Der f 35: An MD‐2‐like house dust mite allergen that cross‐reacts with Der f 2 and Pso o 2. Issue 11 (23rd May 2017)
- Record Type:
- Journal Article
- Title:
- Der f 35: An MD‐2‐like house dust mite allergen that cross‐reacts with Der f 2 and Pso o 2. Issue 11 (23rd May 2017)
- Main Title:
- Der f 35: An MD‐2‐like house dust mite allergen that cross‐reacts with Der f 2 and Pso o 2
- Authors:
- Fujimura, T.
Aki, T.
Isobe, T.
Matsuoka, A.
Hayashi, T.
Ono, K.
Kawamoto, S. - Abstract:
- Abstract: Background: Dermatophagoides farinae is a source of airborne house dust mite (HDM) allergens. We elucidated IgE‐reactive allergens from D. farinae by two‐dimensional immunoblotting‐based allergenome analysis, and identified one new allergen, named Der f 35, that possesses IgE‐binding capacity comparable to that of Der f 2. The aim of this study was to clarify the allergenic capacity of new HDM allergen Der f 35. Methods: We cloned der f 35 from D. farinae mRNA and produced recombinant Der f 35 in Escherichia coli . The IgE‐binding capacity of Der f 35 and its cross‐reactivity with group 2 allergens from D. farinae and Psoroptes ovis were determined by enzyme‐linked immunosorbent assay (ELISA) and ELISA inhibition assays, respectively. Results: The deduced amino acid sequence for der f 35, which possesses the MD‐2‐related lipid‐recognition domain, showed higher identity with group 2 allergens from P. ovis (61.5%) and Blomia tropicalis (50.7%) than with Der f 2 (40.8%). Der f 35 showed IgE‐binding frequencies of 77.5% (31/40) for the native form upon allergenome analysis and 51.4% (18/35) for recombinant structure by ELISA. Der f 35 showed cross‐reactivity with Der f 2 and Pso o 2 in reaction with HDM‐allergic patients' IgE by ELISA inhibition assay. Conclusion: Der f 35 is a candidate major allergen from D. farinae, which is more similar to group 2 allergens from sheep scab mite and storage mites. Der f 35 could be responsible for the cross‐reactivity among group 2Abstract: Background: Dermatophagoides farinae is a source of airborne house dust mite (HDM) allergens. We elucidated IgE‐reactive allergens from D. farinae by two‐dimensional immunoblotting‐based allergenome analysis, and identified one new allergen, named Der f 35, that possesses IgE‐binding capacity comparable to that of Der f 2. The aim of this study was to clarify the allergenic capacity of new HDM allergen Der f 35. Methods: We cloned der f 35 from D. farinae mRNA and produced recombinant Der f 35 in Escherichia coli . The IgE‐binding capacity of Der f 35 and its cross‐reactivity with group 2 allergens from D. farinae and Psoroptes ovis were determined by enzyme‐linked immunosorbent assay (ELISA) and ELISA inhibition assays, respectively. Results: The deduced amino acid sequence for der f 35, which possesses the MD‐2‐related lipid‐recognition domain, showed higher identity with group 2 allergens from P. ovis (61.5%) and Blomia tropicalis (50.7%) than with Der f 2 (40.8%). Der f 35 showed IgE‐binding frequencies of 77.5% (31/40) for the native form upon allergenome analysis and 51.4% (18/35) for recombinant structure by ELISA. Der f 35 showed cross‐reactivity with Der f 2 and Pso o 2 in reaction with HDM‐allergic patients' IgE by ELISA inhibition assay. Conclusion: Der f 35 is a candidate major allergen from D. farinae, which is more similar to group 2 allergens from sheep scab mite and storage mites. Der f 35 could be responsible for the cross‐reactivity among group 2 mite allergens. … (more)
- Is Part Of:
- Allergy. Volume 72:Issue 11(2017:Nov.)
- Journal:
- Allergy
- Issue:
- Volume 72:Issue 11(2017:Nov.)
- Issue Display:
- Volume 72, Issue 11 (2017)
- Year:
- 2017
- Volume:
- 72
- Issue:
- 11
- Issue Sort Value:
- 2017-0072-0011-0000
- Page Start:
- 1728
- Page End:
- 1736
- Publication Date:
- 2017-05-23
- Subjects:
- allergen -- Der f 2 -- Dermatophagoides farinae -- group 2 allergen -- house dust mite
Allergy -- Periodicals
616.97 - Journal URLs:
- http://estar.bl.uk/cgi-bin/sciserv.pl?collection=journals&journal=01054538 ↗
http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1398-9995 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/all.13192 ↗
- Languages:
- English
- ISSNs:
- 0105-4538
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 0790.945000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 4705.xml