CHARLOTTESVILLE, VA, United States

Indoor Biotechnologies

www.inbio.com
CHARLOTTESVILLE, VA, United States

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Grant
Agency: European Commission | Branch: FP7 | Program: CP-TP | Phase: KBBE.2012.2.4-04 | Award Amount: 12.16M | Year: 2013

Up to 20 million European citizens suffer from food allergy. However management of both food allergy (by patients and health practitioners) and allergens (by industry) is thwarted by lack of evidence to either prevent food allergy developing or protect adequately those who are already allergic. iFAAM will develop evidence-based approaches and tools for MANAGEMENT of ALLERGENS in FOOD and integrate knowledge derived from their application and new knowledge from intervention studies into FOOD ALLERGY MANAGEMENT plans and dietary advice. The resulting holistic strategies will reduce the burden of food allergies in Europe and beyond, whilst enabling the European food industry to compete in the global market place. Our approach will build on e-Health concepts to allow full exploitation of complex data obtained from the work in this proposal and previous and ongoing studies, maximising sharing and linkage of data, by developing an informatics platform Allerg-e-lab. This will enable us to (1) Extend and integrate existing cohorts from observation and intervention studies to provide evidence as to how maternal diet and infant feeding practices (including weaning) modulate the patterns and prevalence of allergies across Europe (2) Establish risk factors for the development of severe reactions to food and identify associated biomarkers (3) Develop a clinically-validated tiered risk assessment and evidence-based risk management approach for food allergens for allergens in the food chain (4) Develop clinically-relevant multi-analyte methods of analysis suited to allergen management across the food chain Stakeholders will be integrated into iFAAM to deliver harmonised integrated approaches, including RISK ASSESSORS AND MANAGERS managing population risk, the FOOD INDUSTRY who manage allergens to ensure consumer safety, HEALTH CARE PRACTITIONERS to provide food allergy management plans and dietary advice and ALLERGIC CONSUMERS to manage individual risk.


Romeo M.J.,University of Virginia | Agrawal R.,University of Virginia | Pomes A.,Indoor Biotechnologies | Woodfolk J.A.,University of Virginia
Journal of Allergy and Clinical Immunology | Year: 2014

The cytokines IL-4, IL-13, and thymic stromal lymphopoietin play a key role in allergic disease by virtue of their ability to initiate, maintain, and augment TH2 responses. These molecules mediate their effects through type 1 cytokine receptors, which bind cytokines with a characteristic structure. Receptors are expressed on a broad array of immune cell types and are integral to complex cytokine networks operating in health and disease. T H2-promoting cytokines bind different configurations of receptors. Receptor subunits can exist in surface-bound or soluble forms, as well as in isolation or in partnership with other subunits. Sharing of receptor subunits among different cytokine receptor complexes adds to the intricate landscape. This article describes the characteristics of receptors for IL-4, IL-13, and thymic stromal lymphopoietin and their respective ligands from a structure-function perspective. We detail the mechanisms of receptor complex assembly, the interrelated nature of these receptors, and the effect on allergic inflammation. The ability for novel and atypical types of receptors to modulate inflammatory processes is also discussed. We highlight current and emerging treatments that target TH2-promoting receptor complexes. Understanding the molecular features of these receptors provides insight into different disease phenotypes and the variable clinical outcomes arising from targeted therapies. These considerations can be used to inform future directions for research and creative strategies for treating individual patients. © 2013 American Academy of Allergy, Asthma & Immunology.


Pomes A.,Indoor Biotechnologies | Arruda L.K.,University of Sao Paulo
Methods | Year: 2014

Cockroach allergy is an important health problem associated with the development of asthma, as a consequence of chronic exposure to low levels of allergens in susceptible individuals. In the last 20. years, progress in understanding the disease has been possible, thanks to the identification and molecular cloning of cockroach allergens and their expression as recombinant proteins. Assays for assessment of environmental allergen exposure have been developed and used to measure Bla g 1 and Bla g 2, as markers of cockroach exposure. IgE antibodies to cockroach extracts and to specific purified allergens have been measured to assess sensitization and analyze association with exposure and disease. With the development of the field of structural biology and the expression of recombinant cockroach allergens, insights into allergen structure, function, epitope mapping and allergen-antibody interactions have provided further understanding of mechanisms of cockroach allergic disease at the molecular level. This information will contribute to develop new approaches to allergen avoidance and to improve diagnosis and therapy of cockroach allergy. © 2013 Elsevier Inc.


Mueller G.A.,National Health Research Institute | Pedersen L.C.,National Health Research Institute | Lih F.B.,National Health Research Institute | Glesner J.,Indoor Biotechnologies | And 5 more authors.
Journal of Allergy and Clinical Immunology | Year: 2013

Background Sensitization to cockroach allergens is a major risk factor for asthma. The cockroach allergen Bla g 1 has multiple repeats of approximately 100 amino acids, but the fold of the protein and its biological function are unknown. Objective We sought to determine the structure of Bla g 1, investigate the implications for allergic disease, and standardize cockroach exposure assays. Methods nBla g 1 and recombinant constructs were compared by using ELISA with specific murine IgG and human IgE. The structure of Bla g 1 was determined by x-ray crystallography. Mass spectrometry and nuclear magnetic resonance spectroscopy were used to examine the ligand-binding properties of the allergen. Results The structure of an rBla g 1 construct with comparable IgE and IgG reactivity to the natural allergen was solved by x-ray crystallography. The Bla g 1 repeat forms a novel fold with 6 helices. Two repeats encapsulate a large and nearly spherical hydrophobic cavity, defining the basic structural unit. Lipids in the cavity varied depending on the allergen origin. Palmitic, oleic, and stearic acids were associated with nBla g 1 from cockroach frass. One unit of Bla g 1 was equivalent to 104 ng of allergen. Conclusions Bla g 1 has a novel fold with a capacity to bind various lipids, which suggests a digestive function associated with nonspecific transport of lipid molecules in cockroaches. Defining the basic structural unit of Bla g 1 facilitates the standardization of assays in absolute units for the assessment of environmental allergen exposure. © 2013 American Academy of Allergy, Asthma & Immunology.


Vredegoor D.W.,University Utrecht | Willemse T.,University Utrecht | Chapman M.D.,Indoor Biotechnologies | Heederik D.J.J.,University Utrecht | Krop E.J.M.,University Utrecht
Journal of Allergy and Clinical Immunology | Year: 2012

Background: Certain dog breeds are described and marketed as being "hypoallergenic" on the basis of anecdotal reports that these dogs are better tolerated by patients allergic to dogs. Objective: These observations were investigated by comparing Can f 1 (major dog [Canis familiaris] allergen) levels in hair and coat samples and in the home environment of various hypoallergenic (Labradoodle, Poodle, Spanish Waterdog, and Airedale terrier) and non-hypoallergenic dogs (Labrador retriever and a control group). Methods: Hair and coat samples were obtained from dogs, and settled floor and airborne dust samples were taken from the dogs' homes. Can f 1 concentrations were measured by using ELISA, and results were analyzed by using multiple linear regression analyses. Results: Significantly higher Can f 1 concentrations were found in hair and coat samples of hypoallergenic dogs (n 5 196, geometric mean [GM], 2.26 mgμg, geometric standard deviation [GSD], 0.73, and GM, 27.04 mgμg, GSD, 0.57, respectively) than of non-hypoallergenic dogs (n 5 160, GM, 0.77 mgμg, GSD, 0.71, and GM, 12.98 mgμg, GSD, 0.76, respectively). Differences between breeds were small, relative to the variability within a breed. Can f 1 levels in settled floor dust samples were lower for Labradoodles, but no differences were found between the other groups. No differences in airborne levels were found between breeds. Conclusion: So-called hypoallergenic dogs had higher Can f 1 levels in hair and coat samples than did control breeds. These differences did not lead to higher levels of environmental exposure to dog allergens. There is no evidence for the classification of certain dog breeds as being "hypoallergenic." (J Allergy Clin Immunol 2012;130:904-9. © 2012 American Academy of Allergy, Asthma & Immunology.


Pomes A.,Indoor Biotechnologies
International Archives of Allergy and Immunology | Year: 2010

The 3-dimensional structure of an allergen defines the accessible parts on the surface of the molecule or epitopes that interact with antibodies. Mapping the antigenic determinants for IgE antibody binding has been pursued through strategies based on the use of overlapping synthetic peptides, recombinant allergenic fragments or unfolded allergens. These approaches led to the identification of mostly linear epitopes and are useful for food allergens that undergo digestion or food processing. For inhaled allergens, conformational epitopes appear to be the primary targets of IgE responses. Knowledge of the molecular structure of allergens alone and in complex with antibodies that interfere with IgE antibody binding is important to understand the immune recognition of B cell-antigenic determinants on allergens and the design of recombinant allergens for immunotherapy. Starting with the molecular cloning and expression of allergens, and with the advent of X-ray crystallography and nuclear magnetic resonance techniques, we have been able to visualize conformational epitopes on allergens. © 2009 S. Karger AG, Basel.


Chapman M.D.,Indoor Biotechnologies | Briza P.,University of Salzburg
Current Allergy and Asthma Reports | Year: 2012

Molecular approaches to allergen standardization include the development of purified natural or recombinant allergen standards whose structural and allergenic properties have been validated, in tandem with certified immunoassays for allergen measurement. Purified allergens can be used individually or incorporated into multiple allergen standards. Multicenter international collaborative studies are required to validate candidate allergen standards and immunoassays, as a prelude to being approved by regulatory agencies. Mass spectrometry is a sophisticated and powerful proteomics tool that is being developed for allergen analysis. Recent results using pollen allergens show that mass spectrometry can identify and measure specific allergens in a complex mixture and can provide precise information of the variability of natural allergen extracts. In future, the combined use of immunoassays and mass spectrometry will provide complete standardization of allergenic products. Molecular standardization will form the basis of new allergy diagnostics and therapeutics, as well as assessment of environmental exposure, and will improve the quality of treatment options for allergic patients. © Springer Science+Business Media, LLC 2012.


Grant
Agency: Department of Health and Human Services | Branch: | Program: SBIR | Phase: Phase I | Award Amount: 184.27K | Year: 2013

DESCRIPTION (provided by applicant): Asthma is a serious public health problem in the US that affects one in ten schoolchildren and causes ~500,000 hospitalizations each year, with an estimated economic cost of 56 billion. Allergic sensitization to household allergens (dust mites, cat, dog, mouse, cockroach, molds) is a major risk factor for the development of asthma. Asthma in early childhood can also be influenced by exposure to bacterial products which may potentiate or have protective effects dependingon the level of environmental exposure and genetic factors. Recent studies in a mouse model have shown that the bacterial protein, flagellin, promotes allergic sensitization to indoor allergens and that human patients with asthma have high levels of antibodies to flagellin. Household dust samples have been shown to contain flagellin. However, investigation of the association between exposure to flagellin and asthma requires a robust test to measure flagellin in environmental samples from homes and public buildings. The goal of this SBIR Phase I project is to develop a high throughput immunoassay for flagellin, capable of analyzing several hundred samples per week. The specific aims of the project are i) to purify flagellin from Pseudomonas aeruginosa; ii) to develop a monoclonal or polyclonal antibody based immunoassay which detects flagellin from most bacterial species; iii) to validate the assay performance to measure flagellin in dust samples of known allergen and endotoxin content. The strategy involvesdeveloping a multiplexed immunoassay which can be used to measure flagellin, allergens and molds simultaneously. This assay will be to assess the role of flagellin exposure in allergic disease. Commercial potential: Successful completion of this SBIR willresult in valuable immunoassay product(s) that can be marketed by the applicant, Indoor Biotechnologies, to allergy/immunology researchers in academia, government agencies, pharmaceutical companies and vaccine manufacturers, worldwide. The research couldgenerate several product lines that are complementary to the company's current products and which will enable the company to expand its product range in new markets. PUBLIC HEALTH RELEVANCE PUBLIC HEALTH RELEVANCE: Exposure to bacterial productsin early childhood can affect the development of asthma. Recent animal studies associate exposure to bacterial flagellin with enhancement of allergic responses. A high throughput immunoassay for flagellin will be developed to measure environmental exposure to flagellin in US homes and public places. This will allow the role of flagellin as a biomarker for allergic responses to be investigated and resul in development of commercial assay kits and services for allergy/immunology and infectious diseases.


Grant
Agency: Department of Health and Human Services | Branch: | Program: SBIR | Phase: Phase I | Award Amount: 149.33K | Year: 2010

Molds cause asthma and allergic respiratory diseases and are associated with other illnesses such as sinusitis, chronic fatigue syndrome, lethargy, or migraines. Mold occurs in damp or water damaged housing. The relationships between mold exposure and health effects are poorly understood. The aim of this project is to develop a multiplex array for mold biomarkers that will measure 4-7 biomarkers, simultaneously, from molds associated with asthma or that are found in water damaged buildings. The Technical Objectives are i) to develop a fluorescent Multiplex Array for Mold Biomarkers (MAMB) on the xMAP system to measure allergens/antigens from Alternaria, Aspergillus fumigatus, A. versicolor, Stachybotrys and Penicillium spp.


Trademark
Indoor Biotechnologies | Date: 2014-05-27

diagnostic assay preparations for scientific or research use; antibodies for scientific or research use or for use in the manufacture of allergen detection systems, devices and allergen purification systems; substances composed of antibodies or allergens for scientific or research use or for use in the manufacture of allergen detection systems and devices or allergen purification systems; assay systems, composed of antibodies, for detection and measurement of allergen concentrations in indoor and outdoor environments, or in dust, air, foods or any other substances; diagnostic assay systems, composed of antibodies, for detection and measurement of allergen concentrations in indoor and outdoor environments, or in dust, air, foods, or any other substances; rapid test devices, composed of antibodies, for detection and measurement of allergen concentrations in indoor and outdoor environments, or in dust, air, foods or any other substances; and allergen detection devices, composed of antibodies, for detection and measurement of allergen concentrations in indoor and outdoor environments, or in dust, air, foods or any other substances. diagnostic assay preparations and substances for clinical or medial use; antibodies for clinical or medical laboratory use or for environmental analysis for use in the treatment of allergic diseases, including rhinitis, asthma, atopic dermatitis, food allergies and occupational allergies; substances, composed of antibodies, for use in the treatment of allergic diseases, including rhinitis, asthma, atopic dermatitis, food allergies and occupational allergies; pharmaceutical preparations, including epitope mapping systems, composed of antibodies, for use in the treatment of allergic diseases, including rhinitis, asthma, atopic dermatitis, food allergies and occupational allergies; pharmaceutical preparations, namely, rapid test devices, composed of antibodies, for detection and measurement of allergen concentrations in indoor and outdoor environments, or in dust, air, foods or any other substances; pharmaceutical preparations, namely, allergen detection devices, composed of antibodies, for detection and measurement of allergen concentrations in indoor and outdoor environments, or in dust, air, foods, or any other substances; assay systems, composed of antibodies for detection of antibodies in blood and other body fluids; diagnostic assay systems, composed of antibodies for detection of antibodies in blood and other body fluids; allergen analysis and purification systems, composed of antibodies, for isolation and purification of natural and recombinant allergens for diagnosis and treatment of allergic diseases; epitope mapping systems, composed of antibodies and natural or recombinant allergens, for use in diagnosis and treatment of allergic diseases. medical apparatus, namely, assay systems, composed of plastic microtiter plates, nitrocellulose membranes, affinity matrices and microbeads, for detection of antibodies in blood and other body fluids; medical apparatus, namely, diagnostic assay systems, composed of plastic microtiter plates, nitrocellulose membranes, gel based affinity matrices and microbeads, for detection of antibodies in blood and other body fluids; medical apparatus, namely, allergen analysis and purification systems, composed of plastic microtiter plates, antibody immunoadsorbents prepared using agarose beads, agarose and acrylamide gels, plastic laboratory columns and tubing, for isolation and purification of natural and recombinant allergens for diagnosis and treatment of allergic diseases; medical apparatus, namely, allergen sampling and detection systems, composed of plastic dust collection devices with membrane filters, plastic microtiter plates, plastic cassettes containing antibody coated membranes, and dipsticks for use in diagnosis and treatment of allergic diseases. education services, namely, providing training courses, technical information, white papers, electronic and social media services concerning allergy, immunology and life sciences and providing information regarding the health effects of environmental allergens, molds and bacterial products, indoor air quality, disease associations, exposure assessment and risk factors.

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