4.2 Article

Isolation of HIV-1-reactive antibodies using cell surface-expressed gp160ΔcBaL

Journal

JOURNAL OF IMMUNOLOGICAL METHODS
Volume 397, Issue 1-2, Pages 47-54

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.jim.2013.09.003

Keywords

HIV-1; Surface-expressed envelope trimer; Single B cell sort; HIV-1 neutralizing antibodies

Funding

  1. National Center for Advancing Translational Sciences (NCATS) [UL1 TR000043]
  2. National Institutes of Health (NIH) Clinical and Translational Science Award (CTSA) program
  3. NIH [AI081677, UM1AI100663]
  4. Bill and Melinda Gates Foundation [OPP1033115]
  5. German National Academic Foundation
  6. German Research Foundation (DFG) [KL 2389/1-1]
  7. Stavros Niarchos Foundation
  8. Robert Mapplethorpe Foundation
  9. Bill and Melinda Gates Foundation [OPP1033115] Funding Source: Bill and Melinda Gates Foundation

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Significant efforts have been made to identify HIV-1 neutralizing antibodies because they are considered to be critical to the design of an effective HIV-1 vaccine. Although soluble HIV-1 envelope proteins can be used for this purpose, these reagents differ from membrane-anchored HIV-1 envelope spike in a number of important ways and display only a subset of its native epitopes. Consistent with this, some broadly neutralizing antibodies preferentially bind cell surface-expressed HIV-1 envelope, but not the soluble protein. Here we report the details of a new method for isolating anti-HIV-1 specific B cells based on capturing cells that produce antibodies to cell surface-expressed gp160 Delta c(BaL). While this method is far less efficient than sorting with soluble envelope proteins, it isolated broadly neutralizing anti-HIV-1 antibodies that bind cell surface-expressed gp160 Delta c(BaL) but not soluble envelope proteins. Published by Elsevier B.V.

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