|Title||Coupling of HIV-1 gp120-derived Core Protein to Paramagnetic Beads and Adsorption Assays.|
|Publication Type||Journal Article|
|Year of Publication||2015|
|Authors||Ingale J, Wyatt RT|
Analysis of the functional activity in polyclonal serum following immunization of a complex protein or glycoprotein immunogen is a very important but tedious process. Fine mapping of epitope specific antibodies is difficult when they are elicited at relatively low levels. In our recent study focused at developing an HIV-1 vaccine, we immunized rabbits with hyperglycosylated stable core immunogens, which were designed using high resolution structural information to elicit antibodies against the primary receptor-binding, CD4-binding site on HIV-1 gp120. Using a solid phase adsorption assay, we could map the serum antibodies to the conserved CD4-binding site, a known broadly neutralizing determinant on exterior envelope glycoprotein, gp120.
|Alternate Journal||Bio Protoc|
|PubMed Central ID||PMC4737960|
|Grant List||UM1 AI100663 / AI / NIAID NIH HHS / United States|
Coupling of HIV-1 gp120-derived Core Protein to Paramagnetic Beads and Adsorption Assays.