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Epitope mapping by mass spectrometry: determination of an epitope on HIV-1 IIIB p26 recognized by a monoclonal antibody.

C E Parker, D I Papac, S K Trojak and K B Tomer
J Immunol July 1, 1996, 157 (1) 198-206;
C E Parker
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D I Papac
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S K Trojak
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K B Tomer
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Abstract

Matrix-assisted laser desorption mass spectrometry in combination with proteolytic protection assays has been used to identify the functional epitope on HIV-1 IIIB p26 recognized by a mAb. In this procedure, the intact protein is affinity bound to an immobilized mAb under physiologic conditions. A combination of proteolytic enzymatic cleavages was then performed to remove unprotected residues. Protected residues were identified by matrix-assisted laser desorption mass spectrometry based on their m.w. With this approach, an 11-residue sequence was identified as the most tightly affinity-bound fragment. in addition, two less tightly bound segments were observed. These latter two residues may contain elements of a discontinuous epitope or may be residues involved in a wider contact area. The combination of matrix-assisted laser desorption and proteolytic epitope footprinting has been applied to the determination of the epitope on a recombinant protein recognized by a mAb but should be equally applicable to the definition of an epitope on a native protein in its natural folded conformation.

  • Copyright © 1996 by American Association of Immunologists

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The Journal of Immunology
Vol. 157, Issue 1
1 Jul 1996
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Epitope mapping by mass spectrometry: determination of an epitope on HIV-1 IIIB p26 recognized by a monoclonal antibody.
C E Parker, D I Papac, S K Trojak, K B Tomer
The Journal of Immunology July 1, 1996, 157 (1) 198-206;

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Epitope mapping by mass spectrometry: determination of an epitope on HIV-1 IIIB p26 recognized by a monoclonal antibody.
C E Parker, D I Papac, S K Trojak, K B Tomer
The Journal of Immunology July 1, 1996, 157 (1) 198-206;
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Print ISSN 0022-1767        Online ISSN 1550-6606