Lectin Fingerprinting Distinguishes Antibody Neutralization in SARS-CoV-2.
Lectin Fingerprinting Distinguishes Antibody Neutralization in SARS-CoV-2.
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DOI:
10.1021/acscentsci.2c01471
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发表时间:
2023-05-24
影响因子:
18.2
通讯作者:
Kiessling, Laura L.
中科院分区:
文献类型:
--
作者:
Wuo, Michael G.;Dugan, Amanda E.;Halim, Melanie;Hauser, Blake M.;Feldman, Jared;Caradonna, Timothy M.;Zhang, Shuting;Pepi, Lauren E.;Atyeo, Caroline;Fischinger, Stephanie;Alter, Galit;Garcia-Beltran, Wilfredo F.;Azadi, Parastoo;Hung, Deb;Schmidt, Aaron G.;Kiessling, Laura L.
Enveloped viruses co-opt host glycosylation pathways to decorate their surface proteins. As viruses evolve, emerging strains can modify their glycosylation patterns to influence host interactions and subvert immune recognition. Still, changes in viral glycosylation or their impact on antibody protection cannot be predicted from genomic sequences alone. Using the highly glycosylated SARS-CoV-2 Spike protein as a model system, we present a lectin fingerprinting method that rapidly reports on changes in variant glycosylation state, which are linked to antibody neutralization. In the presence of antibodies or convalescent and vaccinated patient sera, unique lectin fingerprints emerge that distinguish neutralizing versus non-neutralizing antibodies. This information could not be inferred from direct binding interactions between antibodies and the Spike receptor-binding domain (RBD) binding data alone. Comparative glycoproteomics of the Spike RBD of wild-type (Wuhan-Hu-1) and Delta (B.1.617.2) variants reveal O-glycosylation differences as a key determinant of immune recognition differences. These data underscore the interplay between viral glycosylation and immune recognition and reveal lectin fingerprinting to be a rapid, sensitive, and high-throughput assay to distinguish the neutralization potential of antibodies that target critical viral glycoproteins. Lectin fingerprinting is a high-throughput and facile method to rapidly profile the neutralization potential of patient antibodies raised against viral glycoproteins.
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影响因子:
4
作者:
Bojar, Daniel;Meche, Lawrence;Meng, Guanmin;Eng, William;Smith, David F.;Cummings, Richard D.;Mahal, Lara K.
通讯作者:
Mahal, Lara K.
DOI:
10.1126/science.abl6251
发表时间:
2022-01-21
期刊:
Science (New York, N.Y.)
影响因子:
--
作者:
通讯作者:
--
影响因子:
4.8
作者:
Byrnes, James R.;Zhou, Xin X.;Wells, James A.
通讯作者:
Wells, James A.
影响因子:
6.7
作者:
Cook JD;Lee JE
通讯作者:
Lee JE
影响因子:
64.5
作者:
Kang L;He G;Sharp AK;Wang X;Brown AM;Michalak P;Weger-Lucarelli J
通讯作者:
Weger-Lucarelli J