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  1. Article ; Online: SARS-CoV-2 immunogenicity at the crossroads.

    Karamloo, Fariba / König, Renate

    Allergy

    2020  Volume 75, Issue 7, Page(s) 1822–1824

    MeSH term(s) Angiotensin-Converting Enzyme 2 ; Antibodies, Neutralizing/immunology ; Antibodies, Viral/immunology ; Betacoronavirus/genetics ; Betacoronavirus/immunology ; COVID-19 ; Coronavirus Infections/prevention & control ; Coronavirus Infections/virology ; Cross Reactions ; Humans ; Immunogenicity, Vaccine ; Mutation Rate ; Pandemics/prevention & control ; Peptidyl-Dipeptidase A/metabolism ; Pneumonia, Viral/prevention & control ; Pneumonia, Viral/virology ; SARS-CoV-2 ; Spike Glycoprotein, Coronavirus/immunology ; Spike Glycoprotein, Coronavirus/metabolism ; Viral Vaccines/immunology
    Chemical Substances Antibodies, Neutralizing ; Antibodies, Viral ; Spike Glycoprotein, Coronavirus ; Viral Vaccines ; spike protein, SARS-CoV-2 ; Peptidyl-Dipeptidase A (EC 3.4.15.1) ; ACE2 protein, human (EC 3.4.17.23) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
    Keywords covid19
    Language English
    Publishing date 2020-05-25
    Publishing country Denmark
    Document type Letter ; Research Support, Non-U.S. Gov't
    ZDB-ID 391933-x
    ISSN 1398-9995 ; 0105-4538
    ISSN (online) 1398-9995
    ISSN 0105-4538
    DOI 10.1111/all.14360
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  3. Article ; Online: SARS‐CoV‐2 immunogenicity at the crossroads

    Karamloo, Fariba / König, Renate

    Allergy

    2020  Volume 75, Issue 7, Page(s) 1822–1824

    Keywords Immunology ; Immunology and Allergy ; covid19
    Language English
    Publisher Wiley
    Publishing country us
    Document type Article ; Online
    ZDB-ID 391933-x
    ISSN 1398-9995 ; 0105-4538
    ISSN (online) 1398-9995
    ISSN 0105-4538
    DOI 10.1111/all.14360
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article: Phenylcoumaran benzylic ether and isoflavonoid reductases are a new class of cross‐reactive allergens in birch pollen, fruits and vegetables

    Karamloo, Fariba / Wangorsch, Andrea / Kasahara, Hiroyuki / Davin, Laurence B / Haustein, Dieter / Lewis, Norman G / Vieths, Stefan

    European journal of biochemistry. 2001 Oct. 15, v. 268, no. 20

    2001  

    Abstract: We investigated the biochemical function of the birch pollen allergen Bet v 6 and its role in the IgE‐cross‐reactivity between birch pollen and plant foods, and characterized Pyr c 5, a Bet v 6‐related food allergen, from pear; the proteins were ... ...

    Abstract We investigated the biochemical function of the birch pollen allergen Bet v 6 and its role in the IgE‐cross‐reactivity between birch pollen and plant foods, and characterized Pyr c 5, a Bet v 6‐related food allergen, from pear; the proteins were expressed as His‐Tag fusion proteins in Eschershia coli and purified by Ni‐chelate affinity chromatography under native conditions. Nonfusion proteins were obtained by factor Xa protease treatment. The highest degree of amino‐acid sequence identity of Pyr c 5 and Bet v 6 was found with a plant protein related to a defense mechanism, which we have named phenylcoumaran benzylic ether reductase (PCBER) based on its ability to catalyze the NADPH‐dependent reduction of 8–5′ linked lignans such as dehydrodiconiferyl alcohol to give isodihydrodehydrodiconiferyl alcohol. Enzymatic assays with recombinant Pyr c 5 and Bet v 6 showed PCBER catalytic activity for both recombinant allergens. Both Pyr c 5 and Bet v 6 allergens had similar IgE binding characteristics in immunoblotting and enzyme allergosorbent tests (EAST), and bound IgE from 10 sera of birch‐pollen‐allergic patients including six pear‐allergic subjects. EAST inhibition experiments with Pyr c 5 as the solid phase antigen suggested that homologous allergens may be present in many vegetable foods such as apple, peach, orange, lychee fruit, strawberry, persimmon, zucchini (courgette), and carrot. In extracts of pear, apple, orange, and persimmon, the presence of proteins of approximately 30–35 kDa containing Bet v 6 cross‐reactive epitopes was demonstrated with two Bet v 6‐specific monoclonal antibodies. Recombinant Pyr c 5 triggered a strong, dose‐dependent mediator release from basophils of a pear‐allergic subject, suggesting that Pyr c 5 has the potential to elicit type I allergic reactions.
    Keywords Betula ; affinity chromatography ; alcohols ; allergens ; amino acid sequences ; apples ; basophils ; binding properties ; carrots ; catalytic activity ; dose response ; epitopes ; foods ; fruits ; immunoblotting ; immunoglobulin E ; lignans ; litchis ; monoclonal antibodies ; oranges ; patients ; peaches ; pears ; persimmons ; pollen ; protein synthesis ; proteinases ; sequence analysis ; strawberries ; zucchini
    Language English
    Dates of publication 2001-1015
    Size p. 5310-5320.
    Publishing place Blackwell Science Ltd
    Document type Article
    ZDB-ID 3032-6
    ISSN 1432-1033 ; 0014-2956
    ISSN (online) 1432-1033
    ISSN 0014-2956
    DOI 10.1046/j.0014-2956.2001.02463.x
    Database NAL-Catalogue (AGRICOLA)

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  5. Article: Immune responses in healthy and allergic individuals are characterized by a fine balance between allergen-specific T regulatory 1 and T helper 2 cells.

    Akdis, Mübeccel / Verhagen, Johan / Taylor, Alison / Karamloo, Fariba / Karagiannidis, Christian / Crameri, Reto / Thunberg, Sarah / Deniz, Günnur / Valenta, Rudolf / Fiebig, Helmut / Kegel, Christian / Disch, Rainer / Schmidt-Weber, Carsten B / Blaser, Kurt / Akdis, Cezmi A

    The Journal of experimental medicine

    2004  Volume 199, Issue 11, Page(s) 1567–1575

    Abstract: The mechanisms by which immune responses to nonpathogenic environmental antigens lead to either allergy or nonharmful immunity are unknown. Single allergen-specific T cells constitute a very small fraction of the whole CD4+ T cell repertoire and can be ... ...

    Abstract The mechanisms by which immune responses to nonpathogenic environmental antigens lead to either allergy or nonharmful immunity are unknown. Single allergen-specific T cells constitute a very small fraction of the whole CD4+ T cell repertoire and can be isolated from the peripheral blood of humans according to their cytokine profile. Freshly purified interferon-gamma-, interleukin (IL)-4-, and IL-10-producing allergen-specific CD4+ T cells display characteristics of T helper cell (Th)1-, Th2-, and T regulatory (Tr)1-like cells, respectively. Tr1 cells consistently represent the dominant subset specific for common environmental allergens in healthy individuals; in contrast, there is a high frequency of allergen-specific IL-4-secreting T cells in allergic individuals. Tr1 cells use multiple suppressive mechanisms, IL-10 and TGF-beta as secreted cytokines, and cytotoxic T lymphocyte antigen 4 and programmed death 1 as surface molecules. Healthy and allergic individuals exhibit all three allergen-specific subsets in different proportions, indicating that a change in the dominant subset may lead to allergy development or recovery. Accordingly, blocking the suppressor activity of Tr1 cells or increasing Th2 cell frequency enhances allergen-specific Th2 cell activation ex vivo. These results indicate that the balance between allergen-specific Tr1 cells and Th2 cells may be decisive in the development of allergy.
    MeSH term(s) Adult ; Allergens/immunology ; Antigens, CD ; Antigens, Differentiation/physiology ; CTLA-4 Antigen ; Humans ; Hypersensitivity/etiology ; Hypersensitivity/immunology ; Interferon-gamma/biosynthesis ; Interleukin-10/biosynthesis ; Interleukin-4/biosynthesis ; T-Lymphocytes/immunology ; Th2 Cells/immunology ; Transforming Growth Factor beta/biosynthesis
    Chemical Substances Allergens ; Antigens, CD ; Antigens, Differentiation ; CTLA-4 Antigen ; CTLA4 protein, human ; Transforming Growth Factor beta ; Interleukin-10 (130068-27-8) ; Interleukin-4 (207137-56-2) ; Interferon-gamma (82115-62-6)
    Language English
    Publishing date 2004-06-07
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 218343-2
    ISSN 1540-9538 ; 0022-1007
    ISSN (online) 1540-9538
    ISSN 0022-1007
    DOI 10.1084/jem.20032058
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  6. Article: A major allergen gene-fusion protein for potential usage in allergen-specific immunotherapy.

    Kussebi, Fatimah / Karamloo, Fariba / Rhyner, Claudio / Schmid-Grendelmeier, Peter / Salagianni, Maria / Mannhart, Christian / Akdis, Mübeccel / Soldatova, Lyudmilla / Markovic-Housley, Zora / Von Beust, Barbara R / Kündig, Thomas / Kemeny, David M / Blaser, Kurt / Crameri, Reto / Akdis, Cezmi A

    The Journal of allergy and clinical immunology

    2005  Volume 115, Issue 2, Page(s) 323–329

    Abstract: Background: Specific immunotherapy is a common treatment of allergic diseases and could potentially be applied to other immunologic disorders. Despite its use in clinical practice, more defined and safer allergy vaccine preparations are required. ... ...

    Abstract Background: Specific immunotherapy is a common treatment of allergic diseases and could potentially be applied to other immunologic disorders. Despite its use in clinical practice, more defined and safer allergy vaccine preparations are required. Differences between epitopes of IgE that recognize the 3-dimensional structure of allergens and T cells that recognize linear amino acid sequences provide a suitable tool for novel vaccine development for specific immunotherapy.
    Objective: The aim of the study was to delete B-cell epitopes and prevent IgE crosslinking, but to preserve T-cell epitopes by fusion of 2 major allergens of bee venom because of a change in the conformation.
    Methods: By genetic engineering, we produced a fusion protein composed of the 2 major bee venom allergens: phospholipase A 2 (Api m 1) and hyaluronidase (Api m 2).
    Results: The Api m [1/2] fusion protein induced T-cell proliferation and both T H 1-type and T H 2-type cytokine responses. In contrast, IgE reactivity was abolished, and profoundly reduced basophil degranulation and type 1 skin test reactivity was observed. Pretreatment of mice with Api m [1/2] fusion protein significantly suppressed the development of specific IgE as well as other antibody isotypes after immunization with the native allergen.
    Conclusion: The novel fusion protein of 2 major allergens bypasses IgE binding and mast cell/basophil IgE FcepsilonRI crosslinking and protects from IgE development.
    MeSH term(s) Adult ; Allergens/genetics ; Allergens/immunology ; Animals ; Antibodies/analysis ; Antibodies/immunology ; Antibody Formation/drug effects ; Antibody Specificity ; Antigens, Plant ; Bee Venoms/immunology ; Cell Division/drug effects ; Cells, Cultured ; Cytokines/metabolism ; Epitopes ; Humans ; Hyaluronoglucosaminidase/genetics ; Immunoglobulin E/analysis ; Immunoglobulin E/immunology ; Immunoglobulin G/analysis ; Immunotherapy ; Insect Proteins ; Mice ; Middle Aged ; Phospholipases A/genetics ; Phospholipases A/immunology ; Recombinant Fusion Proteins/immunology ; Recombinant Fusion Proteins/pharmacology ; Recombinant Fusion Proteins/therapeutic use ; T-Lymphocytes/cytology ; T-Lymphocytes/metabolism ; Vaccination
    Chemical Substances Allergens ; Antibodies ; Antigens, Plant ; Bee Venoms ; Cytokines ; Epitopes ; Immunoglobulin G ; Insect Proteins ; Recombinant Fusion Proteins ; Immunoglobulin E (37341-29-0) ; Phospholipases A (EC 3.1.1.32) ; Api m 1 allergen, Apis mellifera (EC 3.1.1.4) ; Api m 2 allergen, Apis mellifera (EC 3.2.1.35) ; Hyaluronoglucosaminidase (EC 3.2.1.35)
    Language English
    Publishing date 2005-02
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 121011-7
    ISSN 1085-8725 ; 1097-6825 ; 0091-6749
    ISSN (online) 1085-8725 ; 1097-6825
    ISSN 0091-6749
    DOI 10.1016/j.jaci.2004.11.041
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  7. Article: Prevention of allergy by a recombinant multi-allergen vaccine with reduced IgE binding and preserved T cell epitopes.

    Karamloo, Fariba / Schmid-Grendelmeier, Peter / Kussebi, Fatimah / Akdis, Mübeccel / Salagianni, Maria / von Beust, Barbara R / Reimers, Andrea / Zumkehr, Judith / Soldatova, Lyudmilla / Housley-Markovic, Zora / Müller, Ulrich / Kündig, Thomas / Kemeny, David M / Spangfort, Michael D / Blaser, Kurt / Akdis, Cezmi A

    European journal of immunology

    2005  Volume 35, Issue 11, Page(s) 3268–3276

    Abstract: Novel approaches for the prevention of allergy are required, because of the inevitably increasing prevalence of allergic diseases during the last 30 years. Here, a recombinant chimeric protein, which comprises the whole amino acid sequences of three bee ... ...

    Abstract Novel approaches for the prevention of allergy are required, because of the inevitably increasing prevalence of allergic diseases during the last 30 years. Here, a recombinant chimeric protein, which comprises the whole amino acid sequences of three bee venom major allergens has been engineered and used in prevention of bee venom sensitization in mice. Phospholipase A2 (Api m 1), hyaluronidase (Api m 2) and melittin (Api m 3) fragments with overlapping amino acids were assembled in a different order in the Api m (1/2/3) chimeric protein, which preserved entire T cell epitopes, whereas B cell epitopes of all three allergens were abrogated. Accordingly, IgE cross-linking leading to mast cell and basophil mediator release was profoundly reduced in humans. Supporting these findings, the Api m (1/2/3) induced 100 to 1000 times less type-1 skin test reactivity in allergic patients. Treatment of mice with Api m (1/2/3) led to a significant reduction of specific IgE development towards native allergen, representing a protective vaccine effect in vivo. These results demonstrate a novel prototype of a preventive allergy vaccine, which preserves the entire T cell epitope repertoire, but bypasses induction of IgE against native allergen, and side effects related to mast cell/basophil IgE FcepsilonRI cross-linking in sensitized individuals.
    MeSH term(s) Allergens/administration & dosage ; Allergens/immunology ; Allergens/metabolism ; Animals ; Antigens, Plant ; Bees ; Binding Sites, Antibody ; Cells, Cultured ; Epitopes, T-Lymphocyte/administration & dosage ; Epitopes, T-Lymphocyte/immunology ; Epitopes, T-Lymphocyte/metabolism ; Female ; Humans ; Hyaluronoglucosaminidase/administration & dosage ; Hyaluronoglucosaminidase/immunology ; Hyaluronoglucosaminidase/metabolism ; Hypersensitivity/immunology ; Hypersensitivity/prevention & control ; Hypersensitivity/therapy ; Immunoglobulin E/biosynthesis ; Immunoglobulin E/metabolism ; Immunoglobulin G/biosynthesis ; Insect Bites and Stings/immunology ; Insect Bites and Stings/therapy ; Insect Proteins ; Mice ; Mice, Inbred C57BL ; Phospholipases A/administration & dosage ; Phospholipases A/immunology ; Phospholipases A/metabolism ; Phospholipases A2 ; T-Lymphocytes/immunology ; Vaccines, Synthetic/administration & dosage ; Vaccines, Synthetic/immunology ; Vaccines, Synthetic/metabolism
    Chemical Substances Allergens ; Antigens, Plant ; Epitopes, T-Lymphocyte ; Immunoglobulin G ; Insect Proteins ; Vaccines, Synthetic ; Immunoglobulin E (37341-29-0) ; Phospholipases A (EC 3.1.1.32) ; Api m 1 allergen, Apis mellifera (EC 3.1.1.4) ; Phospholipases A2 (EC 3.1.1.4) ; Api m 2 allergen, Apis mellifera (EC 3.2.1.35) ; Hyaluronoglucosaminidase (EC 3.2.1.35)
    Language English
    Publishing date 2005-11
    Publishing country Germany
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 120108-6
    ISSN 1521-4141 ; 0014-2980
    ISSN (online) 1521-4141
    ISSN 0014-2980
    DOI 10.1002/eji.200425522
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  8. Article: SARS-CoV-2 immunogenicity at the crossroads

    Karamloo, Fariba / König, Renate

    Allergy, 75(7):1822-1824

    2020  

    Institution Paul-Ehrlich-Institut
    Keywords COVID-19 ; infections ; inflammation ; lung diseases other than asthma and COPD ; vaccines ; virus
    Language English
    Document type Article
    Database Repository for Life Sciences

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