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6CJK

Anti HIV Fab 10A

Summary for 6CJK
Entry DOI10.2210/pdb6cjk/pdb
DescriptorImmunoglobulin Fab light chain, Immunoglobulin Fab heavy chain, ACETATE ION, ... (5 entities in total)
Functional Keywordsfab, hiv, immune system
Biological sourceOryctolagus cuniculus (rabbit)
More
Total number of polymer chains4
Total formula weight93096.46
Authors
Hangartner, L.,Ward, A.B.,Wilson, I.A.,Oyen, D. (deposition date: 2018-02-26, release date: 2018-08-15, Last modification date: 2024-11-06)
Primary citationBianchi, M.,Turner, H.L.,Nogal, B.,Cottrell, C.A.,Oyen, D.,Pauthner, M.,Bastidas, R.,Nedellec, R.,McCoy, L.E.,Wilson, I.A.,Burton, D.R.,Ward, A.B.,Hangartner, L.
Electron-Microscopy-Based Epitope Mapping Defines Specificities of Polyclonal Antibodies Elicited during HIV-1 BG505 Envelope Trimer Immunization.
Immunity, 49:288-300.e8, 2018
Cited by
PubMed Abstract: Characterizing polyclonal antibody responses via currently available methods is inherently complex and difficult. Mapping epitopes in an immune response is typically incomplete, which creates a barrier to fully understanding the humoral response to antigens and hinders rational vaccine design efforts. Here, we describe a method of characterizing polyclonal responses by using electron microscopy, and we applied this method to the immunization of rabbits with an HIV-1 envelope glycoprotein vaccine candidate, BG505 SOSIP.664. We detected known epitopes within the polyclonal sera and revealed how antibody responses evolved during the prime-boosting strategy to ultimately result in a neutralizing antibody response. We uncovered previously unidentified epitopes, including an epitope proximal to one recognized by human broadly neutralizing antibodies as well as potentially distracting non-neutralizing epitopes. Our method provides an efficient and semiquantitative map of epitopes that are targeted in a polyclonal antibody response and should be of widespread utility in vaccine and infection studies.
PubMed: 30097292
DOI: 10.1016/j.immuni.2018.07.009
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.795 Å)
Structure validation

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