Orchestration of an uncommon maturation cascade of the house dust mite protease allergen quartet

MINI REVIEW ARTICLE

Front. Immunol., 31 March 2014 | doi: 10.3389/fimmu.2014.00138

Marie-Eve Dumez^1,2, Julie Herman², Vincenzo Campizi^1,2, Moreno Galleni², Alain Jacquet³ and Andy Chevigné¹*

• 1Laboratory of Retrovirology, Department of Infection and Immunity, Centre de Recherche Public Santé, Luxembourg, Luxembourg
• 2Macromolécules Biologiques, Department of Life Sciences, Centre for Protein Engineering, University of Liège, Liège, Belgium
• 3Faculty of Medicine, Department of Medicine, Division of Allergy and Clinical Immunology, Chulalongkorn University, Bangkok, Thailand

In more than 20% of the world population, sensitization to house dust mite allergens triggers typical allergic diseases such as allergic rhinitis and asthma. Amongst the 23 mite allergen groups hitherto identified, group 1 is cysteine proteases belonging to the papain-like family whereas groups 3, 6, and 9 are serine proteases displaying trypsin, chymotrypsin, and collagenolytic activities, respectively. While these proteases are more likely to be involved in the mite digestive system, they also play critical roles in the initiation and in the chronicity of the allergic response notably through the activation of innate immune pathways. All these allergenic proteases are expressed in mite as inactive precursor form. Until recently, the exact mechanisms of their maturation into active proteases remained to be fully elucidated. Recent breakthroughs in the understanding of the activation mechanisms of mite allergenic protease precursors have highlighted an uncommon and unique maturation pathway orchestrated by group 1 proteases that tightly regulates the proteolytic activities of groups 1, 3, 6, and 9 through complex intra- or inter-molecular mechanisms. This review presents and discusses the currently available knowledge of the activation mechanisms of group 1, 3, 6, and 9 allergens of Dermatophagoides pteronyssinus laying special emphasis on their localization, regulation, and interconnection.

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Keywords: mite, proteases, Der p 1, allergen, activation cascade, localization, interaction

Citation: Dumez M-E, Herman J, Campizi V, Galleni M, Jacquet A and Chevigné A (2014) Orchestration of an uncommon maturation cascade of the house dust mite protease allergen quartet. Front. Immunol. 5:138. doi: 10.3389/fimmu.2014.00138

Received: 13 December 2013; Accepted: 18 March 2014;
Published online: 31 March 2014.

Edited by:

Christiane Hilger, Centre de Recherche Public Santé, Luxembourg

Reviewed by:

Beatrice Jahn-Schmid, Medical University of Vienna, Austria
Enrique Fernandez-Caldas, Inmunotek, Spain

Copyright: © 2014 Dumez, Herman, Campizi, Galleni, Jacquet and Chevigné. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

*Correspondence: Andy Chevigné, Laboratory of Retrovirology, Centre de Recherche Public Santé, 84 Val Fleuri, Luxembourg L-1526, Luxembourg e-mail: andy.chevigne@crp-sante.lu