Journal article

Enhanced Ability of Plant-Derived PGT121 Glycovariants To Eliminate HIV-1-Infected Cells

Sai Priya Anand, Shilei Ding, William D Tolbert, Jeremie Prevost, Jonathan Richard, Hwi Min Gil, Gabrielle Gendron-Lepage, Wing-Fai Cheung, Haifeng Wang, Rebecca Pastora, Hirak Saxena, Warren Wakarchuk, Halima Medjahed, Bruce D Wines, Mark Hogarth, George M Shaw, Malcom A Martin, Dennis R Burton, Lars Hangartner, David T Evans Show all

JOURNAL OF VIROLOGY | AMER SOC MICROBIOLOGY | Published : 2021

Abstract

The activity of broadly neutralizing antibodies (bNAbs) targeting HIV-1 depends on pleiotropic functions, including viral neutralization and the elimination of HIV-1-infected cells. Several in vivo studies have suggested that passive administration of bNAbs represents a valuable strategy for the prevention or treatment of HIV-1. In addition, different strategies are currently being tested to scale up the production of bNAbs to obtain the large quantities of antibodies required for clinical trials. Production of antibodies in plants permits low-cost and large-scale production of valuable therapeutics; furthermore, pertinent to this work, it also includes an advanced glycoengineering platform...

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University of Melbourne Researchers

Grants

Awarded by CIHR foundation


Awarded by NIH


Awarded by Canada Research Chair on Retroviral Entry


Awarded by NRC-IRAP


Awarded by DOE Office of Science


Awarded by National Institutes of Health, National Institute of General Medical Sciences (NIGMS)


Awarded by DOE Office of Biological and Environmental Research


Funding Acknowledgements

This study was supported by a National Research Council (Canada) Industrial Research Assistance Program (NRC-IRAP) grant to M.D.M. and A.F., by CIHR foundation grant 352417 to A.F., and by NIH grants R01 AI129 AI129769 to M.P. and A.F., R01 AI116274 to M.P., P01 AI120756 to Georgia Tomaras, R01 AI121135 and R37 AI095098 to D.T.E., and R01 AI148379 to A.F. and D.T.E. A.F. is the recipient of a Canada Research Chair on Retroviral Entry (grant RCHS0235 950-232424) . L.H. was supported by NIH R01 AI136621-02 and NIH UM1 AI144462-01. D.R.B. was supported by NIH UM1 AI144462. Plant antibody production and analyses by PlantForm Corporation were supported in part by NRC-IRAP (catalog no. 778829 and 812182) , and glycosylation analyses were performed by Warren Wakarchuk. S.P.A. and J.P. are supported by CIHR fellowships. This research used resources of the National Synchrotron Light Source II, a U.S. Department of Energy (DOE) Office of Science User Facility operated for the DOE Office of Science by the Brookhaven National Laboratory under contract DE-SC0012704. The Center for BioMolecular Structure (CBMS) is primarily supported by the National Institutes of Health, National Institute of General Medical Sciences (NIGMS) , through a Center Core P30 grant (P30GM133893) and by the DOE Office of Biological and Environmental Research (KP1607011) . The funders had no role in study design, data collection and analysis, the decision to publish, or preparation of the manuscript.