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Jörg Kleine-Tebbe - Molecular Allergy Diagnostics: Innovation for a Better Patient Management

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Molecular Allergy Diagnostics: Innovation for a Better Patient Management
Author:
Jrg KleineTebbe / Thilo Jakob
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Springer
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2017
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This book, based on a recent German publication, offers an overview of basic data and recent developments in the groundbreaking field of molecular allergology. It comprehensively explores the origin and structure of single allergen molecules (components) and their utility in improving the management of type I, IgE-mediated allergic reactions and disorders like allergic respiratory diseases, food allergies, and anaphylaxis. Highly specific testing, called component-resolved diagnostics, aims to identify and utilize single molecules. Over 200 single allergens from plant or animal sources have been applied to single or multiplex laboratory testing for the presence of allergen-specific IgE. This leap in assay sensitivity and specificity has led to three major advances in patient management: discrimination between primary allergic sensitization and complex cross-reactivity, recognition of IgE profiles for certain allergens and identification of patients most likely to benefit from allergen-specific immunotherapy. The book discusses in detail the benefits and limitations of this 21st century technology, and offers suggestions for the use of molecular allergology in routine clinical practice. It is a must read for physicians treating allergic patients as well as scientists interested in natural allergic molecules and their interactions with the human immune system.

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Part I
Protein Families and Relationships

Springer International Publishing Switzerland 2017

Jrg Kleine-Tebbe and Thilo Jakob (eds.) Molecular Allergy Diagnostics 10.1007/978-3-319-42499-6_1

1. Introduction to Molecular Allergology: Protein Families, Databases, and Potential Benefits

J. Kleine-Tebbe 1

(1)

Allergy & Asthma Center Westend, Outpatient Clinic Hanf, Ackermann & Kleine-Tebbe, Berlin, Germany

(2)

Department of Infection and Immunity, Luxembourg Institute of Health (LIH), Esch-sur-Alzette, Luxembourg

(3)

Odense Research Center for Anaphylaxis (ORCA), Department of Dermatology and Allergy Center, Odense University Hospital, University of Southern Denmark, Odense C, Denmark

(4)

Department of Pathophysiology and Allergy Research, Center for Pathophysiology, Infectiology and Immunology, Medical University of Vienna, Vienna, Austria

(5)

Department of Dermatology and Allergology, University Medical Center Giessen (UKGM), Justus-Liebig-University, Giessen, Germany

J. Kleine-Tebbe (Corresponding author)

Email:

M. Ollert

Email:

URL: http://www.lih.lu

URL: http://www.anafylaksi.net/

C. Radauer

Email:

T. Jakob

Email:

This contribution is based on a publication that appeared in the Allergo Journal in 2010 (Kleine-Tebbe J, Ollert M, Jakob T: Molekulare Allergologie: Nomenklatur, Proteinfamilien, Datenbanken und potenzieller Nutzen. Allergo J 2010; 19: 390394) and which has been updated, expanded, and translated into English as a chapter for this book.

The authors gratefully thank Dr. Steve Love, PhD, Laguna Niguel, CA, USA, for reading the manuscript, helpful suggestions, and editorial assistance with the English translation.

1.1 The Era of Molecular Allergology

Thanks to advances in methods of protein biochemistry and molecular biology, the past 30 years have seen the identification of the most important allergens that induce IgE-mediated immediate-type reactions and atopic conditions. The study of allergens (the main focus of which was previously the biological relatedness of allergy sources, e.g., plant, mite, and mammalian species) was thus mounting a molecular dimension and new terminology ( brief glossary). Modern allergen research is providing the foundation for improved allergy diagnostics and therapy which complements and/or replaces our previous allergological methodology (for review, see also Matricardi et al. ).

Molecular Allergology: A Brief Glossary (modified from Kleine-Tebbe et al )

Allergen (also single allergen

A molecule (protein, e.g., major allergen Bet v 1or allergen component)from birch pollen, in rare cases carbohydrate moieties) that may induce an allergic immune response

Allergen extract

Mixture of allergenic and nonallergenic components extracted from the allergen source (e.g., birch pollen)

Allergen nomenclature

International agreement on the designation (naming) of allergens

Allergen source

Biological species that produces (single) allergens and releases them into the environment

CRD

Component-resolved diagnostics (allergy diagnostic procedures with single allergens)

Epitope

Binding site for antibodies

Isoallergen

Variant form of an allergen with similar amino acid sequence (>67 % identity score)

Linear epitope

Peptide sequence that may be bound by an antibody or a T cell receptor

Conformational epitope

Discontinuous, structure-dependent binding site for antibodies

Cross- reaction

Immunological response caused by structural similarity and involving molecules not responsible for the original sensitization

Major allergen

An allergen that binds IgE in 50 % of allergic individuals

Minor allergen

Allergen that binds IgE in <50 % of allergic individuals

Multiplex assay

In vitro diagnostic test with concurrent testing of antibodies (e.g., IgE) to many (single) allergens

Panallergen

An allergen that is ubiquitous or present in many allergen sources, generally highly conserved (i.e., little changed by evolution)

Protein family

Group of proteins related in terms of sequence and structural similarity

Recombinant

Produced by means of genetically modified microorganisms

Recombinant allergen

Allergenic protein frequently produced in Escherichia coli that lacks modifications occurring in native allergens (e.g., carbohydrate side chains)

Sequential epitope

Antibody binding site whose basis is a continuous peptide sequence ( linear epitope)

Singleplex assay

In vitro diagnostic test (e.g., antibody test) detecting allergy to a single allergen

Species specific

Allergen or other characteristic present in only one species

1.2 Immediate-Type Allergens and Their Names

As early as the 1980s, a systematic naming convention was proposed for the first purified protein allergens and an allergen nomenclature devised (Marsh et al. ).

This official nomenclature (Chapman ).

Table 1.1

Allergen nomenclature : names of allergens illustrated with reference to rBet v 1.0102, a major allergen of the silver birch ( Betula verrucosa )

Abbreviation	Full term	Explanatory notes
n	Natural	Obtained from the allergen source (= purified)
r	Recombinant	Produced in microorganisms such as bacteria
Bet	Betula	The first 34 letters of the genus name
v	verrucosa	The first 12 letters of the species name
	Allergen number	Indicates order in which allergens were first reported
.01	Isoallergen number	Different sequences of an allergen with >67 % sequence identity are termed isoallergens
	Variant number	Different sequences of an allergen with >90 % sequence identity are termed variants

1.3 Sequence and Structure: From T Cell to Antibody (B Cell) Epitopes

As with other proteins, each allergen (including its natural variants) is coded for by corresponding genes.

By means of its physicochemical properties, the resulting amino acid sequence (primary structure) gives rise to folding and the spatial arrangement of the polypeptide chain in regular structural elements ( Fig. ): examples are -helix, -sheet, and -turn (secondary structure). The overall arrangement of the secondary structure elements determines a proteins three-dimensional structure (tertiary structure). Additionally, several polypeptide chains can combine to form larger complexes (quaternary structure). Practically, allergen molecules or their fragments correspond to the general structural hierarchy of proteins.

Fig. 1.1

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