AI Article Synopsis
- Researchers have characterized the structures of mite profilins for the first time, specifically from the registered allergen Tyr p 36.0101 and Der p profilin, which are unique to arachnids.
- The study compares the thermal stability of mite and plant profilins, suggesting that more cysteine residues in mite profilins contribute to their greater stability.
- Despite structural similarities, mite profilins have low sequence identity with plant and human profilins, indicating minimal cross-reactivity with plant profilins, although they retain conserved sites for poly(l-proline) and actin binding.
Article Abstract
Structural and allergenic characterization of mite profilins has not been previously pursued to a similar extent as plant profilins. Here, we describe structures of profilins originating from (registered allergen Tyr p 36.0101) and (here termed Der p profilin), which are the first structures of profilins from Arachnida. Additionally, the thermal stabilities of mite and plant profilins are compared, suggesting that the high number of cysteine residues in mite profilins may play a role in their increased stability. We also examine the cross-reactivity of plant and mite profilins as well as investigate the relevance of these profilins in mite inhalant allergy. Despite their high structural similarity to other profilins, mite profilins have low sequence identity with plant and human profilins. Subsequently, these mite profilins most likely do not display cross-reactivity with plant profilins. At the same time the profilins have highly conserved poly(l-proline) and actin binding sites.
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| http://dx.doi.org/10.1515/hsz-2023-0366 | DOI Listing |
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