In silico comparison of interaction of allergen and human profilin 1 with natural ligands of human profilin 1
IgE-mediated allergy, or type 1 hypersensitivity, is an acute reaction caused by allergen-induced cross-linking of IgE bound to FcεRs on the surface of effector cells. Birch pollen is a common cause of type 1 hypersensitivity affecting seasonal symptoms of allergic rhinitis and asthma-related emerge...
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| Formato: | Artículo revista |
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Universidad Nacional Córdoba. Facultad de Ciencias Médicas. Secretaria de Ciencia y Tecnología
2022
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| Acceso en línea: | https://revistas.unc.edu.ar/index.php/med/article/view/38967 |
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I10-R327-article-38967 |
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ojs |
| institution |
Universidad Nacional de Córdoba |
| institution_str |
I-10 |
| repository_str |
R-327 |
| container_title_str |
Revista de la Facultad de Ciencias Médicas de Córdoba |
| format |
Artículo revista |
| topic |
Allergy pollen profilina VASP alergia polen profilina VASP . |
| spellingShingle |
Allergy pollen profilina VASP alergia polen profilina VASP . Cossy Isasi , S Muiño , JC In silico comparison of interaction of allergen and human profilin 1 with natural ligands of human profilin 1 |
| topic_facet |
Allergy pollen profilina VASP alergia polen profilina VASP . |
| author |
Cossy Isasi , S Muiño , JC |
| author_facet |
Cossy Isasi , S Muiño , JC |
| author_sort |
Cossy Isasi , S |
| title |
In silico comparison of interaction of allergen and human profilin 1 with natural ligands of human profilin 1 |
| title_short |
In silico comparison of interaction of allergen and human profilin 1 with natural ligands of human profilin 1 |
| title_full |
In silico comparison of interaction of allergen and human profilin 1 with natural ligands of human profilin 1 |
| title_fullStr |
In silico comparison of interaction of allergen and human profilin 1 with natural ligands of human profilin 1 |
| title_full_unstemmed |
In silico comparison of interaction of allergen and human profilin 1 with natural ligands of human profilin 1 |
| title_sort |
in silico comparison of interaction of allergen and human profilin 1 with natural ligands of human profilin 1 |
| description |
IgE-mediated allergy, or type 1 hypersensitivity, is an acute reaction caused by allergen-induced cross-linking of IgE bound to FcεRs on the surface of effector cells. Birch pollen is a common cause of type 1 hypersensitivity affecting seasonal symptoms of allergic rhinitis and asthma-related emergencies. Bet v 1 (17 kDa) the immunodominant and most abundant allergenic protein in this pollen is a profilin. Profilins are proteins that regulate actin polymerization with functions that go beyond the cytoskeleton. Structural homology indicates that the G-actin-profilin interaction is conserved in all eukaryotic organisms with mechanistic differences in the binding of proline-rich ligands. Therefore, it is likely that exogenous profilins may play biological roles in humans. We tested this hypothesis with computational simulations to compare the predictable affinity of Bet v1 and human profilin 1 (Pf1H) for natural Pf1H ligands.
The structures obtained from the RSCB PDB of crystallized and digitalized samples (7mxl, 1pfl, 2pav, 4A87) were separated and the files re-edited to calculate the interaction energies (Kcal/mol) and their structural mean square deviations (RMSD-Angstroms) by means of USFC Chimera PyMol, Autodock Vina, Hdock and HADDOCK, software run on local I5 processors and on the EGI/EOSC high throughput computing (HTC) network employing 2 million processors in Europe.
The binding energies (Kcal/mol) of Bet v1 and Pf1H to VASP (Vasodilator-Stimulated phosphoprotein Peptide) were -7 and -6.4; with RMSD of 7 and 5; to monoclonal antibodies (IgG4) anti Bet v1 -25.2 and -27.3; with RMSD of 12.7 and 10.8 respectively. Binding energy values describe higher affinity for the Bet-VASP pair than for Pf1H-VASP and higher affinity for the IgG4-Pf1H pair than IgG4-Bet. The RMSD of the complexes with VASP correspond to structures similar to the spontaneous ones and those of IgG4-Pf1H are more similar to the spontaneous ones than the IgG4-Bet, which would be the natural antigen.
These values, subject to experimental validation, allow us to hypothesize that exogenous profilins could perform biological functions in addition to being allergens. |
| publisher |
Universidad Nacional Córdoba. Facultad de Ciencias Médicas. Secretaria de Ciencia y Tecnología |
| publishDate |
2022 |
| url |
https://revistas.unc.edu.ar/index.php/med/article/view/38967 |
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AT cossyisasis insilicocomparisonofinteractionofallergenandhumanprofilin1withnaturalligandsofhumanprofilin1 AT muinojc insilicocomparisonofinteractionofallergenandhumanprofilin1withnaturalligandsofhumanprofilin1 AT cossyisasis comparacioninsilicodeinteracciondealergenoyprofilina1humanaconligandosnaturalesdeprofilina1humana AT muinojc comparacioninsilicodeinteracciondealergenoyprofilina1humanaconligandosnaturalesdeprofilina1humana |
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2024-09-03T21:03:49Z |
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2024-09-03T21:03:49Z |
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I10-R327-article-389672024-04-15T16:14:45Z In silico comparison of interaction of allergen and human profilin 1 with natural ligands of human profilin 1 Comparación in sílico de interacción de alergeno y profilina 1 humana con ligandos naturales de profilina 1 humana . Cossy Isasi , S Muiño , JC Allergy pollen profilina VASP alergia polen profilina VASP . IgE-mediated allergy, or type 1 hypersensitivity, is an acute reaction caused by allergen-induced cross-linking of IgE bound to FcεRs on the surface of effector cells. Birch pollen is a common cause of type 1 hypersensitivity affecting seasonal symptoms of allergic rhinitis and asthma-related emergencies. Bet v 1 (17 kDa) the immunodominant and most abundant allergenic protein in this pollen is a profilin. Profilins are proteins that regulate actin polymerization with functions that go beyond the cytoskeleton. Structural homology indicates that the G-actin-profilin interaction is conserved in all eukaryotic organisms with mechanistic differences in the binding of proline-rich ligands. Therefore, it is likely that exogenous profilins may play biological roles in humans. We tested this hypothesis with computational simulations to compare the predictable affinity of Bet v1 and human profilin 1 (Pf1H) for natural Pf1H ligands. The structures obtained from the RSCB PDB of crystallized and digitalized samples (7mxl, 1pfl, 2pav, 4A87) were separated and the files re-edited to calculate the interaction energies (Kcal/mol) and their structural mean square deviations (RMSD-Angstroms) by means of USFC Chimera PyMol, Autodock Vina, Hdock and HADDOCK, software run on local I5 processors and on the EGI/EOSC high throughput computing (HTC) network employing 2 million processors in Europe. The binding energies (Kcal/mol) of Bet v1 and Pf1H to VASP (Vasodilator-Stimulated phosphoprotein Peptide) were -7 and -6.4; with RMSD of 7 and 5; to monoclonal antibodies (IgG4) anti Bet v1 -25.2 and -27.3; with RMSD of 12.7 and 10.8 respectively. Binding energy values describe higher affinity for the Bet-VASP pair than for Pf1H-VASP and higher affinity for the IgG4-Pf1H pair than IgG4-Bet. The RMSD of the complexes with VASP correspond to structures similar to the spontaneous ones and those of IgG4-Pf1H are more similar to the spontaneous ones than the IgG4-Bet, which would be the natural antigen. These values, subject to experimental validation, allow us to hypothesize that exogenous profilins could perform biological functions in addition to being allergens. La alergia mediada por IgE, o hipersensibilidad tipo 1, es una reacción aguda causada por la reticulación inducida por alergenos de IgE unida a FcεRs en la superficie de las células efectoras. El polen de abedules es una causa común de hipersensibilidad tipo 1 que afecta los síntomas estacionales de rinitis alérgica y emergencias relacionadas con el asma. Bet v 1 (17 kDa) la proteína alergénica inmunodominante y más abundante en este polen es una profilina. Las profilinas son proteínas reguladoras de la polimerización de actina con funciones que exceden al citoesqueleto. La homología estructural indica que la interacción actina-profilina G se conserva en todos los organismos eucariotas con diferencias mecánicas en la unión de ligandos ricos en prolina. Por lo tanto, es probable que profilinas exógenas puedan desempeñar funciones biológicas en seres humanos. Evaluamos esta hipótesis con simulaciones computacionales para comparar la afinidad predecible de Bet v1 y de profilina 1 humana (Pf1H) por ligandos naturales de Pf1H. Las estructuras obtenidas del RSCB PDB de muestras cristalizadas y digitalizadas (7mxl, 1pfl, 2pav, 4A87) fueron separadas y los archivos reeditados para calcular las energías de interacción (Kcal/mol) y sus desvíos cuadráticos medios estructurales (RMSD- Angstroms) mediante USFC Chimera PyMol, Autodock Vina, Hdock y HADDOCK, software corrido en procesadores locales I5 y en EGI/EOSC high throughput computing (HTC) red que emplea 2 millones de procesadores en Europa. Las energìas (Kcal/mol) de unión de Bet v1 y Pf1H a VASP (Vasodilator-Stimulated phosphoprotein Peptide) fueron -7 y -6,4; con RMSD de 7 y 5; a anticuerpos monoclonales (IgG4) anti Bet v1 -25,2 y -27,3; con RMSD de 12,7 y 10,8 respectivamente. Los valores de energías de unión describen mayor afinidad para el par Bet-VASP que para Pf1H-VASP y mayor afinidad de los pares IgG4-Pf1H que IgG4-Bet. Los RMSD de los complejos con VASP corresponden a estructuras semejantes a las espontáneas y los de IgG4-Pf1H son más parecidos a los espontáneos que los IgG4-Bet que sería el antígeno natural. Estos valores sujetos a validación experimental, nos permiten considerar que profilinas exógenas pueden desempeñar funciones biológicas además de ser alergenos. . Universidad Nacional Córdoba. Facultad de Ciencias Médicas. Secretaria de Ciencia y Tecnología 2022-10-26 info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion texto texto . https://revistas.unc.edu.ar/index.php/med/article/view/38967 Revista de la Facultad de Ciencias Médicas de Córdoba.; Vol. 79 No. Suplemento JIC XXIII (2022): Suplemento JIC XXIII Revista de la Facultad de Ciencias Médicas de Córdoba; Vol. 79 Núm. Suplemento JIC XXIII (2022): Suplemento JIC XXIII Revista da Faculdade de Ciências Médicas de Córdoba; v. 79 n. Suplemento JIC XXIII (2022): Suplemento JIC XXIII 1853-0605 0014-6722 http://creativecommons.org/licenses/by-nc/4.0 |