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Correction for Polymenidou Et Al., Humoral Immune Response to Native Eukaryotic Prion Protein Correlates with Anti-Prion Protect

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Correction for Polymenidou Et Al., Humoral Immune Response to Native Eukaryotic Prion Protein Correlates with Anti-Prion Protect Correction Colloquium Correction for “Humoral immune response to native eukaryotic described in Fig. 2 consisted of 44 samples analyzed by fluorescence- prion protein correlates with anti-prion protection,” by Magdalini activated cell sorting (FACS), including four biological replicates Polymenidou, Frank L. Heppner, Erica C. Pellicioli, Eduard Urich, for each experimental group. The published Fig. 2 was compiled Gino Miele, Nathalie Braun, Franziska Wopfner, Hermann M. by a single, representative image from each experimental group, Schätzl, Burkhard Becher, and Adriano Aguzzi, which was first which was chosen randomly. The panel in the Upper Right corner published August 3, 2004; 10.1073/pnas.0404772101 (Proc. Natl. of the published figure (Prnpo/o serum on tg33 cells) was acci- Acad. Sci. U.S.A. 101, 14670–14676). dentally duplicated in the Lower Left panel (6H4μ × Prnpo/o serum The authors note “It has recently come to our attention that on Prnpo/o cells) during preparation of the figures.” The corrected there is an error in Fig. 2 of our manuscript. The experiment Fig. 2 and its legend appear below. Fig. 2. Sera from 6H4μ transgenic mice react with PrPC on the surface of tg33 T cells. Scattergrams show representative FACS analyses of lymphocytes (tg33 or Prnpo/o) stained with mouse sera. 6H4μ transgenic sera react with PrPC overexpressing T cells (tg33; Upper), but not with Prnpo/o T cells (Lower). PrPC gene dosage in 6H4μ mice correlates negatively with the extent of binding to PrPC, suggesting the occurrence, to some extent, of clonal deletion of auto-reactive B cells. Published under the PNAS license. First published November 9, 2020. www.pnas.org/cgi/doi/10.1073/pnas.2021354117 29988 | PNAS | November 24, 2020 | vol. 117 | no. 47 www.pnas.org Downloaded by guest on September 27, 2021 Colloquium Humoral immune response to native eukaryotic prion protein correlates with anti-prion protection Magdalini Polymenidou*†, Frank L. Heppner*†, Erica C. Pellicioli*‡, Eduard Urich§, Gino Miele*, Nathalie Braun*, Franziska Wopfner¶, Hermann M. Scha¨ tzl¶, Burkhard Becher§, and Adriano Aguzzi*ʈ *Institute of Neuropathology and §Department of Neurology, Neuroimmunology Unit, University Hospital, Schmelzbergstrasse 12 and Frauenklinikstrasse 10, CH-8091 Zurich, Switzerland; ‡Cytos Biotechnology AG, Wagistrasse 25, CH-8952 Zurich-Schlieren, Switzerland; and ¶Institute of Virology, Technical University, Biedersteinstrasse 29, 80802 Munich, Germany Prion diseases are characterized by the deposition of an abnormal in chronically scrapie-infected neuroblastoma cells (10). Further, form (termed PrPSc) of the cellular prion protein (PrPC). Because transgenic expression of anti-PrP antibodies in mice arrested antibodies to PrPC can antagonize deposition of PrPSc in cultured peripheral scrapie pathogenesis (11). In line with our results, cells and mice, they may be useful for anti-prion therapy. However, White and colleagues (12) confirmed the efficiency of anti-PrP induction of protective anti-prion immune responses in WT animals antibodies in preventing prion disease by injecting such antibod- may be hindered by host tolerance. Here, we studied the cellular ies into WT mice upon peripheral prion challenge. and molecular basis of tolerance to PrPC. Immunization of Prnpo/o The prionostatic efficacy of anti-PrP antibodies is highest in mice with bacterially expressed PrP (PrPREC) resulted in vigorous extraneural compartments: transgenic 6H4␮ mice expressing humoral immune responses to PrPREC and native cell-surface PrPC. anti-PrP-specific IgM molecules were not protected when prions Instead, WT mice yielded antibodies that failed to recognize native were administered intracerebrally (F.L.H. and A.A., unpub- PrPC despite immunoreactivity with PrPREC, even after immuniza- lished observations), and passive transfer of PrP-specific IgGs tion with PrP-PrP polyprotein and͞or upon administration of anti- (12) was inefficient when started after onset of clinical signs. This OX40 antibodies. Consequently, immunized WT mice experienced finding may be caused by the limited influx of Igs into the CNS insignificantly delayed prion pathogenesis upon peripheral prion and the high prion load of clinically symptomatic animals. By challenge. Anti-PrP immune responses in Prnpo/o mice were com- providing stable, sustained titers, active immunization may pletely abrogated by transgenic expression of PrPC in B cells, T cells, obviate to some of the problems listed above. However, host neurons, or hepatocytes, but only moderately reduced by expres- tolerance to endogenous PrPC remains a major obstacle to sion in myelinating cells, despite additional thymic Prnp transcrip- devising active immunization regimens. Nevertheless, several tion in each case. We conclude that tolerance to PrPC can coexist recent studies suggest that the induction of anti-PrP antibodies with immunoreactivity to PrPREC and does not depend on thymic in WT mice is in principle feasible (13–18). Although anti-PrP PrPC expression. Its circumvention might represent an important Ig titers could be measured in most of these studies, the titers step toward the development of effective anti-prion immunotherapy. were rather low. Accordingly, the biological efficacy of these immunization series, if evaluated at all, was limited, emphasizing rion diseases or transmissible spongiform encephalopathies the need for alternative strategies. Pare lethal neurodegenerative disorders affecting many ani- The current study explores the efficacy of active immunization mal species. They include bovine spongiform encephalopathy of strategies against PrP. We found that none of these strategies C cattle, chronic wasting disease of deer and elk, and Creutzfeldt– leads to antibody titers to native cell-bound PrP as displayed on C Jakob disease in humans. The causative agent is termed prion (1) the cell surface of PrP -overexpressing tg33 splenocytes (19). C and was proposed to be identical with PrPSc, a pathological This finding suggests that host tolerance to endogenous PrP is conformer of the cellular prion protein (PrPC) encoded by the nonpermissive to generating high-affinity anti-PrP B cell clones Prnp gene (2). PrPC is expressed on the surface of almost all cells or leads to deletion or anergy of the cognate T cell clones. To in the body, but at particularly high levels on neurons in the gain further insight into the mechanism of tolerance to PrP, a key peripheral and central nervous systems. PrPC is essential for the to defining successful immunization strategies against prions in development of prion disease, and Prnpo/o mice, which lack PrPC, the future, we investigated the immune responses of transgenic C are resistant to scrapie (3). mice exhibiting expression of PrP restricted to specific cell C Bovine spongiform encephalopathy (BSE) (4) is caused by types. Expression of PrP within the thymus did not completely REC prions amplified through the bovine food chain (5). Transmis- prevent humoral immune responses to PrP . However, extra- C sion of bovine prions to humans has given rise to variant thymic and extraneural PrP , even if expressed in very small C Creutzfeldt–Jakob disease (vCJD) (6). Although the incidence amounts, blocked all immune responses to both PrP and REC C of BSE and vCJD may be stabilizing or even declining, the steep PrP . While antibodies recognizing cell-surface PrP inter- rise of chronic wasting disease (7) underlines the fact that prion fered with prion pathogenesis in two independent paradigms, we diseases of farm and wild animals still represent a major threat. Thus, there is an urgent and growing need for efficient prophy- ͞ This paper results from the Arthur M. Sackler Colloquium of the National Academy of lactic and or therapeutic measures against prion diseases (8). Sciences, ‘‘Therapeutic Vaccines: Realities of Today and Hopes for Tomorrow,’’ held April Although prions use immune and lymphoreticular cells to gain 1–3, 2004, at the National Academy of Sciences in Washington, DC. access to the brain (9), several reports indicate that humoral Abbreviations: PrP, prion protein; MBP, myelin basic protein; Alb, albumin; CFA, complete immune responses to the PrP can antagonize prion infection. Freund’s adjuvant; IFA, incomplete Freund’s adjuvant; KLH, keyhole limpet hemocyanin; This is true even when such responses are directed primarily CFSE, carboxyfluorescein; NSE, neuron-specific enolase. against PrPC and do not selectively target PrPSc. mAbs and F(ab) †M.P. and F.L.H. contributed equally to this work. fragments recognizing PrP were shown to prevent de novo ʈTo whom correspondence should be addressed. E-mail: [email protected]. scrapie infection and to abolish PrPSc as well as prion infectivity © 2004 by The National Academy of Sciences of the USA 14670–14676 ͉ PNAS ͉ October 5, 2004 ͉ vol. 101 ͉ suppl. 2 www.pnas.org͞cgi͞doi͞10.1073͞pnas.0404772101 found that humoral immune responses were not protective if scribed (11). Cells were washed and incubated with a FITC-labeled their affinity was restricted to PrPREC. anti-mouse IgG secondary antibody or FITC-labeled anti-mouse IgM secondary antibody (Caltag Laboratories, Naenikon, Switzer- Methods land). Thereafter, cells were stained with phycoerythrin (PE)- Mice. All mice were maintained under specific pathogen-free labeled anti-Thy 1.2 or PE-labeled anti-CD3 antibody for detecting conditions. WT mice F1 progeny of mixed background T cells. All antibodies were obtained from Becton Dickinson unless C57BL͞6 ϫ 129Sv were purchased
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