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Image Search Results
Journal: PLoS ONE
Article Title: Antigenic and immunosuppressive properties of a trimeric recombinant transmembrane envelope protein gp41 of HIV-1
doi: 10.1371/journal.pone.0173454
Figure Lengend Snippet: a) Glycosylation analysis of purified gp41. The protein was denatured and left untreated or incubated with Endoglycosidase H (EndoH) or with PNGase F (PNGase) as indicated. The exclusive sensitivity to PNGase F digestion suggests that the protein is properly post-translationally modified with N-linked sugar residues. b) Analysis of the purified protein using native PAGE, The migration of gp41 at ~160 kDa suggests a trimeric state of the protein. c) Binding of different monoclonal antibodies to recombinant gp41. Binding was measured in a capture ELISA at 4 or 37°C incubation temperature with indicated antibodies coated to the plate. 2nd, secondary anti HIS-HRP probe only, human, anti-gp120 control antibody, mouse, anti gp120 control antibody. For details on the monoclonal antibodies, please see . Different levels of binding and a temperature sensitive recognition pattern was observed for selected antibodies. d) Results of surface plasmon resonance studies using recombinant gp41 and various monoclonal antibodies. Single cycle kinetics were determined by capturing the indicated anti-gp41 antibodies to the chip via covalently linked anti-mouse or anti human IgG, followed by five injections of gp41 at increasing concentrations. Data shown (ΔRU) represent double referenced sensograms with relative signal intensities obtained by subtraction of flow cell 2 (gp41 antibody) and flow cell 1 (no antibody). Measurement curves (black) and fitted curves (red) are indicated.
Article Snippet: Affinity measurements were performed on a Biacore X100 device (GE Healthcare, Germany) at 37°C using the human or
Techniques: Glycoproteomics, Purification, Incubation, Modification, Clear Native PAGE, Migration, Binding Assay, Bioprocessing, Recombinant, Enzyme-linked Immunosorbent Assay, Control, SPR Assay