ArticlebioRxiv : the preprint server for biology2020
The ACE2-binding interface of SARS-CoV-2 Spike inherently deflects immune recognition.
Takamitsu Hattori, Akiko Koide, Tatyana Panchenko, Larizbeth A Romero, Kai Wen Teng, Takuya Tada, Nathaniel R Landau, Shohei Koide
Open access · greenAbstract readPreprint
In one paragraphArticle in bioRxiv : the preprint server for biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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0cells of the map it votes in
0citing papers in PubMed
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What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
2 · The registryThe trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
3 · Its place in the literatureWho cites it
0 citing papers in PubMed, 3 citations in OpenAlex.
No citing paper in PubMed yet.
4 · The recordCorrections and comments
5 · Who and what moneyAuthors and funding
8 authors at 2 institutions in 1 country.
Takamitsu HattoriPerlmutter Cancer Center, New York University Langone Health, New York, NY 10016, U.S.A.
Akiko KoidePerlmutter Cancer Center, New York University Langone Health, New York, NY 10016, U.S.A.
Tatyana PanchenkoPerlmutter Cancer Center, New York University Langone Health, New York, NY 10016, U.S.A.
Larizbeth A RomeroPerlmutter Cancer Center, New York University Langone Health, New York, NY 10016, U.S.A.
Kai Wen TengPerlmutter Cancer Center, New York University Langone Health, New York, NY 10016, U.S.A.
Takuya TadaDepartment of Microbiology, New York University Grossman School of Medicine, New York, NY 10016.
Nathaniel R LandauDepartment of Microbiology, New York University Grossman School of Medicine, New York, NY 10016.
Shohei KoidePerlmutter Cancer Center, New York University Langone Health, New York, NY 10016, U.S.A.
NYU Langone Health · USNew York University · US
Funding
Probing RAS-mediated Signaling with Monobody InhibitorsR01CA212608 · NCI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI SHOHEI KOIDE, John P O'Bryan · 2017 to 2026
$5.8MTherapeutic Dendritic Cell Vaccine for HIVDP1DA046100 · NIDA · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI LANDAU, NATHANIEL R. · 2018 to 2023
$4.2MMolecular mechanisms of SHP2 signaling dissected with designer binding proteinsR01CA194864 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI KOIDE, SHOHEI · 2016 to 2020
$1.8MDendritic Cell Vaccine for Controlling the Latent ReservoirR33AI122390 · NIAID · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI KIEM, HANS-PETER, KITCHEN, SCOTT G · 2018 to 2020
$1.6MLentiviral Vector Vaccine for HIV-1K08AI120898 · NIAID · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI NORTON, THOMAS D · 2015 to 2018
$774kRational generation of high-performance recombinant antibodies to post-translational modificationsR21CA246457 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI HATTORI, TAKAMITSU · 2020 to 2020
$620kAccurate prediction of neutralization capacity from deep mining of SARS-CoV-2 serologyR21AI158997 · NIAID · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI KOIDE, SHOHEI · 2020 to 2020
$466kDendritic Cell Vaccine for Controlling the Latent ReservoirR21AI122390 · NIAID · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI KIEM, HANS-PETER, KITCHEN, SCOTT G · 2016 to 2017
$457kNCI NIH HHS R01 CA194864NCI NIH HHS R01 CA212608NCI NIH HHS R21 CA246457NIAID NIH HHS K08 AI120898NIAID NIH HHS R21 AI122390NIAID NIH HHS R21 AI158997NIAID NIH HHS R33 AI122390NIDA NIH HHS DP1 DA046100
6 · The paper itselfAbstract
The COVID-19 pandemic remains a global threat, and host immunity remains the main mechanism of protection against the disease. The spike protein on the surface of SARS-CoV-2 is a major antigen and its engagement with human ACE2 receptor plays an essential role in viral entry into host cells. Consequently, antibodies targeting the ACE2-interacting surface (ACE2IS) located in the receptor-binding domain (RBD) of the spike protein can neutralize the virus. However, the understanding of immune responses to SARS-CoV-2 is still limited, and it is unclear how the virus protects this surface from recognition by antibodies. Here, we designed an RBD mutant that disrupts the ACE2IS and used it to characterize the prevalence of antibodies directed to the ACE2IS from convalescent sera of 94 COVID19-positive patients. We found that only a small fraction of RBD-binding antibodies targeted the ACE2IS. To assess the immunogenicity of different parts of the spike protein, we performed
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PMID33173869
PMCPMC7654858
OpenAlexW3095657813
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