Proteomic profiling and characterization of differential allergens in the nematodes Anisakis simplex sensu stricto and A. pegreffii. Issue 12 (21st May 2014)
- Record Type:
- Journal Article
- Title:
- Proteomic profiling and characterization of differential allergens in the nematodes Anisakis simplex sensu stricto and A. pegreffii. Issue 12 (21st May 2014)
- Main Title:
- Proteomic profiling and characterization of differential allergens in the nematodes Anisakis simplex sensu stricto and A. pegreffii
- Authors:
- Arcos, Susana C.
Ciordia, Sergio
Roberston, Lee
Zapico, Inés
Jiménez‐Ruiz, Yolanda
Gonzalez‐Muñoz, Miguel
Moneo, Ignacio
Carballeda‐Sangiao, Noelia
Rodriguez‐Mahillo, Ana
Albar, Juan P.
Navas, Alfonso - Abstract:
- <abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The parasite species complex <italic>Anisakis simplex sensu lato</italic> (<italic>Anisakis simplex sensu stricto</italic>; (<italic>A. simplex s.s</italic>.), <italic>A. pegreffii</italic>, <italic>A. simplex C</italic>) is the main cause of severe anisakiasis (allergy) worldwide and is now an important health matter. In this study, the relationship of this <italic>Anisakis</italic> species complex and their allergenic capacities is assessed by studying the differences between the two most frequent species (<italic>A. simplex s.s</italic>., <italic>A. pegreffii</italic>) and their hybrid haplotype by studying active L3 larvae parasiting <italic>Merluccius merluccius</italic>. They were compared by 2D gel electrophoresis and parallel Western blot (2DE gels were hybridized with pools of sera from <italic>Anisakis</italic> allergenic patients). Unambiguous spot differences were detected and protein assignation was made by MALDI‐TOF/TOF analysis or de novo sequencing. Seventy‐five gel spots were detected and the corresponding proteins were identified. Differentially expressed proteins for A<italic>. simplex s.s., A. pegreffii</italic>, and their hybrid are described and results are statistically supported. Twenty‐eight different allergenic proteins are classified according to different families belonging to different biological functions. These proteins are described for the first time as<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The parasite species complex <italic>Anisakis simplex sensu lato</italic> (<italic>Anisakis simplex sensu stricto</italic>; (<italic>A. simplex s.s</italic>.), <italic>A. pegreffii</italic>, <italic>A. simplex C</italic>) is the main cause of severe anisakiasis (allergy) worldwide and is now an important health matter. In this study, the relationship of this <italic>Anisakis</italic> species complex and their allergenic capacities is assessed by studying the differences between the two most frequent species (<italic>A. simplex s.s</italic>., <italic>A. pegreffii</italic>) and their hybrid haplotype by studying active L3 larvae parasiting <italic>Merluccius merluccius</italic>. They were compared by 2D gel electrophoresis and parallel Western blot (2DE gels were hybridized with pools of sera from <italic>Anisakis</italic> allergenic patients). Unambiguous spot differences were detected and protein assignation was made by MALDI‐TOF/TOF analysis or de novo sequencing. Seventy‐five gel spots were detected and the corresponding proteins were identified. Differentially expressed proteins for A<italic>. simplex s.s., A. pegreffii</italic>, and their hybrid are described and results are statistically supported. Twenty‐eight different allergenic proteins are classified according to different families belonging to different biological functions. These proteins are described for the first time as antigenic and potentially new allergens in <italic>Anisakis</italic>. Comparative proteomic analyses of allergenic capacities are useful for diagnosis, epidemiological surveys, and clinical research. All MS data have been deposited in the ProteomeXchange with identifier PXD000662 (<ext-link ext-link-type="uri" xlink:href="http://proteomecentral.proteomexchange.org/dataset/PXD000662" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink">http://proteomecentral.proteomexchange.org/dataset/PXD000662</ext-link>).</p> </abstract> … (more)
- Is Part Of:
- Proteomics. Volume 14:Issue 12(2014:Jun.)
- Journal:
- Proteomics
- Issue:
- Volume 14:Issue 12(2014:Jun.)
- Issue Display:
- Volume 14, Issue 12 (2014)
- Year:
- 2014
- Volume:
- 14
- Issue:
- 12
- Issue Sort Value:
- 2014-0014-0012-0000
- Page Start:
- 1547
- Page End:
- 1568
- Publication Date:
- 2014-05-21
- Subjects:
- Proteins -- Separation -- Periodicals
Bioinformatics -- Periodicals
Proteomics -- Periodicals
Genomes -- Periodicals
Molecular genetics -- Periodicals
572.605 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1615-9861 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/pmic.201300529 ↗
- Languages:
- English
- ISSNs:
- 1615-9853
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6936.178000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 4361.xml