The molecular basis of allergenicity

免疫学 生物 抗原 免疫系统 免疫球蛋白E 过敏 先天免疫系统 过敏原 蛋白酶 糖基化 获得性免疫系统 抗体 遗传学 酶 生物化学
作者
Farouk Shakib,Amir M. Ghaemmaghami,Herb F. Sewell
出处
期刊:Trends in Immunology [Elsevier BV]
卷期号:29 (12): 633-642 被引量:125
标识
DOI:10.1016/j.it.2008.08.007
摘要

Allergens are mostly innocuous antigens that elicit powerful T helper cell type 2 (Th2) responses leading to hyper-immunoglobulin E (IgE) production and allergy. Research carried out over several years has highlighted the possible role of the inherent protease activity, surface features and glycosylation patterns of allergens in the engagement of a Th2 signalling pathway. It is thought that allergens possess common features and patterns that enable them to be recognized by innate immune defences as Th2-inducing antigens. These events are further amplified by proteolytically active allergens through digestion of cell surface molecules involved in regulating innate and adaptive immune functions, favouring Th2 responses. A greater understanding of the molecular features that make proteins allergenic will help define new therapeutic targets aimed at blocking allergen recognition and protease activity. Allergens are mostly innocuous antigens that elicit powerful T helper cell type 2 (Th2) responses leading to hyper-immunoglobulin E (IgE) production and allergy. Research carried out over several years has highlighted the possible role of the inherent protease activity, surface features and glycosylation patterns of allergens in the engagement of a Th2 signalling pathway. It is thought that allergens possess common features and patterns that enable them to be recognized by innate immune defences as Th2-inducing antigens. These events are further amplified by proteolytically active allergens through digestion of cell surface molecules involved in regulating innate and adaptive immune functions, favouring Th2 responses. A greater understanding of the molecular features that make proteins allergenic will help define new therapeutic targets aimed at blocking allergen recognition and protease activity.
最长约 10秒,即可获得该文献文件

科研通智能强力驱动
Strongly Powered by AbleSci AI
科研通是完全免费的文献互助平台,具备全网最快的应助速度,最高的求助完成率。 对每一个文献求助,科研通都将尽心尽力,给求助人一个满意的交代。
实时播报
刚刚
null的应助被科研通管家采纳,获得10
刚刚
诸葛明明的应助被科研通管家采纳,获得10
刚刚
汉堡包的应助被科研通管家采纳,获得10
1秒前
深情安青的应助被小白采纳,获得10
1秒前
辰溟的应助被科研通管家采纳,获得20
1秒前
充电宝的应助被科研通管家采纳,获得30
1秒前
顾矜的应助被科研通管家采纳,获得10
1秒前
传奇3的应助被G浅浅采纳,获得10
1秒前
华仔的应助被周大侠采纳,获得10
1秒前
无花果的应助被科研通管家采纳,获得10
1秒前
1秒前
1秒前
传奇3的应助被科研通管家采纳,获得10
1秒前
爆米花的应助被科研通管家采纳,获得10
1秒前
顾矜的应助被科研通管家采纳,获得10
1秒前
null的应助被科研通管家采纳,获得10
2秒前
3503264269发布了新的文献求助10
2秒前
Orange的应助被科研通管家采纳,获得10
2秒前
研友_VZG7GZ的应助被科研通管家采纳,获得10
2秒前
赘婿的应助被科研通管家采纳,获得10
2秒前
2秒前
2秒前
2秒前
华仔的应助被科研通管家采纳,获得10
2秒前
小胖完成签到,获得积分10
2秒前
2秒前
wanci的应助被科研通管家采纳,获得10
3秒前
俞志远的应助被科研通管家采纳,获得10
3秒前
赘婿的应助被科研通管家采纳,获得10
3秒前
3秒前
丘比特的应助被科研通管家采纳,获得10
3秒前
3秒前
Jasper的应助被科研通管家采纳,获得10
3秒前
3秒前
5秒前
CodeCraft的应助被简单面包采纳,获得10
5秒前
苏暮雨完成签到 ,获得积分20
6秒前
7秒前
科研通AI6.2的应助被XZM采纳,获得40
7秒前
高分求助中
(应助此贴封号)【重要!!请各用户(尤其是新用户)详细阅读】【科研通的精品贴汇总】 10000
Essentials of Carbohydrate Chemistry and Biochemistry, 4th Edition 1000
Электротехническая система магнитожидкостной герметизации валов регулируемых электродвигателей 800
Guidelines for fracture-safe and fatigue-reliable design of steel structures 600
The Basics of Practical Optimization, Second Edition 600
Problems and Solutions for Integer and Combinatorial Optimization: Building Skills in Discrete Optimization 600
Organizational Behavior 510
热门求助领域 (近24小时)
化学 材料科学 医学 生物 纳米技术 计算机科学 工程类 有机化学 化学工程 生物化学 物理 复合材料 内科学 催化作用 光电子学 人工智能 细胞生物学 无机化学 物理化学 数学
热门帖子
关注 科研通微信公众号,转发送积分 7984885
求助须知:如何正确求助?哪些是违规求助? 9444390
关于积分的说明 21090880
捐赠科研通 7559412
什么是DOI,文献DOI怎么找? 3376953
关于科研通互助平台的介绍 2510911
邀请新用户注册赠送积分活动 2410220