PMID- 31636292
OWN - NLM
STAT- MEDLINE
DCOM- 20201030
LR  - 20210110
IS  - 2045-2322 (Electronic)
IS  - 2045-2322 (Linking)
VI  - 9
IP  - 1
DP  - 2019 Oct 21
TI  - Ole e 15 and its human counterpart -PPIA- chimeras reveal an heterogeneous IgE 
      response in olive pollen allergic patients.
PG  - 15027
LID - 10.1038/s41598-019-51005-2 [doi]
LID - 15027
AB  - 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.
FAU - San Segundo-Acosta, Pablo
AU  - San Segundo-Acosta P
AD  - Departamento de Bioquimica y Biologia Molecular, Facultad de Ciencias Quimicas, 
      Universidad Complutense de Madrid, E-28040, Madrid, Spain.
FAU - Oeo-Santos, Carmen
AU  - Oeo-Santos C
AD  - Departamento de Bioquimica y Biologia Molecular, Facultad de Ciencias Quimicas, 
      Universidad Complutense de Madrid, E-28040, Madrid, Spain.
FAU - Navas, Ana
AU  - Navas A
AD  - Hospital Universitario Reina Sofia de Cordoba, E-14004, Cordoba, Spain.
FAU - Jurado, Aurora
AU  - Jurado A
AD  - Hospital Universitario Reina Sofia de Cordoba, E-14004, Cordoba, Spain.
FAU - Villalba, Mayte
AU  - Villalba M
AD  - Departamento de Bioquimica y Biologia Molecular, Facultad de Ciencias Quimicas, 
      Universidad Complutense de Madrid, E-28040, Madrid, Spain.
FAU - Barderas, Rodrigo
AU  - Barderas R
AD  - Chronic Disease Programme (UFIEC), Instituto de Salud Carlos III, Majadahonda, 
      E-28220, Madrid, Spain. r.barderasm@isciii.es.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20191021
PL  - England
TA  - Sci Rep
JT  - Scientific reports
JID - 101563288
RN  - 0 (Amino Acids)
RN  - 0 (Antigens, Plant)
RN  - 0 (Immunoglobulin G)
RN  - 0 (Peptides)
RN  - 0 (Recombinant Proteins)
RN  - 37341-29-0 (Immunoglobulin E)
RN  - EC 5.2.1.- (Cyclophilin A)
SB  - IM
MH  - Amino Acid Sequence
MH  - Amino Acids/genetics
MH  - Antigens, Plant/chemistry/*immunology
MH  - Cross Reactions
MH  - Cyclophilin A/chemistry/*immunology
MH  - Humans
MH  - Immunoglobulin E/blood/*immunology
MH  - Immunoglobulin G/metabolism
MH  - Models, Molecular
MH  - Mutation/genetics
MH  - Olea/*immunology
MH  - Peptides/metabolism
MH  - Protein Binding
MH  - Recombinant Proteins/genetics/*immunology
MH  - Rhinitis, Allergic, Seasonal/blood/*immunology
PMC - PMC6803672
COIS- The authors declare no competing interests.
EDAT- 2019/10/23 06:00
MHDA- 2020/10/31 06:00
PMCR- 2019/10/21
CRDT- 2019/10/23 06:00
PHST- 2019/07/22 00:00 [received]
PHST- 2019/09/16 00:00 [accepted]
PHST- 2019/10/23 06:00 [entrez]
PHST- 2019/10/23 06:00 [pubmed]
PHST- 2020/10/31 06:00 [medline]
PHST- 2019/10/21 00:00 [pmc-release]
AID - 10.1038/s41598-019-51005-2 [pii]
AID - 51005 [pii]
AID - 10.1038/s41598-019-51005-2 [doi]
PST - epublish
SO  - Sci Rep. 2019 Oct 21;9(1):15027. doi: 10.1038/s41598-019-51005-2.