Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/30752
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dc.contributor.authorWines, Bruce D-
dc.contributor.authorKurtovic, Liriye-
dc.contributor.authorTrist, Halina M-
dc.contributor.authorEsparon, Sandra-
dc.contributor.authorLopez, Ester-
dc.contributor.authorChappin, Klasina-
dc.contributor.authorChan, Li-Jin-
dc.contributor.authorMordant, Francesca L-
dc.contributor.authorLee, Wen Shi-
dc.contributor.authorGherardin, Nicholas A-
dc.contributor.authorPatel, Sheila K-
dc.contributor.authorHartley, Gemma E-
dc.contributor.authorPymm, Phillip-
dc.contributor.authorCooney, James P-
dc.contributor.authorBeeson, James G-
dc.contributor.authorGodfrey, Dale I-
dc.contributor.authorBurrell, Louise M-
dc.contributor.authorvan Zelm, Menno C-
dc.contributor.authorWheatley, Adam K-
dc.contributor.authorChung, Amy W-
dc.contributor.authorTham, Wai-Hong-
dc.contributor.authorSubbarao, Kanta-
dc.contributor.authorKent, Stephen J-
dc.contributor.authorHogarth, P Mark-
dc.date2022-
dc.date.accessioned2022-08-25T05:17:48Z-
dc.date.available2022-08-25T05:17:48Z-
dc.date.issued2022-07-28-
dc.identifier.citationFrontiers in Immunology 2022; 13: 889372en
dc.identifier.urihttps://ahro.austin.org.au/austinjspui/handle/1/30752-
dc.description.abstractJoining a function-enhanced Fc-portion of human IgG to the SARS-CoV-2 entry receptor ACE2 produces an antiviral decoy with strain transcending virus neutralizing activity. SARS-CoV-2 neutralization and Fc-effector functions of ACE2-Fc decoy proteins, formatted with or without the ACE2 collectrin domain, were optimized by Fc-modification. The different Fc-modifications resulted in distinct effects on neutralization and effector functions. H429Y, a point mutation outside the binding sites for FcγRs or complement caused non-covalent oligomerization of the ACE2-Fc decoy proteins, abrogated FcγR interaction and enhanced SARS-CoV-2 neutralization. Another Fc mutation, H429F did not improve virus neutralization but resulted in increased C5b-C9 fixation and transformed ACE2-Fc to a potent mediator of complement-dependent cytotoxicity (CDC) against SARS-CoV-2 spike (S) expressing cells. Furthermore, modification of the Fc-glycan enhanced cell activation via FcγRIIIa. These different immune profiles demonstrate the capacity of Fc-based agents to be engineered to optimize different mechanisms of protection for SARS-CoV-2 and potentially other viral pathogens.en
dc.language.isoeng
dc.subjectACE2-Fcen
dc.subjectADCCen
dc.subjectCOVID-19en
dc.subjectSARS-CoV-2en
dc.subjectantibody effector functionen
dc.subjectcomplementen
dc.subjectcoronavirusen
dc.subjectneutralizationen
dc.titleFc engineered ACE2-Fc is a potent multifunctional agent targeting SARS-CoV2.en
dc.typeJournal Articleen_US
dc.identifier.journaltitleFrontiers in Immunologyen
dc.identifier.affiliationLife Sciences, Burnet Institute, Melbourne, VIC, Australia..en
dc.identifier.affiliationWorld Health Organization (WHO) Collaborating Centre for Reference and Research on Influenza, The Peter Doherty Institute for Infection and Immunity, The University of Melbourne, Melbourne, VIC, Australia..en
dc.identifier.affiliationAustralian Research Council Centre for Excellence in Convergent Bio-Nano Science and Technology, The University of Melbourne, Melbourne, VIC, Australia..en
dc.identifier.affiliationDepartment of Allergy, Immunology and Respiratory Medicine, Central Clinical School, Alfred Hospital, Melbourne, VIC, Australia..en
dc.identifier.affiliationDepartment of Microbiology, Monash University, Clayton VIC, Australia..en
dc.identifier.affiliationDepartment of Medicine, Royal Melbourne Hospital, The University of Melbourne, Parkville, VIC, Australia..en
dc.identifier.affiliationMedicine (University of Melbourne)en
dc.identifier.affiliationImmune therapies Laboratory, Burnet Institute, Melbourne, VIC, Australia..en
dc.identifier.affiliationDepartment of Immunology and Pathology, Central Clinical School, Monash University, Melbourne, VIC, Australia..en
dc.identifier.affiliationMelbourne Sexual Health Centre and Department of Infectious Diseases, Alfred Hospital and Central Clinical School, Monash University, Melbourne, VIC, Australia..en
dc.identifier.affiliationDepartment of Medical Biology, The University of Melbourne, Melbourne, VIC, Australia..en
dc.identifier.affiliationInfectious Diseases and Immune Defence Division, The Walter and Eliza Hall Institute of Medical Research, Parkville, VIC, Australia..en
dc.identifier.affiliationDepartment of Microbiology and Immunology, The Peter Doherty Institute for Infection and Immunity, The University of Melbourne, Melbourne, VIC, Australia..en
dc.identifier.affiliationDepartment of Clinical Pathology, The University of Melbourne, Parkville, VIC, Australia..en
dc.identifier.pubmedurihttps://pubmed.ncbi.nlm.nih.gov/35967361/en
dc.identifier.doi10.3389/fimmu.2022.889372en
dc.type.contentTexten_US
dc.identifier.orcid0000-0002-0626-1899en
dc.identifier.orcid0000-0003-1863-7539en
dc.identifier.pubmedid35967361
local.name.researcherBurrell, Louise M
item.fulltextNo Fulltext-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.cerifentitytypePublications-
item.openairetypeJournal Article-
item.grantfulltextnone-
item.languageiso639-1en-
crisitem.author.deptMedicine (University of Melbourne)-
crisitem.author.deptCardiology-
crisitem.author.deptGeneral Medicine-
crisitem.author.deptMedicine (University of Melbourne)-
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