Site-specific glycosylation of differentially affinity-purified CZA97.012 SOSIP.664 trimer.
figure
posted on 2023-10-30, 18:00 authored by Rajesh P. Ringe, Philippe Colin, Gabriel Ozorowski, Joel D. Allen, Anila Yasmeen, Gemma E. Seabright, Jeong Hyun Lee, Aleksandar Antanasijevic, Kimmo Rantalainen, Thomas Ketas, John P. Moore, Andrew B. Ward, Max Crispin, P. J. KlasseTrimer was purified by 2G12-, PGT145-, or PGT151-affinity chromatography followed by SEC. Differentially purified trimer was analyzed by a method based on PNGase F or Endo H digestion. The bar graphs represent the relative amounts of digested glycopeptides possessing the footprints for oligo-mannose- and hybrid-type glycans together (green), complex-type glycans (magenta), and unoccupied PNGS (gray). The results were obtained by LC-MS. The error bars represent s.e.m. of all peptides detected for each site; n.d. = not detectable (which does not suggest low occupancy).
History
Usage metrics
Keywords
surface plasmon resonanceproviding one explanationrefuting apex openingdepleting nab increaseddepleting nab decreasedsubstantial persistent fractionspgt151 increased sensitivitydiv >< pdetectable persistent fractionfractionated soluble nativepurified trimer fractions012 trimer determinedreduced pgt145 bindingpersistent fractionspersistent fractiontrimer apexsoluble nativepurified formnab pgt151nab pgt145nab bindingtrimer purificationtrimer adopted012 trimersoluble cza97β19 transitionå resolutiontherapeutic outcomereactive virionsrabbits immunizedpseudoviral populationspeptide epitopepassive immunizationnew structureneutralizing antibodiesmultiple epitopesmass spectrometryinfected personsglycan shieldglycan heterogeneityf infectivityevidence suggestsenvelope glycoproteinelectron microscopydirect effectsdifferential antigenicityclosed conformationc isolateantibody contacts15 %.100 %.
Licence
Exports
RefWorks
BibTeX
Ref. manager
Endnote
DataCite
NLM
DC