Delineation of the Olive Pollen Proteome and Its Allergenome Unmasks Cyclophilin as a Relevant Cross-Reactive Allergen

Segundo‐Acosta, Pablo San; Oeo-Santos, Carmen; Benedé, Sara; Rı́os, Vivian de los; Navas, Ana; Ruíz-León, Berta; Moreno‐Aguilar, Carmen; Pastor-Vargas, Carlos; Jurado, Aurora; Villalba, Mayte; Barderas, Rodrigo

doi:10.1021/acs.jproteome.9b00167

Cited by 22 publications

(25 citation statements)

References 70 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Indeed, it is a main allergenic source in California (US), China, India, Australia and South America beyond the Mediterranean Basin, where this pollen has been extensively studied . Fourteen olive pollen allergens have been identified so far . Among them, the nsLTP Ole e 7 is a major allergen associated with severe clinical symptoms in regions with high levels of olive pollen counts such as in Andalusia (Spain) .…”

Section: Introductionmentioning

confidence: 99%

New insights into the sensitization to nonspecific lipid transfer proteins from pollen and food: New role of allergen Ole e 7

Oeo-Santos

Navas

Benedé

et al. 2019

Allergy

Self Cite

View full text Add to dashboard Cite

Background Ole e 7 is a nonspecific lipid transfer protein (nsLTP) from olive pollen, one of the main allergenic pollens worldwide. This allergenic nsLTP is responsible for severe symptoms in regions with high olive pollen exposure, where many Ole e 7‐sensitized patients exhibit a co‐sensitization to the peach nsLTP, Pru p 3. However, there is no evidence of cross‐reactivity, which explains this observed co‐sensitization. Therefore, the purpose of this study was to explore the relationship between Ole e 7 and Pru p 3. Methods A total of 48 patients sensitized to Ole e 7 and/or Pru p 3 were included in the study. Specific IgE serum levels were measured by ImmunoCAP 250 and ELISA. Inhibition assays were performed to determine the existence of cross‐reactivity between both nsLTPs. Allergic response was analyzed ex vivo (basophil activation test) and in vitro (RBL‐2H3 mast cell model). Results Common IgG and IgE epitopes were identified between both allergens. IgE‐binding inhibition was detected in Ole e 7–monosensitized patients using rPru p 3 as inhibitor, reaching inhibition values of 25 and 100%. Ex vivo and in vitro assays revealed a response against rPru p 3 in four (31%) Ole e 7–monosensitized patients. Conclusions Our results suggest that Ole e 7 could play a new role as primary sensitizer in regions with high olive pollen exposure, leading to the peach nsLTP sensitization. This co‐sensitization process would occur because of the cross‐reactivity between Ole e 7 and Pru p 3 observed in some allergic patients.

show abstract

Section: Introductionmentioning

confidence: 99%

New insights into the sensitization to nonspecific lipid transfer proteins from pollen and food: New role of allergen Ole e 7

Oeo-Santos

Navas

Benedé

et al. 2019

Allergy

Self Cite

View full text Add to dashboard Cite

show abstract

“…The cyclophilins, including Asp f 11 and Asp f 27 ( 62 ), are structurally conserved pan-allergens able to elicit IgE-mediated hypersensitivity reactions ( 62 , 64 , 65 ). It was reported previously that the conserved N81–N149 region of Rhizopus oryzae cyclophilin Rhi o 2 (see Fig.…”

Section: Discussionmentioning

confidence: 99%

Biotinylated Surfome Profiling Identifies Potential Biomarkers for Diagnosis and Therapy of Aspergillus fumigatus Infection

Jia

Krüger

Blango

et al. 2020

mSphere

View full text Add to dashboard Cite

Aspergillus fumigatus is one of the most common airborne molds capable of causing mycoses and allergies in humans. During infection, fungal surface proteins mediate the first contact with the human immune system to evade immune responses or to induce hypersensitivity. Several methods have been established for surface proteomics (surfomics). Biotinylation coupled with liquid chromatography-tandem mass spectrometry (LC-MS/MS) identification of peptides is a particularly efficient method to identify the surface-exposed regions of proteins that potentially mediate interaction with the host. After biotinylation of surface proteins during spore germination, we detected 231 different biotinylated surface proteins (including several well-known proteins such as RodA, CcpA, and DppV; allergens; and heat shock proteins [HSPs]), as well as some previously undescribed surface proteins. The dynamic change of the surface proteome was illustrated by detection of a relatively high number of proteins exclusively at one developmental stage. Using immunofluorescence microscopy, we confirmed the surface localization of several HSPs of the HSP70 family, which may have moonlighting functions. Collectively, by comparing our data with data representative of previously published A. fumigatus surface proteomes, our study generated a comprehensive data set corresponding to the A. fumigatus surfome and uncovered the surface-exposed regions of many proteins on the surface of conidia or hyphae. These surface-exposed regions are candidates for direct interaction with host cells and may represent antigenic epitopes that either induce protective immune responses or mediate immune evasion. Thus, our data sets provided and compiled here represent reasonable immunotherapy and diagnostic targets for future investigations. IMPORTANCE Aspergillus fumigatus is the most important airborne human-pathogenic mold, capable of causing both life-threatening invasive pulmonary aspergillosis in immunocompromised patients and allergy-inducing infections in individuals with atopic allergy. Despite its obvious medical relevance, timely diagnosis and efficient antifungal treatment of A. fumigatus infection remain major challenges. Proteins on the surface of conidia (asexually produced spores) and mycelium directly mediate host-pathogen interaction and also may serve as targets for diagnosis and immunotherapy. However, the similarity of protein sequences between A. fumigatus and other organisms, sometimes even including the human host, makes selection of targets for immunological-based studies difficult. Here, using surface protein biotinylation coupled with LC-MS/MS analysis, we identified hundreds of A. fumigatus surface proteins with exposed regions, further defining putative targets for possible diagnostic and immunotherapeutic design.

show abstract

“…The rabbit polyclonal antiserum against Ole e 15 (Ole e 15-specific pAb) was previously obtained 8 .…”

Section: Methodsmentioning

confidence: 99%

“…To date, a total of fifteen olive allergens (Ole e 1 to 15) have been identified 5–7 . Besides, an extensive proteomic profiling of olive pollen has been recently reported, making this important allergenic source one of the best characterized 8 .…”

Section: Introductionmentioning

confidence: 99%

“…Ole e 15, as well as other plant pollen allergenic cyclophilins, like Bet v 7 from birch and Cat r 1 from periwinkle, belong to the subgroup of divergent cyclophilins, which present a conserved Glu83 residue, two invariable cysteines and an additional stretch of seven amino acids with the consensus sequence XXGKXLH called divergent loop 20 . These allergens have also been shown to cross react with cyclophilins from plants 8,17,21 , animals (including human) 8 and molds 17,21 .…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Ole e 15 and its human counterpart -PPIA- chimeras reveal an heterogeneous IgE response in olive pollen allergic patients

Segundo‐Acosta

Oeo-Santos

Navas

et al. 2019

Sci Rep

Self Cite

View full text Add to dashboard Cite

Olive pollen is a major cause of immunoglobulin E (IgE)-mediated allergy in Mediterranean countries. It is expected to become a worldwide leading allergenic source because olive cultivation is increasing in many countries. Ole e 15 belongs to the cyclophilin pan-allergen family, which includes highly cross-reactive allergens from non-related plant, animal and mold species. Here, the amino acid differences between Ole e 15 and its weak cross-reactive human homolog PPIA were grafted onto Ole e 15 to assess the contribution of specific surface areas to the IgE-binding. Eight Ole e 15-PPIA chimeras were produced in E. coli, purified and tested with 20 sera from Ole e 15-sensitized patients with olive pollen allergy by ELISA experiments. The contribution of linear epitopes was analyzed using twelve overlapping peptides spanning the entire Ole e 15 sequence. All the patients displayed a diverse reduction of the IgE-reactivity to the chimeras, revealing a highly polyclonal and patient-specific response to Ole e 15. IgE-epitopes are distributed across the entire Ole e 15 surface. Two main surface areas containing relevant conformational epitopes have been characterized. This is the first study to identify important IgE-binding regions on the surface of an allergenic cyclophilin.

show abstract

Delineation of the Olive Pollen Proteome and Its Allergenome Unmasks Cyclophilin as a Relevant Cross-Reactive Allergen

Cited by 22 publications

References 70 publications

New insights into the sensitization to nonspecific lipid transfer proteins from pollen and food: New role of allergen Ole e 7

New insights into the sensitization to nonspecific lipid transfer proteins from pollen and food: New role of allergen Ole e 7

Biotinylated Surfome Profiling Identifies Potential Biomarkers for Diagnosis and Therapy of Aspergillus fumigatus Infection

Ole e 15 and its human counterpart -PPIA- chimeras reveal an heterogeneous IgE response in olive pollen allergic patients

Contact Info

Product

Resources

About