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屋尘螨蛋白酶

Proteases of Dermatophagoides pteronyssinus.

作者信息

Randall Thomas A, London Robert E, Fitzgerald Michael C, Mueller Geoffrey A

机构信息

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.

出版信息

Int J Mol Sci. 2017 Jun 6;18(6):1204. doi: 10.3390/ijms18061204.

DOI:10.3390/ijms18061204
PMID:28587273
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5486027/
Abstract

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 (DP) was mined for information regarding the complete degradome of this house dust mite. has more proteases than the closely related Acari, (DF) and (SS). The group of proteases in 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 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 degradome to which humans may be exposed.

摘要

自从发现Der p 1是一种半胱氨酸蛋白酶以来,人们就开始探索蛋白水解活性在过敏性致敏中的作用。有许多具有蛋白水解活性的过敏原;然而,来自尘螨的暴露并不局限于过敏原。在本文中,挖掘了关于(DP)的基因组、转录组和蛋白质组数据,以获取有关这种屋尘螨完整降解组的信息。(DP)比密切相关的螨类(DF)和(SS)拥有更多的蛋白酶。发现(DP)中的蛋白酶组转录水平比该物种的正常水平更高。蛋白酶类型的分布以半胱氨酸蛋白酶为主,如Der p 1,其转录丰度约占蛋白酶转录的一半,特别是Der p 1占总蛋白酶转录本的22%。在蛋白酶稳定性分析中,发现一组过敏原(Der p 1、Der p 3、Der p 6和Der p 9)比平均值更稳定。统计结果还表明,蛋白酶过敏原同时比所检测的(DP)蛋白酶组表达水平更高且更稳定,这与关于过敏原的一般常见假设一致。在正常蛋白酶组中有几个高表达和高稳定性的显著非过敏原异常值,应检测它们与IgE的结合情况。本文汇编了人类可能接触到的(DP)降解组的首张整体图谱。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/31c2/5486027/3eb7fd35745b/ijms-18-01204-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/31c2/5486027/fcd224ff6029/ijms-18-01204-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/31c2/5486027/f09c4767ce15/ijms-18-01204-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/31c2/5486027/f1c456701a0a/ijms-18-01204-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/31c2/5486027/c8afe509f4d8/ijms-18-01204-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/31c2/5486027/3eb7fd35745b/ijms-18-01204-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/31c2/5486027/fcd224ff6029/ijms-18-01204-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/31c2/5486027/f09c4767ce15/ijms-18-01204-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/31c2/5486027/f1c456701a0a/ijms-18-01204-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/31c2/5486027/c8afe509f4d8/ijms-18-01204-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/31c2/5486027/3eb7fd35745b/ijms-18-01204-g005.jpg

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