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Title: Native Mass Spectrometry, Ion mobility, and Collision-Induced Unfolding Categorize Malaria Antigen/Antibody Binding

Abstract

Plasmodium vivax Duffy Binding Protein (PvDBP) is a promising vaccine candidate for P. vivax malaria. Recently, we reported the epitopes on PvDBP region II (PvDBP-II) for three inhibitory monoclonal antibodies (2D10, 2H2, and 2C6). In this communication, we describe the combination of native mass spectrometry and ion mobility (IM) with collision induced unfolding (CIU) to study the conformation and stabilities of three malarial antigen–antibody complexes. These complexes, when collisionally activated, undergo conformational changes that depend on the location of the epitope. CIU patterns for PvDBP-II in complex with antibody 2D10 and 2H2 are highly similar, indicating comparable binding topology and stability. A different CIU fingerprint is observed for PvDBP-II/2C6, indicating that 2C6 binds to PvDBP-II on an epitope different from 2D10 and 2H2. This work supports the use of CIU as a means of classifying antigen-antibody complexes by their epitope maps in a high throughput screening workflow. .

Authors:
 [1]; ; ;  [2];  [1]
  1. Washington University in St. Louis, Department of Chemistry (United States)
  2. Washington University School of Medicine in St. Louis, Department of Molecular Microbiology (United States)
Publication Date:
OSTI Identifier:
22776824
Resource Type:
Journal Article
Journal Name:
Journal of the American Society for Mass Spectrometry
Additional Journal Information:
Journal Volume: 28; Journal Issue: 11; Other Information: Copyright (c) 2017 American Society for Mass Spectrometry; http://www.springer-ny.com; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 1044-0305
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; 46 INSTRUMENTATION RELATED TO NUCLEAR SCIENCE AND TECHNOLOGY; ANTIGENS; COLLISIONS; COMPARATIVE EVALUATIONS; CONFORMATIONAL CHANGES; ION MOBILITY; MALARIA; MASS SPECTROSCOPY; MONOCLONAL ANTIBODIES; PROTEINS

Citation Formats

Huang, Yining, Salinas, Nichole D., Chen, Edwin, Tolia, Niraj H., and Gross, Michael L., E-mail: mgross@wustl.edu. Native Mass Spectrometry, Ion mobility, and Collision-Induced Unfolding Categorize Malaria Antigen/Antibody Binding. United States: N. p., 2017. Web. doi:10.1007/S13361-017-1782-0.
Huang, Yining, Salinas, Nichole D., Chen, Edwin, Tolia, Niraj H., & Gross, Michael L., E-mail: mgross@wustl.edu. Native Mass Spectrometry, Ion mobility, and Collision-Induced Unfolding Categorize Malaria Antigen/Antibody Binding. United States. doi:10.1007/S13361-017-1782-0.
Huang, Yining, Salinas, Nichole D., Chen, Edwin, Tolia, Niraj H., and Gross, Michael L., E-mail: mgross@wustl.edu. Wed . "Native Mass Spectrometry, Ion mobility, and Collision-Induced Unfolding Categorize Malaria Antigen/Antibody Binding". United States. doi:10.1007/S13361-017-1782-0.
@article{osti_22776824,
title = {Native Mass Spectrometry, Ion mobility, and Collision-Induced Unfolding Categorize Malaria Antigen/Antibody Binding},
author = {Huang, Yining and Salinas, Nichole D. and Chen, Edwin and Tolia, Niraj H. and Gross, Michael L., E-mail: mgross@wustl.edu},
abstractNote = {Plasmodium vivax Duffy Binding Protein (PvDBP) is a promising vaccine candidate for P. vivax malaria. Recently, we reported the epitopes on PvDBP region II (PvDBP-II) for three inhibitory monoclonal antibodies (2D10, 2H2, and 2C6). In this communication, we describe the combination of native mass spectrometry and ion mobility (IM) with collision induced unfolding (CIU) to study the conformation and stabilities of three malarial antigen–antibody complexes. These complexes, when collisionally activated, undergo conformational changes that depend on the location of the epitope. CIU patterns for PvDBP-II in complex with antibody 2D10 and 2H2 are highly similar, indicating comparable binding topology and stability. A different CIU fingerprint is observed for PvDBP-II/2C6, indicating that 2C6 binds to PvDBP-II on an epitope different from 2D10 and 2H2. This work supports the use of CIU as a means of classifying antigen-antibody complexes by their epitope maps in a high throughput screening workflow. .},
doi = {10.1007/S13361-017-1782-0},
journal = {Journal of the American Society for Mass Spectrometry},
issn = {1044-0305},
number = 11,
volume = 28,
place = {United States},
year = {2017},
month = {11}
}