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024 7 |a 10.1002/adma.202005637  |2 doi 
028 5 2 |a pubmed25n1055.xml 
035 |a (DE-627)NLM316800252 
035 |a (NLM)33111375 
040 |a DE-627  |b ger  |c DE-627  |e rakwb 
041 |a eng 
100 1 |a Huang, Wei-Chiao  |e verfasserin  |4 aut 
245 1 0 |a SARS-CoV-2 RBD Neutralizing Antibody Induction is Enhanced by Particulate Vaccination 
264 1 |c 2020 
336 |a Text  |b txt  |2 rdacontent 
337 |a ƒaComputermedien  |b c  |2 rdamedia 
338 |a ƒa Online-Ressource  |b cr  |2 rdacarrier 
500 |a Date Completed 08.01.2021 
500 |a Date Revised 28.08.2024 
500 |a published: Print-Electronic 
500 |a Citation Status MEDLINE 
520 |a © 2020 Wiley-VCH GmbH. 
520 |a The receptor-binding domain (RBD) of the SARS-CoV-2 spike protein is a candidate vaccine antigen that binds angiotensin-converting enzyme 2 (ACE2), leading to virus entry. Here, it is shown that rapid conversion of recombinant RBD into particulate form via admixing with liposomes containing cobalt-porphyrin-phospholipid (CoPoP) potently enhances the functional antibody response. Antigen binding via His-tag insertion into the CoPoP bilayer results in a serum-stable and conformationally intact display of the RBD on the liposome surface. Compared to other vaccine formulations, immunization using CoPoP liposomes admixed with recombinant RBD induces multiple orders of magnitude higher levels of antibody titers in mice that neutralize pseudovirus cell entry, block RBD interaction with ACE2, and inhibit live virus replication. Enhanced immunogenicity can be accounted for by greater RBD uptake into antigen-presenting cells in particulate form and improved immune cell infiltration in draining lymph nodes. QS-21 inclusion in the liposomes results in an enhanced antigen-specific polyfunctional T cell response. In mice, high dose immunization results in minimal local reactogenicity, is well-tolerated, and does not elevate serum cobalt levels. Taken together, these results confirm that particulate presentation strategies for the RBD immunogen should be considered for inducing strongly neutralizing antibody responses against SARS-CoV-2 
650 4 |a Journal Article 
650 4 |a COVID-19 
650 4 |a SARS-CoV-2 
650 4 |a antigens 
650 4 |a liposomes 
650 4 |a nanoparticles 
650 4 |a vaccines 
650 7 |a Antibodies, Neutralizing  |2 NLM 
650 7 |a Antibodies, Viral  |2 NLM 
650 7 |a Spike Glycoprotein, Coronavirus  |2 NLM 
650 7 |a spike protein, SARS-CoV-2  |2 NLM 
650 7 |a ACE2 protein, human  |2 NLM 
650 7 |a EC 3.4.17.23  |2 NLM 
650 7 |a Angiotensin-Converting Enzyme 2  |2 NLM 
650 7 |a EC 3.4.17.23  |2 NLM 
700 1 |a Zhou, Shiqi  |e verfasserin  |4 aut 
700 1 |a He, Xuedan  |e verfasserin  |4 aut 
700 1 |a Chiem, Kevin  |e verfasserin  |4 aut 
700 1 |a Mabrouk, Moustafa T  |e verfasserin  |4 aut 
700 1 |a Nissly, Ruth H  |e verfasserin  |4 aut 
700 1 |a Bird, Ian M  |e verfasserin  |4 aut 
700 1 |a Strauss, Mike  |e verfasserin  |4 aut 
700 1 |a Sambhara, Suryaprakash  |e verfasserin  |4 aut 
700 1 |a Ortega, Joaquin  |e verfasserin  |4 aut 
700 1 |a Wohlfert, Elizabeth A  |e verfasserin  |4 aut 
700 1 |a Martinez-Sobrido, Luis  |e verfasserin  |4 aut 
700 1 |a Kuchipudi, Suresh V  |e verfasserin  |4 aut 
700 1 |a Davidson, Bruce A  |e verfasserin  |4 aut 
700 1 |a Lovell, Jonathan F  |e verfasserin  |4 aut 
773 0 8 |i Enthalten in  |t Advanced materials (Deerfield Beach, Fla.)  |d 1998  |g 32(2020), 50 vom: 28. Dez., Seite e2005637  |w (DE-627)NLM098206397  |x 1521-4095  |7 nnas 
773 1 8 |g volume:32  |g year:2020  |g number:50  |g day:28  |g month:12  |g pages:e2005637 
856 4 0 |u http://dx.doi.org/10.1002/adma.202005637  |3 Volltext 
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952 |d 32  |j 2020  |e 50  |b 28  |c 12  |h e2005637