The family of thaumatin-like proteins (TLPs), also designated pathogenesis-related proteins PR-5, comprises proteins with diverse functions. Most family members were found in plants, but TLPs were also identified in fungi, C. elegans, mites, and insects [1]. Their synthesis in plants is induced in response to biotic or abiotic stress, but is also developmentally regulated particularly in fruits during ripening [2]. The majority of TLPs has a molecular mass of about 20 kDa, mainly consists of anti-parallel β-sheets and is stabilized by eight disulfide bonds [3]. There are acidic, basic and neutral TLPs. The basic TLPs tend to be in vacuoles or other vesicles, while the acidic forms are more likely secreted into the extracellular spaces. TLPs are stable at low pH and resistant to heat treatment and proteolytic degradation [4].
TLPs have been characterized as minor allergens in several fruits such as apple (Mal d 2), cherry (Pru av 2), bell paper (Cup a 1), kiwifruit (Act d 2), orange, and grape as well as in pollen of tress from the family Cupressaceae such as mountain cedar (Jun a 3), and cypress (Cup a 3) [5]. Fruit TLPs retain their IgE binding ability after heating and gastrointestinal digestion [4].
Family-defining Pfam domains (at least one of these domains is present in each family member):
| Pfam domain | Pfam clan | ||
| PF00314 | Thaumatin family | - | |
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