Isolation and characterization of the major centipede allergen Sco m 5 from Scolopendra subspinipes mutilans

Background: Allergic reactions have been observed following both direct centipede bites and the clinical use of centipede-containing medicines, such as traditional Chinese medicines utilizing Scolopendra subspinipes mutilans; however, no natural centipede allergen has yet been characterized. Methods...

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Main Authors: Xin-Qiang Lan, Feng Zhao, Qi-Quan Wang, Jiang-Hua Li, Lin Zeng, Yun Zhang, Wen-Hui Lee
Format: Article
Language:English
Published: Elsevier 2021-01-01
Series:Allergology International
Subjects:
IgE
Online Access:http://www.sciencedirect.com/science/article/pii/S1323893020300927
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record_format Article
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language English
format Article
sources DOAJ
author Xin-Qiang Lan
Feng Zhao
Qi-Quan Wang
Jiang-Hua Li
Lin Zeng
Yun Zhang
Wen-Hui Lee
spellingShingle Xin-Qiang Lan
Feng Zhao
Qi-Quan Wang
Jiang-Hua Li
Lin Zeng
Yun Zhang
Wen-Hui Lee
Isolation and characterization of the major centipede allergen Sco m 5 from Scolopendra subspinipes mutilans
Allergology International
Allergen
Centipede
Cross-reactivity
IgE
Venom
author_facet Xin-Qiang Lan
Feng Zhao
Qi-Quan Wang
Jiang-Hua Li
Lin Zeng
Yun Zhang
Wen-Hui Lee
author_sort Xin-Qiang Lan
title Isolation and characterization of the major centipede allergen Sco m 5 from Scolopendra subspinipes mutilans
title_short Isolation and characterization of the major centipede allergen Sco m 5 from Scolopendra subspinipes mutilans
title_full Isolation and characterization of the major centipede allergen Sco m 5 from Scolopendra subspinipes mutilans
title_fullStr Isolation and characterization of the major centipede allergen Sco m 5 from Scolopendra subspinipes mutilans
title_full_unstemmed Isolation and characterization of the major centipede allergen Sco m 5 from Scolopendra subspinipes mutilans
title_sort isolation and characterization of the major centipede allergen sco m 5 from scolopendra subspinipes mutilans
publisher Elsevier
series Allergology International
issn 1323-8930
publishDate 2021-01-01
description Background: Allergic reactions have been observed following both direct centipede bites and the clinical use of centipede-containing medicines, such as traditional Chinese medicines utilizing Scolopendra subspinipes mutilans; however, no natural centipede allergen has yet been characterized. Methods: An allergen was purified from S. s. mutilans venom using Superdex 75 gel filtration and RESOURCE S ion chromatography, and its primary structure was determined via a combination of LC-MS-MS, MALDI-TOF/TOF and protein sequencing techniques. Its potential allergenicity was evaluated by immunoblotting, ELISAs, skin prick tests (SPTs) and mast cell activation assays. Results: A novel allergen Sco m 5 (210 amino acids long) was successfully purified from crude S. s. mutilans venom. Sco m 5 could promote the degranulation of a human mast cell line, HMC-1. Among centipede-allergic patients, Sco m 5 showed an 83.3% IgE-binding frequency and a 66.7% positive reaction frequency, as detected by immunoblotting and SPTs, respectively. Sco m 5 IgE-binding frequencies of common Chinese population was found to be 9%–16%. Sera positive for Sco m 5 IgE-binding was cross-reactive against venom from the wasp Vespa mandaeinia. Conclusions: The present study isolated and characterized a novel allergen termed as Sco m 5 from the centipede S. s. mutilans. The use of Sco m 5 to identify centipede-allergic individuals could be important, given the high potential allergenicity of Sco m 5 among the general Chinese population, along with the likely possibility of cross-reactivity against wasp venom among centipede-allergic patients.
topic Allergen
Centipede
Cross-reactivity
IgE
Venom
url http://www.sciencedirect.com/science/article/pii/S1323893020300927
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spelling doaj-db96e3dc02244294b9df9cb7edbc437d2020-12-19T05:04:38ZengElsevierAllergology International1323-89302021-01-01701121128Isolation and characterization of the major centipede allergen Sco m 5 from Scolopendra subspinipes mutilansXin-Qiang Lan0Feng Zhao1Qi-Quan Wang2Jiang-Hua Li3Lin Zeng4Yun Zhang5Wen-Hui Lee6Key Laboratory of Animal Models and Human Disease Mechanisms of the Chinese Academy of Sciences/Key Laboratory of Bio-active Peptides of Yunnan Province, Kunming Institute of Zoology, Kunming, Yunnan, China; Key Laboratory of Ethic Medical Resources Research and Southeast Asian International Cooperation of Yunnan Universities, Department of Biology and Chemistry, Puer University, Puer, Yunnan, China; Kunming College of Life Science, University of Chinese Academy of Sciences, Kunming, Yunnan, ChinaKey Laboratory of Animal Models and Human Disease Mechanisms of the Chinese Academy of Sciences/Key Laboratory of Bio-active Peptides of Yunnan Province, Kunming Institute of Zoology, Kunming, Yunnan, China; Key Laboratory of Ethic Medical Resources Research and Southeast Asian International Cooperation of Yunnan Universities, Department of Biology and Chemistry, Puer University, Puer, Yunnan, ChinaKey Laboratory of Animal Models and Human Disease Mechanisms of the Chinese Academy of Sciences/Key Laboratory of Bio-active Peptides of Yunnan Province, Kunming Institute of Zoology, Kunming, Yunnan, China; Kunming College of Life Science, University of Chinese Academy of Sciences, Kunming, Yunnan, ChinaPuer People's Hospital, Puer, Yunnan, ChinaKey Laboratory of Animal Models and Human Disease Mechanisms of the Chinese Academy of Sciences/Key Laboratory of Bio-active Peptides of Yunnan Province, Kunming Institute of Zoology, Kunming, Yunnan, ChinaKey Laboratory of Animal Models and Human Disease Mechanisms of the Chinese Academy of Sciences/Key Laboratory of Bio-active Peptides of Yunnan Province, Kunming Institute of Zoology, Kunming, Yunnan, China; CAS Center for Excellence in Animal Evolution and Genetics, Kunming Institute of Zoology, The Chinese Academy of Sciences, Kunming, Yunnan, China; Corresponding author. Kunming Institute of Zoology, The Chinese Academy of Science, 32 East Jiao Chang Road, Kunming, Yunnan 650223, China.Key Laboratory of Animal Models and Human Disease Mechanisms of the Chinese Academy of Sciences/Key Laboratory of Bio-active Peptides of Yunnan Province, Kunming Institute of Zoology, Kunming, Yunnan, China; Corresponding author. Kunming Institute of Zoology, The Chinese Academy of Sciences, 32 East Jiao Chang Road, Kunming, Yunnan 650223, China.Background: Allergic reactions have been observed following both direct centipede bites and the clinical use of centipede-containing medicines, such as traditional Chinese medicines utilizing Scolopendra subspinipes mutilans; however, no natural centipede allergen has yet been characterized. Methods: An allergen was purified from S. s. mutilans venom using Superdex 75 gel filtration and RESOURCE S ion chromatography, and its primary structure was determined via a combination of LC-MS-MS, MALDI-TOF/TOF and protein sequencing techniques. Its potential allergenicity was evaluated by immunoblotting, ELISAs, skin prick tests (SPTs) and mast cell activation assays. Results: A novel allergen Sco m 5 (210 amino acids long) was successfully purified from crude S. s. mutilans venom. Sco m 5 could promote the degranulation of a human mast cell line, HMC-1. Among centipede-allergic patients, Sco m 5 showed an 83.3% IgE-binding frequency and a 66.7% positive reaction frequency, as detected by immunoblotting and SPTs, respectively. Sco m 5 IgE-binding frequencies of common Chinese population was found to be 9%–16%. Sera positive for Sco m 5 IgE-binding was cross-reactive against venom from the wasp Vespa mandaeinia. Conclusions: The present study isolated and characterized a novel allergen termed as Sco m 5 from the centipede S. s. mutilans. The use of Sco m 5 to identify centipede-allergic individuals could be important, given the high potential allergenicity of Sco m 5 among the general Chinese population, along with the likely possibility of cross-reactivity against wasp venom among centipede-allergic patients.http://www.sciencedirect.com/science/article/pii/S1323893020300927AllergenCentipedeCross-reactivityIgEVenom