Limits...
Human IgE against the major allergen Bet v 1--defining an epitope with limited cross-reactivity between different PR-10 family proteins.

Levin M, Davies AM, Liljekvist M, Carlsson F, Gould HJ, Sutton BJ, Ohlin M - Clin. Exp. Allergy (2014)

Bottom Line: The interaction between IgE and allergen is a key event at the initiation of an allergic response, and its characteristics have substantial effects on the clinical manifestation.We here display the usefulness of allergen-specific human monoclonal IgE as a tool in studies of the crucial molecular interaction taking place at the initiation of an allergic response.Such studies may aid us in development of better diagnostic tools and guide us in the development of new therapeutic compounds.

View Article: PubMed Central - PubMed

Affiliation: Department of Immunotechnology, Lund University, Lund, Sweden.

Show MeSH
(a) Overall structure of the M0418 scFv. The disposition of CDRH3 above the surface of molecule A is shown, and the H and L chain V domains are coloured in salmon and white, respectively. (b) CDRH3 from molecule A. A 2Fo-Fc electron density map is contoured at 1.0σ around residues from CDRH3. Two symmetry-related copies of molecule B (pink and green) flank CDRH3 on either side. Residues from CDRH3 molecule A are shown as a stick representation, as are selected residues from the two symmetry-related molecules, and the two alternative conformations modelled for Leu107 (VH) and Ser92 (VL) are also shown. A hydrogen bond between Tyr114 (VH) Arg95 (VL) is indicated with a black line. The figure was produced with PyMOL 42.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
getmorefigures.php?uid=PMC4215112&req=5

fig05: (a) Overall structure of the M0418 scFv. The disposition of CDRH3 above the surface of molecule A is shown, and the H and L chain V domains are coloured in salmon and white, respectively. (b) CDRH3 from molecule A. A 2Fo-Fc electron density map is contoured at 1.0σ around residues from CDRH3. Two symmetry-related copies of molecule B (pink and green) flank CDRH3 on either side. Residues from CDRH3 molecule A are shown as a stick representation, as are selected residues from the two symmetry-related molecules, and the two alternative conformations modelled for Leu107 (VH) and Ser92 (VL) are also shown. A hydrogen bond between Tyr114 (VH) Arg95 (VL) is indicated with a black line. The figure was produced with PyMOL 42.

Mentions: The crystal structure of the M0418 scFv was determined to 1.3Å resolution. The structures of the two independent molecules of the asymmetric unit were similar and were superposed with an RMSD value of 0.56Å over 232 Cα atoms. The most significant difference between the two molecules was disorder of a stretch of residues from CDRH3 of molecule B (residues 110-112.3), while that from molecule A was completely modelled. In molecule A, CDRH3 extends ˜8Å above the surface of the scFv (Fig.5a).


Human IgE against the major allergen Bet v 1--defining an epitope with limited cross-reactivity between different PR-10 family proteins.

Levin M, Davies AM, Liljekvist M, Carlsson F, Gould HJ, Sutton BJ, Ohlin M - Clin. Exp. Allergy (2014)

(a) Overall structure of the M0418 scFv. The disposition of CDRH3 above the surface of molecule A is shown, and the H and L chain V domains are coloured in salmon and white, respectively. (b) CDRH3 from molecule A. A 2Fo-Fc electron density map is contoured at 1.0σ around residues from CDRH3. Two symmetry-related copies of molecule B (pink and green) flank CDRH3 on either side. Residues from CDRH3 molecule A are shown as a stick representation, as are selected residues from the two symmetry-related molecules, and the two alternative conformations modelled for Leu107 (VH) and Ser92 (VL) are also shown. A hydrogen bond between Tyr114 (VH) Arg95 (VL) is indicated with a black line. The figure was produced with PyMOL 42.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4215112&req=5

fig05: (a) Overall structure of the M0418 scFv. The disposition of CDRH3 above the surface of molecule A is shown, and the H and L chain V domains are coloured in salmon and white, respectively. (b) CDRH3 from molecule A. A 2Fo-Fc electron density map is contoured at 1.0σ around residues from CDRH3. Two symmetry-related copies of molecule B (pink and green) flank CDRH3 on either side. Residues from CDRH3 molecule A are shown as a stick representation, as are selected residues from the two symmetry-related molecules, and the two alternative conformations modelled for Leu107 (VH) and Ser92 (VL) are also shown. A hydrogen bond between Tyr114 (VH) Arg95 (VL) is indicated with a black line. The figure was produced with PyMOL 42.
Mentions: The crystal structure of the M0418 scFv was determined to 1.3Å resolution. The structures of the two independent molecules of the asymmetric unit were similar and were superposed with an RMSD value of 0.56Å over 232 Cα atoms. The most significant difference between the two molecules was disorder of a stretch of residues from CDRH3 of molecule B (residues 110-112.3), while that from molecule A was completely modelled. In molecule A, CDRH3 extends ˜8Å above the surface of the scFv (Fig.5a).

Bottom Line: The interaction between IgE and allergen is a key event at the initiation of an allergic response, and its characteristics have substantial effects on the clinical manifestation.We here display the usefulness of allergen-specific human monoclonal IgE as a tool in studies of the crucial molecular interaction taking place at the initiation of an allergic response.Such studies may aid us in development of better diagnostic tools and guide us in the development of new therapeutic compounds.

View Article: PubMed Central - PubMed

Affiliation: Department of Immunotechnology, Lund University, Lund, Sweden.

Show MeSH