Pear allergens encompass a group of proteins found in pears that have the potential to induce allergic reactions. Among the notable allergen proteins are Pyr c 1, Pyr c 3, Pyr c 4, and Pyr c 5. These proteins primarily belong to the molecular family of pathogenesis-related (PR) proteins. The structural characteristics and classification of each play a crucial role in understanding their allergenic properties.
Pyr c 1, a major pear allergen in the PR-10 family, possesses a compact, globular structure, with its three-dimensional arrangement of amino acids enhancing its allergenicity. Its classification as a PR-10 protein signifies its role in plant defense mechanisms, making it a key contributor to pear-induced allergies. Pyr c 3, another prominent pear allergen, belongs to the Bet v 1-related proteins, sharing structural similarities with the major birch pollen allergen, Bet v 1. The molecular structure of Pyr c 3 contributes to its allergenic potential, leading to cross-reactivity with other allergens, particularly those found in tree pollens.
Pyr c 4, classified as a lipid transfer protein (LTP), plays a significant role in pear-induced allergies. LTPs, known for their stability and resistance to heat and digestive enzymes, enhance their allergenicity. Pyr c 4's structural features contribute to its stability, making it a key target for allergic reactions upon pear consumption. Pyr c 5, categorized as an nsLTP (non-specific lipid transfer protein), is involved in lipid binding and transport. Its molecular structure and role in lipid interactions contribute to its allergenic potential, providing insights into the mechanisms behind pear allergies.
| Cat.No. | Product Name | Species | Source | Tag |
| ra-3796P | Recombinant Pyr c 1 | Pyrus communis (Pear) | E.coli or Yeast | His |
| ra-3797P | Recombinant Pyr c 3 | Pyrus communis (Pear) | E.coli or Yeast | His |
| ra-3798P | Recombinant Pyr c 4 | Pyrus communis (Pear) | E.coli or Yeast | His |
| ra-3799P | Recombinant Pyr c 5 | Pyrus communis (Pear) | E.coli or Yeast | His |
The biological functions of pear allergen proteins delve into their role in the plant's defense system and the subsequent allergic responses they induce in humans. Pyr c 1, Pyr c 3, Pyr c 4, and Pyr c 5 collectively contribute to the allergenicity of pears.
Pyr c 1, Pyr c 3, Pyr c 4, and Pyr c 5 play a crucial role in pear allergies, eliciting immune responses in susceptible individuals. The molecular mechanisms underlying these allergies involve the recognition of these allergen proteins by the immune system. This recognition triggers the production of specific antibodies, leading to allergic symptoms ranging from mild itching to severe anaphylaxis.
Cross-reactivity is a notable phenomenon, especially with Pyr c 3, which shares similarities with birch pollen allergens. This cross-reactivity expands the spectrum of potential allergens for individuals, complicating the diagnosis and management of pear allergies.
