the SCGB protein family have distinct amino‐acid sequences, they share structural similarities. Of particularly interest is the not yet fully understood self‐assembly ability of SCGBs, which arise from covalent disulfide dimerization and non‐covalent oligomerization. Recently, SCGB3A2 has attracted attention for its singular expression profile in airways. However, the knowledge on SCGB3A2 (patho)physiology derives exclusively from in‐vivo and complex ex‐vivo mixtures, which hampers characterization of the mechanisms driving SCGB3A2 structural behavior. In this report, we document the chemical synthesis of SCGB3A2 in multi‐milligram quantities. Key to access both monomeric and homo‐dimeric SCGB3A2 analogues was the use of KAHA ligation and enabled masking of the cysteine residue. The synthetic proteins were used to investigate SCGB3A2 self‐assembly profile, confirming their high propensity to dimerization even in the absence of the key Cys residue.

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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

Cited by 18 publications

References 75 publications

Keep the cat, change the care pathway: A transformational approach to managing Fel d 1, the major cat allergen

Keep the cat, change the care pathway: A transformational approach to managing Fel d 1, the major cat allergen

The Major Cat Allergen Fel d 1 Binds Steroid and Fatty Acid Semiochemicals: A Combined In Silico and In Vitro Study

Chemical Synthesis of Secretoglobin 3A2 Covalent Homodimer and Photocaged Monomeric Variants

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