Structural and allergenic properties of the fatty acid binding protein from shrimp Litopenaeus vannamei.

BACKGROUND: The shrimp Litopenaeus vannamei is an important source of food allergens but its allergenic repertoire is poorly characterized. Cross-reactivity between crustacean and mites has been reported, with tropomyosin, the most relevant allergen involved. The aim of this study was to investigate the structural and immunological properties of a recombinant Fatty Acid Binding Protein (FABP) family from L. vannamei (LvFABP). METHODS: ELISA, skin prick test (SPT) and basophil activation assays were performed to determine IgE reactivity and allergenic activity of LvFABP. LC-MS/MS and Circular Dichroism experiments were done for structural analysis. B-cell epitope mapping with overlapping peptides, and cross-inhibition studies using human sera were done to identify antigenic regions and cross-reactivity. RESULTS: The recombinant LvFABP bound serum IgE from 27% of 36 shrimp allergic patients and showed allergenic activity when tested for basophil activation and SPT in a selected number of them. CD-spectroscopy of LvFABP revealed that the protein is folded with a secondary structure composed of mainly ß-strands and a smaller fraction of α helices. This is consistent with molecular modelling results, which exhibit a typical ß barrel fold with two α-helices and ten ß-strands. Epitope mapping identified two IgE-binding antigenic regions and inhibition assays found high cross-reactivity between LvFABP and Blo t 13, mediated by the antigenic region involving amino acids 54 to 72. CONCLUSIONS: Our results show that LvFABP is a shrimp allergen that cross reacts with the house dust mite allergen Blo t 13 and has allergenic activity, which suggest that it could be clinically relevant in case of shellfish allergy. This new allergen, named Lit v 13, will also help to understand basic mechanisms of sensitization to shrimp.

Identification of B Cell Epitopes of Blo t 13 Allergen and Cross-Reactivity with Human Adipocytes and Heart Fatty Acid Binding Proteins.

Cross-reactivity between allergens and human proteins could have a clinical impact in allergic diseases. Blo t 13 is an allergen from the mite Blomia tropicalis, which belongs to the fatty acid binding protein (FABP) family and has structural homology with human FABPs. This work aimed to map B cell epitopes on Blo t 13 and to identify epitopes involved in cross-reactivity with human heart FABP (FABP3) and adipocyte FABP (FABP4). Sera from 25 patients with house dust mite (HDM) allergy that were sensitized to Blo t 13 were used for testing the reactivity of immunoglobulin E (IgE) and IgG to FABP. The epitope mapping of Blo t 13 was performed using overlapping peptides, and cross-reactivity between Blo t 13 and human FABP was analyzed using human sera and anti-Blo t 13 monoclonal antibodies. IgE antibodies to all FABPs were detected in 14/25 serum samples, and IgG was detected in 25/25 serum samples. The cross-reactivity of Blo t 13 was 42% with FABP3 and 48% with FABP4. Two IgE-binding regions were identified in Blo t 13; one between residues 54 and 72 (the main cross-reacting region) and another between residues 111 to 129. Our results suggest that exposure to the Blo t 13 allergen could induce an auto-reactive response to endogenous FABP in allergic patients sensitized to Blo t 13.

An Engineered Hybrid Protein from Dermatophagoides pteronyssinus Allergens Shows Hypoallergenicity.

The house dust mite (HDM) Dermatophagoides pteronyssinus is an important risk factor for asthma and rhinitis. Allergen specific immunotherapy that is based on recombinant proteins has been proposed for the safer and more efficient treatment of allergic diseases. The aim of this study was to design and obtain a hybrid protein (DPx4) containing antigenic regions of allergens Der p 1, Der p 2, Der p 7, and Der p 10 from this mite. DPx4 was produced in Escherichia coli and its folding was determined by circular dichroism. Non-denaturing dot-blot, ELISA, basophil activation test, dot blot with monoclonal antibodies, ELISA inhibition, and cysteine protease activity assays were performed. Mice that were immunized with DPx4 were also analyzed. We found that DPx4 had no cysteine protease activity and it showed significantly lower IgE reactivity than Der p 1, Der p 2, and D. pteronyssinus extract. DPx4 induced lower basophil activation than Der p 2 and the allergen extract. Immunized mice produced IgG antibodies that inhibited the binding of allergic patient's IgE to the allergen extract and induced comparatively higher levels of IL-10 than the extract in peripheral blood mononuclear cells (PBMC) culture. These results suggest that DPx4 has immunological properties that are useful for the development of a mite allergy vaccine.

[In silico analysis of molecular mimicry between human aquaporin 3, Aspergillus fumigatus aquaporin and aquaporins from allergic sources]. / Análisis en silico del mimetismo molecular entre acuaporina 3 humana y Aspergillus fumigatus: implicaciones para el potencial de reactividad cruzada.

OBJECTIVE: Conduct an in-silico assessment of potential molecular mimicry between human aquaporins, A. fumigatus, and diverse allergenic sources. METHODS: Amino acid sequences of human AQP3 and A. fumigatus aquaporin were compared through multiple alignments with 25 aquaporins from diverse allergenic sources. Phylogenetic analysis and homology-based modeling were executed, and the ElliPro server predicted conserved antigenic regions on 3D structures. RESULTS: Global identity among studied aquaporins was 32.6%, with a specific conserved local region at 71.4%. Five monophyletic clades (A-E) were formed, and Group B displayed the highest identity (95%), including 6 mammalian aquaporins, notably AQP3. A. fumigatus aquaporin exhibited the highest identity with Malassezia sympodialis (35%). Three linear and three discontinuous epitopes were identified in both human and A. fumigatus aquaporins. The Root Mean Square Deviation (RMSD) from overlapping aquaporin structures was 1.006. CONCLUSION: Identification of potential linear and conformational epitopes on human AQP3 suggests likely molecular mimicry with A. fumigatus aquaporins. High identity in a specific antigenic region indicates potential autoreactivity and a probable antigenic site involved in cross-reactivity. Validation through in vitro and in vivo studies is essential for further understanding and confirmation.

OBJETIVO: Realizar una evaluación in silico del posible mimetismo molecular entre las acuaporinas humanas, A. fumigatus y diversas fuentes alergénicas. MÉTODOS: Se compararon secuencias de aminoácidos de AQP3 humana y acuaporina de A. fumigatus mediante alineamientos múltiples con 25 acuaporinas de diversas fuentes alergénicas. Se ejecutaron análisis filogenéticos y modelos basados en homología, y el servidor ElliPro predijo regiones antigénicas preservadas en estructuras 3D. RESULTADOS: La identidad global entre las acuaporinas estudiadas fue del 32.6%, con una región local específica preservada en el 71.4%. Se formaron cinco clados monofiléticos (A-E), y el grupo B mostró la identidad más alta (95%), incluidas 6 acuaporinas de mamíferos, en particular AQP3. A. fumigatus aquaporin exhibió la mayor identidad con Malassezia sympodialis (35%). Se identificaron tres epítopos lineales y tres discontinuos en acuaporinas tanto humanas como de A. fumigatus. La desviación cuadrática media (RMSD) de las estructuras de acuaporinas superpuestas fue de 1,006. CONCLUSIÓN: La identificación de posibles epítopos lineales y conformacionales en AQP3 humano sugiere un probable mimetismo molecular con acuaporinas de A. fumigatus. La identidad alta en una región antigénica específica indica autorreactividad potencial y un sitio antigénico probable implicado en la reactividad cruzada. La validación mediante estudios in vitro e in vivo es desicivo para una mayor comprensión y confirmación.

Potential contribution of Helicobacter pylori proteins in the pathogenesis of type 1 gastric neuroendocrine tumor and urticaria. In silico approach.

BACKGROUND: Helicobacter pylori has been linked to several diseases such as chronic urticaria, gastritis, and type 1 gastric neuroendocrine tumors (type 1 gNET). Although these diseases seem to have different mechanisms, their relationship with H. pylori suggests a common inflammatory pathway. OBJECTIVE: To identify potential cross-reactive antigens between H. pylori and humans involved in chronic urticaria and type 1 gNET. METHODS: Alignment was carried out among human proteins associated with urticaria (9 proteins), type 1 gNET (32 proteins), and H. pylori proteome. We performed pairwise alignment among the human and H. pylori antigens with PSI-BLAST. Modeling based on homology was done with the Swiss model server and epitope prediction with the Ellipro server. Epitopes were located on a 3D model using PYMOL software. RESULTS: The highest conserved sequence was found between the human HSP 60 antigen and the H. pylori chaperonin GroEL with an identity of 54% and a cover of 92%, followed by the alpha and gamma enolases and two H. pylori phosphopyruvate hydratase, both with an identity and cover of 48% and 96%, respectively. The H/K ATPase (Chain A) showed high identity with two H. pylori proteins (35.21% with both P-type ATPase), but with low cover (only 6%). We observed eight linear and three discontinuous epitopes for human HSP 60 and three lineal and one discontinuous epitope for both alpha-enolase and gamma enolase, high conserved with H. pylori sequences. CONCLUSION: Some type 1 gNET antigens shared potential cross-reactive epitopes with H. pylori proteins, suggesting that molecular mimicry could be a mechanism that explains the relationship between the infection and this disease. Studies evaluating the functional impact of this relationship are needed.

[Hevea brasiliensis como fuente alergénica: revisión bibliográfica].

Abstract: La planta Hevea brasiliensis se utiliza ampliamente en la industria como fuente de extracción de caucho, un elemento empleado en diversas áreas comerciales y médicas. Los estudios inmunológicos de esta especie indican que es una fuente alergénica importante, que puede provocar sensibilización y alergia. Se han identificado diferentes componentes alergénicos de esta planta, con diversas propiedades inmunitarias y bioquímicas, y estudiado más de diez tipos diferentes de alérgenos, cada uno con distinta capacidad de inducir síntomas alérgicos. En esta revisión informamos los avances actuales en el estudio de Hevea brasiliensis.

Resumen: Hevea brasiliensis, a plant species used extensively for rubber extraction, is a common allergenic source that can cause sensitization and allergic reactions. Recent immunological studies have characterized various allergenic components of Hevea brasiliensis that possess diverse immune and biochemical properties. Over ten types of allergens have been identified, each with varying capacities to induce allergic symptoms. This review presents the current advances in the study of this allergenic source.

Increased incidence of rheumatoid arthritis after COVID-19.

An increase in the incidence of inflammatory arthritis after COVID-19 has been reported. Since many diseases exhibit population-specific causal effect sizes, we aimed to evaluate the incidence trends of inflammatory arthritis, including rheumatoid arthritis (RA), after COVID-19 in a large admixed Colombian population. Data analysis for this retrospective, population-based cohort study was carried out using the COOSALUD EPS registry. The following codes were selected for analyses: M059, seropositive RA, M069, unspecified RA, M060 seronegative RA, and other RA-related diagnoses: M064, M139, M068, M058, M130 and M053. The study period was limited to January 01, 2018, through December 31, 2022. Incidence rates (IRs) and incidence rate ratios (IRRs) were assessed. A Cox survival model was built to evaluate the influence of age, gender, and COVID-19 vaccination status on the development of inflammatory arthritis. A bioinformatic analysis was performed to evaluate the homology between SARS-CoV-2 and autoantigen peptides related to RA. The entire population study comprised 3,335,084 individuals. During the pandemic period (2020-2022) the total IIR for seropositive and unspecified RA were 1.60 (95% CI, 1.16-2.22) and 2.93 (95% CI, 2.04-4.19), respectively, and the IIR for overall RA-related diagnosis was 2.01 (95% CI 1.59-2.53). The age groups hazard ratios (HRs) were increased until the age group of 51-60 years (HR: 9.16; 95% CI, 7.24-11.59) and then decreased slightly in the age group 61 years or older (HR: 5.364; 95% CI, 4.24-6.78) compared to those within 18-30 years. Men were less at risk than women to develop inflammatory arthritis (HR: 0.21; 95% CI, 0.18-0.24). The greater time since COVID-19 diagnosis was associated with a lower likelihood of developing inflammatory arthritis (HR: 0.99; 95% CI:0.998-0.999). Vaccination (all types of COVID-19 vaccines included) did not prevent the development of inflammatory arthritis after COVID-19. Low identity was found between the SARS-CoV-2 ORF1ab antigen and the human antigens Poly ADP-ribose polymerase 14 and Protein mono-ADP-ribosyltransferase PARP9 isoform D (39% and 29%, respectively). In conclusion, our study confirms increased incidence of inflammatory arthritis, including RA, after COVID-19, with the greatest increase occurring before the first year post-covid. Women in their fifties were more susceptible. Further research is required to examine the effectiveness of vaccination in preventing post-COVID inflammatory arthritis and the mechanisms implicated in the development of RA after COVID-19.

In silico analysis of cross reactivity among phospholipases from Hymenoptera species.

Background: Phospholipases are enzymes with the capacity to hydrolyze membrane lipids and have been characterized in several allergenic sources, such as hymenoptera species. However, cross-reactivity among phospholipases allergens are little understood. The objective of this study was to determine potential antigenic regions involved in cross-reactivity among allergens of phospholipases using an in silico approach. Methods: In total, 18 amino acids sequences belonging to phospholipase family derived from species of the order hymenoptera were retrieved from the UniProt database to perform phylogenetic analysis to determine the closest molecular relationship. Multialignment was done to identify conserved regions and matched with antigenic regions predicted by ElliPro server. 3D models were obtained from modeling by homology and were used to locate cross-reactive antigenic regions. Results: Phylogenetic analysis showed that the 18 phospholipases split into four monophyletic clades (named here as A, B, C and D). Phospholipases from A clade shared an amino acid sequences' identity of 79%. Antigenic patches predicted by Ellipro were located in highly conserved regions, suggesting that they could be involved in cross-reactivity in this group (Ves v 1, Ves a 1 and Ves m 1). Conclusions: At this point, we advanced to the characterization of potential antigenic sites involved in cross-reactivity among phospholipases. Inhibition assays are needed to confirm our finding.

Presence of IgE Autoantibodies Against Eosinophil Peroxidase and Eosinophil Cationic Protein in Severe Chronic Spontaneous Urticaria and Atopic Dermatitis.

PURPOSE: Eosinophils are frequently found in atopic dermatitis (AD) and chronic spontaneous urticaria (CSU) that release eosinophil peroxidase (EPX) and eosinophil cationic protein (ECP). Continuous exposure to these proteins could trigger an autoimmune response which may contribute to the pathogenesis and severity of skin inflammation. In this study, we investigate the immunoglobulin E (IgE) response against eosinophil proteins in CSU and AD. METHODS: We recruited patients with severe AD, severe CSU and healthy subjects to explore the presence of IgE autoantibodies and cross-reactivity against EPX, ECP and thyroid peroxidase (TPO). The potential cross-reactive epitopes among the peroxidase family were determined using in silico tools. RESULTS: The frequencies of anti-EPX IgE (28.8%) and anti-ECP IgE (26.6%) were higher in the AD group, and anti-TPO IgE was higher in the CSU group (27.2%). In the CSU group, there was a correlation between the anti-EPX IgE and anti-TPO IgE levels (r = 0.542, P < 0.001); TPO inhibited 42% of IgE binding to EPX, while EPX inhibited 59% of IgE binding to TPO, suggesting a cross-reactivity with EPX as a primary sensitizer. There was greater inhibition when we used a pool of sera CSU and AD, TPO inhibited 52% of IgE binding to EPX, while EPX inhibited 78% of IgE binding to TPO. In silico analysis showed a possible shared epitope in the peroxidase protein family. CONCLUSIONS: IgE against eosinophil proteins may contribute to chronic inflammation in patients with AD and CSU. Cross-reactivity between EPX and TPO could explain thyroid problems in CSU patients.

Identification of antigenic epitopes of thyroperoxidase, thyroglobulin and interleukin-24. Exploration of cross-reactivity with environmental allergens and possible role in urticaria and hypothyroidism.

BACKGROUND: Human proteins such as interleukin-24 (IL24), thyroperoxidase (TPO) and thyroglobulin (Tg) are targets of IgE or IgG autoantibodies. Why these proteins are recognized by autoantibodies in some patients with chronic spontaneous urticaria (CSU) or hypothyroidism is unknown. OBJECTIVE: Through in silico analysis, identify antigen patches of TPO, Tg and IL24 and compare the sequences of these human proteins with some prevalent allergens. METHODS: The amino acids sequences of IL24, thyroperoxidase and thyroglobulin were compared between them and with 22 environmental allergens. Phylogenetic studies and multiple pairing were carried out to explore the degree of protein identity and cover. The proteins without 3D structure reported in the database, were modeled by homology with "Swiss Modeller" and compared through PYMOL. Residues conserved and accessible to the solvent (rASA> 0.25) were located in the 3D model to identify possible areas of cross-reactivity and antigen binding. RESULTS: We build a 3D model of the TPO and thyroglobulin protein base on proteins closely related. Five epitopes for TPO, six for IL24 and six for thyroglobulin were predicted. The amino acid sequences of allergens from different sources (Dermatophagoides pteronyssinus, Blomia tropicalis, Betula verrucosa, Cynodon dactylon, Aspergillus fumigatus, Canis domesticus, Felis domesticus) were compared with human TPO, Tg and IL24. The cover and alignments between allergens and human proteins were low. CONCLUSION: We identify possible linear and conformational epitopes of TPO, Tg and IL24 that could be the target of IgE or IgG binding in patients with urticaria or hypothyroidism; These epitopes do not appear to be present among common environmental allergens, suggesting that autoreactivity to these human proteins are not by cross-reactivity.

Nasal Provocation Test with Cat and Dog Extracts: Results according to Molecular Components.

BACKGROUND: IgE sensitization (atopy) to pets is commonly evaluated using pet dander extracts. However, the diagnosis by components seems to be more adequate to evaluate the clinical relevance (allergy) of sIgE sensitization. OBJECTIVE: To study the association between IgE sensitization to pet allergen components and clinical symptoms. Methodology. Dander extracts and sIgE levels to pet components (Can f 1, Can f 2, Can f 3, Can f 5, Fel d 1, Fel 2, and Fel 4) were measured in a rhinitis group (n = 101) and a control group (n = 101) and a control group (. RESULTS: Dog (34.6% vs. 23.5%) and cat dander (26.7% vs. 8.8%, p = 0.05) IgE sensitization was frequent among rhinitis and no-rhinitis subjects, and it was similar to dog (29.7% vs. 20.5%) and cat (18.8% vs. 8.8%) components. Polysensitization for dog (3.1, 95% CI: 1.5 to 6.1, p = 0.05) IgE sensitization was frequent among rhinitis and no-rhinitis subjects, and it was similar to dog (29.7% vs. 20.5%) and cat (18.8% vs. 8.8%) components. Polysensitization for dog (3.1, 95% CI: 1.5 to 6.1, p = 0.05) IgE sensitization was frequent among rhinitis and no-rhinitis subjects, and it was similar to dog (29.7% vs. 20.5%) and cat (18.8% vs. 8.8%) components. Polysensitization for dog (3.1, 95% CI: 1.5 to 6.1. CONCLUSIONS: Sensitization to pet dander extract identifies atopic patients, but its utility to predict clinical relevance is poor. Allergenic components could help to define the clinical relevance of sensitization to furry animals and could reduce the need for provocation test.

In silico analysis of a major allergen from Rattus norvegicus, Rat n 1, and cross-reactivity with domestic pets.

Background: Lipocalins play a role in the cellular trafficking of pheromones and are involved in allergic responses to domestic pets. However, the cross-reactivity among allergens of this group has been poorly explored, and the pheromone linking capacity is not well characterized. The aim of this study was to explore cross-reactive epitopes and pheromone linking capacity among Rat n 1 and homologues in domestic pets through an in silico approach. Methods: ElliPro and BepiPred in silico tools were used to predict B cell linear and cross-reactive epitopes. The pheromone linking capacity was explored by docking virtual screening with 2-ethylhexanol, 2,5-dimethylpyrazine, 2-sec-butyl-4,5-dihydrothiazole, and 2-heptanone ligands. Results: According to the analysis, Rat n 1 shares 52% identity with Equ c 1, Can f 6, Fel d 4, and Mus m 1 allergens. The overlapping structures analysis  revealed high structural homology (root mean square deviation < 1). Four lineal and three discontinuous epitopes were predicted on Ra t n 1. A lineal epitope located between amino acids residues 24 and 36 was highly conserved on all allergens explored. A cross-reactive discontinuous epitope (T142, K143, D144, L145, S146, S147, D148, K152, L170, T171, T173, D174) was also found. Docking molecular simulations revealed the region involved in linking ligands, and we identified the properties of the binding of four pheromones and the binding potential of Rat n 1. Critical residues for interactions are reported in this study. Conclusions: We identified some possible allergens from Rattus norvegicus, and those allergens could have cross-reactivity with allergens from some animals. The results need to be confirmed with in vitro studies and could be utilized to contribute to immunotherapy and reduce allergic diseases related to lipocalins.

[The phylogenetic relationship of Glyciphagidae, Pyroglyphidae, Chortoglyphidae and Acaridae mites families according to the sequence of their main allergens]. / Relación filogenética de ácaros Glyciphagidae, Pyroglyphidae, Chortoglyphidae y Acaridae, según la secuencia de sus alérgenos.

BACKGROUND: Mites are the main cause of atopy and allergies in the Tropical region. It is necessary to know the phylogenetic relationship of their allergenic proteins in order to determine the best combination of extracts for its use at the clinic. OBJECTIVE: To assess the phylogenetic relationship between the main allergenic proteins of mites. METHODS: Groups 1, 2 and 5 of Glyciphagidae, Pyroglyphidae, Chortoglyphidae and Acaridae families were compared according to the sequence of mRNA and amino acids with the validated sequences of the National Center for Biotechnology Information and through bioinformatic alignment analyses for the construction of the trees, the method of neighbor-joining, with bootstrap support with 500 replications, was used as a measure of reliability and robustness. RESULTS: 15% to 87% of identity was found in the three groups of allergens; the highest was between Der p2 and Der f2 (86.98%) and, the lowest, between Der f 5 and Gly d 5 (17.87%) Piroglyphidae showed the highest relationship between the species. The longest branching distance was identified in Glicyphagidae, especially in Blomia tropicalis. CONCLUSION: Some allergenic proteins have a high identity between the different species of mites, unlike Blomia tropicalis. These results can be taken into consideration when the diagnosis and treatment of allergic diseases is being defined.

Antecedentes: Los ácaros son la principal causa de atopía y alergias en la región del trópico. Es necesario conocer la relación filogenética de sus proteínas alergénicas para determinar la mejor combinación de extractos para su empleo en la clínica. Objetivo: Evaluar la relación filogenética entre las principales proteínas alergénicas de los ácaros. Método: Se compararon los grupos 1, 2 y 5 de las familias Glyciphagidae, Pyroglyphidae, Chortoglyphidae y Acaridae de acuerdo con la secuencia de ARNm y aminoácidos con las secuencias validadas en el National Center for Biotechnology Information y mediante análisis bioinformáticos de alineamiento. Para la construcción de los árboles se utilizó el método de neighbor-joining, con soporte por bootstrap con 500 replicaciones como medida de fiabilidad y robustez. Resultados: Se encontró 15 a 87 % de identidad en los tres grupos de alérgenos; la más alta entre Der p 2 y Der f 2 (86.98 %) y la menor entre Der f 5 y Gly d 5 (17.87 %) Piroglyphidae presentó la mayor relación entre las especies. En Glicyphagidae, especialmente en Blomia tropicalis, se identificó la mayor distancia de ramificación. Conclusión: Algunas proteínas alergénicas tienen alta identidad entre las diferentes especies de ácaros, no así Blomia tropicalis. Estos resultados pueden considerarse al definir el diagnóstico y tratamiento de las enfermedades alérgicas.

Allergy to Mus m 1: Allergy to Mus m 1: A review of structural, and immunological features.

The prevalence of allergies to pets has been increasing over the past decades. Some of the most important animal-derived allergens are members of the lipocalin protein family, which are found in dander, saliva, and urine. These allergens disperse effectively and are widely present in indoor environments. Exposure to high levels of mouse urinary protein (Mus m 1, hereinafter called 'mouse allergen') has been previously linked to sensitization to mouse, and indicators of asthma severity or control in some studies. To date, this is the only known mouse allergen registered in the IUIS database. This allergen is responsible for 27% of the total T cell response, confirming the dominant role it plays in mouse allergy. Mice have a worldwide distribution affecting both rural and urban areas; hence humans are frequently exposed to mouse-derived proteins. Additionally, exposure to mouse allergens has increased since they are more frequently being made pets, and in addition, exposure of laboratory animal care personnel to mice has been associated with a high risk of developing occupational allergies. Mus m 1 has been recognized as the main mouse allergen, and several studies suggest its clinical relevance. What makes Mus m 1 such an important allergen? In this review, we explored its structural, immunological, and clinical features.

[Shrimp as an allergen source]. / El camarón como una fuente de alérgenos.

Allergy to shellfish is one of the most prevalent food allergies in several countries, especially the one induced by consuming or having contact with shrimp. Several shrimp species are known to induce allergy diseases. However, the whole spectrum of allergens they contain is unknown and few of them have been completely characterized. This study was done in order to know the recent advances in the characterization of shrimp allergens and its relationship with allergens from other arthropods of importance in allergic diseases. We emphasize the species Litopenaeus vannamei , the most consumed shrimp in Colombia. Well characterized shrimp allergens are named following an official classification; nevertheless, they are better known according to the biological function associated with them. Tropomiosin, the main and most studied allergen in different shrimp species, is involved in crossreactivity among shrimp and other arthropods like domestic mites. The other characterized allergens seem to have a minor participation in this cross-reactivity. The allergenic potential of L. vannamei is not well known and few of its allergens have been characterized, whilst others that were recently identified such as the hemocyanin and the fatty acid binding proteins are beginning to be studied. Preliminary results suggest that these allergens are involved in the cross-reactivity between shrimp and domestic mites, which deserves further evaluation. The molecular and immunological characterization of all allergens present in shrimp would help understanding its allergenic role.

El camarón como una fuente de alérgenos / Shrimp as an allergen source

La alergia a los mariscos es una de las alergias alimentarias de mayor prevalencia en muchos países, especialmente la inducida por el consumo o contacto con los camarones. A varias especies de camarón se les conoce la capacidad de inducir alergias; sin embargo, el conjunto de alérgenos que producen no se conoce y pocos de ellos se han caracterizado completamente. Este trabajo se llevó a cabo para conocer los avances recientes en la caracterización de los alérgenos del camarón y su relación con alérgenos de otros artrópodos de importancia en las alergias. Se hace énfasis en la especie Litopenaeus vannamei , la de mayor consumo en Colombia. A los alérgenos de los camarones mayormente caracterizados se les nombra según la nomenclatura oficial, aunque se les conoce más por la función biológica asociada. La tropomiosina, el alérgeno principal y más estudiado en diferentes especies de camarón, participa en la reacción cruzada entre el camarón y otros artrópodos, como los ácaros domésticos. Los otros alérgenos caracterizados parecen contribuir poco en este tipo de reacción. El potencial alergénico del camarón L. vannamei no está completamente dilucidado y unos pocos de sus alérgenos se han caracterizado, mientras que otros recientemente identificados, como la hemocianina y las proteínas de unión a ácidos grasos, se empiezan a investigar. Los resultados preliminares sugieren que participan en la reacción cruzada entre el camarón y los ácaros. La caracterización molecular e inmunológica del conjunto de alérgenos presentes en el camarón, ayudaría a conocer mejor su papel alergénico.

Allergy to shellfish is one of the most prevalent food allergies in several countries, especially the one induced by consuming or having contact with shrimp. Several shrimp species are known to induce allergy diseases. However, the whole spectrum of allergens they contain is unknown and few of them have been completely characterized. This study was done in order to know the recent advances in the characterization of shrimp allergens and its relationship with allergens from other arthropods of importance in allergic diseases. We emphasize the species Litopenaeus vannamei , the most consumed shrimp in Colombia. Well characterized shrimp allergens are named following an official classification; nevertheless, they are better known according to the biological function associated with them. Tropomiosin, the main and most studied allergen in different shrimp species, is involved in crossreactivity among shrimp and other arthropods like domestic mites. The other characterized allergens seem to have a minor participation in this cross-reactivity. The allergenic potential of L. vannamei is not well known and few of its allergens have been characterized, whilst others that were recently identified such as the hemocyanin and the fatty acid binding proteins are beginning to be studied. Preliminary results suggest that these allergens are involved in the cross-reactivity between shrimp and domestic mites, which deserves further evaluation. The molecular and immunological characterization of all allergens present in shrimp would help understanding its allergenic role.