Related ArticlesNMR identification of epitopes of Lyme disease antigen OspA to monoclonal antibodies.
J Mol Biol. 1998 Aug 7;281(1):61-7
Authors: Huang X, Yang X, Luft BJ, Koide S
Outer surface protein A (OspA) from the Lyme disease spirochete Borrelia burgdorferi has been a focus of vaccine development. We have identified epitopes of OspA to two monoclonal antibodies (mAbs) by comparing NMR chemical shifts of free OspA and those in Fab complexes. Deuteration of non-labile protons in OspA extended the size limit of this technique so that it was applicable to the 78 kDa complexes of OspA and the Fab fragment. The epitope identified by NMR to an mAb, 184.1, agrees well with that previously defined by the crystal structure of the same complex, indicating the ability of the NMR method to accurately map an epitope in a large protein complex. The technique mapped the epitope to mAb 336, a mAb of clinical interest, to a region centered at the C-terminal alpha-helix. The results provides a basis for rational design of OspA-based Lyme disease vaccines.
[NMR paper] Precise epitope mapping of malaria parasite inhibitory antibodies by TROSY NMR cross-
Precise epitope mapping of malaria parasite inhibitory antibodies by TROSY NMR cross-saturation.
Related Articles Precise epitope mapping of malaria parasite inhibitory antibodies by TROSY NMR cross-saturation.
Biochemistry. 2005 Jan 18;44(2):518-23
Authors: Morgan WD, Frenkiel TA, Lock MJ, Grainger M, Holder AA
We have applied NMR cross-saturation with TROSY detection to the problem of precisely mapping conformational epitopes on complete protein antigen molecules. We have investigated complexes of the Fab fragments of two antibodies that...
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[NMR paper] Malaria parasite-inhibitory antibody epitopes on Plasmodium falciparum merozoite surf
Malaria parasite-inhibitory antibody epitopes on Plasmodium falciparum merozoite surface protein-1(19) mapped by TROSY NMR.
Related Articles Malaria parasite-inhibitory antibody epitopes on Plasmodium falciparum merozoite surface protein-1(19) mapped by TROSY NMR.
Mol Biochem Parasitol. 2004 Nov;138(1):29-36
Authors: Morgan WD, Lock MJ, Frenkiel TA, Grainger M, Holder AA
Plasmodium falciparum merozoite surface protein 1 (MSP1)(19), the C-terminal fragment of merozoite surface protein 1, is a leading candidate antigen for development of a...
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[NMR paper] Epitope mapping of gibberellin to the anti-gibberellin A(4) monoclonal antibody by sa
Epitope mapping of gibberellin to the anti-gibberellin A(4) monoclonal antibody by saturation transfer difference NMR spectroscopy.
Related Articles Epitope mapping of gibberellin to the anti-gibberellin A(4) monoclonal antibody by saturation transfer difference NMR spectroscopy.
Biochem Biophys Res Commun. 2003 Aug 1;307(3):498-502
Authors: Murata T, Hemmi H, Nakajima M, Yoshida M, Yamaguchi I
Saturation transfer difference (STD) NMR spectroscopy is a promising tool for rapid screening, identifying ligands that interact with a target protein,...
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[NMR paper] NMR study on the interaction between MHC class I protein and its antigen peptide.
NMR study on the interaction between MHC class I protein and its antigen peptide.
Related Articles NMR study on the interaction between MHC class I protein and its antigen peptide.
Biochem Biophys Res Commun. 2000 Nov 30;278(3):609-13
Authors: Nakagawa M, Chiba-Kamoshida K, Udaka K, Nakanishi H
A major histcompatibility complex (MHC) class I protein H-2K(b) was expressed in a large scale as a fusion protein with thioredoxin and hexahistidine at the N-terminus to analyze the interaction with the antigen peptide SIYRYYGL. NMR spectra of the...
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[NMR paper] NMR studies of Borrelia burgdorferi OspA, a 28 kDa protein containing a single-layer
NMR studies of Borrelia burgdorferi OspA, a 28 kDa protein containing a single-layer beta-sheet.
Related Articles NMR studies of Borrelia burgdorferi OspA, a 28 kDa protein containing a single-layer beta-sheet.
J Biomol NMR. 1998 May;11(4):407-14
Authors: Pham TN, Koide S
The crystal structure of outer surface protein A (OspA) from Borrelia burgdorferi contains a single-layer beta-sheet connecting the N- and C-terminal globular domains. The central beta-sheet consists largely of polar amino acids and it is solvent-exposed on both faces, which...
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[NMR paper] NMR and CD studies on the conformation of a synthetic peptide containing epitopes of
NMR and CD studies on the conformation of a synthetic peptide containing epitopes of the human immunodeficiency virus 1 transmembrane protein gp41.
Related Articles NMR and CD studies on the conformation of a synthetic peptide containing epitopes of the human immunodeficiency virus 1 transmembrane protein gp41.
Biopolymers. 1996 Mar;38(3):423-35
Authors: Consonni R, Limiroli R, Longhi R, Manera E, Vecchio G, Ragona L, Siccardi AG, Zetta L
CD and nmr characterizations are reported for the 23-mer peptide CMC3, corresponding to residues 577-599...