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Int. J. Mol. Sci. 2017, 18(6), 1204;

Proteases of Dermatophagoides pteronyssinus

Integrative Bioinformatics Support Group, National Institute of Environmental Health Sciences, Research Triangle Park, NC 27709, USA
Genome Integrity and Structural Biology Laboratory, National Institute of Environmental Health Sciences, 111 T.W. Alexander Dr., Research Triangle Park, NC 27709, USA
Chemistry Department, Duke Univeristy, Durham, NC, 27708, USA
Author to whom correspondence should be addressed.
Academic Editors: Fatima Ferreira and Hans Brandstetter
Received: 25 April 2017 / Revised: 22 May 2017 / Accepted: 25 May 2017 / Published: 6 June 2017
(This article belongs to the Special Issue Proteolysis in Allergic Sensitization and Th2 Response)
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Since the discovery that Der p 1 is a cysteine protease, the role of proteolytic activity in allergic sensitization has been explored. There are many allergens with proteolytic activity; however, exposure from dust mites is not limited to allergens. In this paper, genomic, transcriptomic and proteomic data on Dermatophagoides pteronyssinus (DP) was mined for information regarding the complete degradome of this house dust mite. D. pteronyssinus has more proteases than the closely related Acari, Dermatophagoides farinae (DF) and Sarcoptes scabiei (SS). The group of proteases in D. pteronyssinus is found to be more highly transcribed than the norm for this species. The distribution of protease types is dominated by the cysteine proteases like Der p 1 that account for about half of protease transcription by abundance, and Der p 1 in particular accounts for 22% of the total protease transcripts. In an analysis of protease stability, the group of allergens (Der p 1, Der p 3, Der p 6, and Der p 9) is found to be more stable than the mean. It is also statistically demonstrated that the protease allergens are simultaneously more highly expressed and more stable than the group of D. pteronyssinus proteases being examined, consistent with common assumptions about allergens in general. There are several significant non-allergen outliers from the normal group of proteases with high expression and high stability that should be examined for IgE binding. This paper compiles the first holistic picture of the D. pteronyssinus degradome to which humans may be exposed. View Full-Text
Keywords: allergens; proteases; allergen source-derived proteases; allergic sensitization; exposure allergens; proteases; allergen source-derived proteases; allergic sensitization; exposure

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Randall, T.A.; London, R.E.; Fitzgerald, M.C.; Mueller, G.A. Proteases of Dermatophagoides pteronyssinus. Int. J. Mol. Sci. 2017, 18, 1204.

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