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Structural basis of ribosomal frameshifting during translation of the SARS-CoV-2 RNA genome

Structural basis of ribosomal frameshifting during translation of the SARS-CoV-2 RNA genome
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National Center , Irish Research Council Advanced Laureate , Protein Data Bank , Swiss National Science Foundation , Electron Microscopy Data Bank , Carbery Group Ltd , Ministry Of Education , Creative Commons Attribution , Federal Ministry , Carbery Group , தேசிய மையம் , ப்ரோடீந் தகவல்கள் வங்கி , சுவிஸ் தேசிய அறிவியல் அடித்தளம் , எதிர் மின்னணு நுண்ணோக்கி தகவல்கள் வங்கி , கார்பரி குழு லிமிடெட் , அமைச்சகம் ஆஃப் கல்வி , கூட்டாட்சியின் அமைச்சகம் , கார்பரி குழு ,

Prevalent, protective, and convergent IgG recognition of SARS-CoV-2 non-RBD spike epitopes

Most analyses of the antibody responses induced by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection have focused on antibodies cloned from memory B cells. This approach has led researchers to conclude that neutralizing antibodies (nAbs) primarily target the receptor-binding domain (RBD) of the virus s spike protein. Voss et al. took a different approach, using proteomic deconvolution of the serum immunoglobulin G antibody repertoire from four COVID-19 convalescent patients. They found that the nAb response was largely directed against epitopes such as the N-terminal domain (NTD), which lie outside the RBD. Several of these nAbs were shared among donors and targeted an NTD epitope that is frequently mutated by variants of concern.

Science , abg5268, this issue p. [1108][1]

The molecular composition and binding epitopes of the immunoglobulin G (IgG) antibodies that circulate in blood plasma after severe acute respiratory syndrome coronavirus 2 (SARS-Co ....

United States , San Francisco , University Of California , Lamontagne Center , Ut System Proteomics Network , National Institute Of Allergy , Department Of Defense , Infectious Diseases Research Program , Sauer Structural Biology Laboratory , Us Army , Research Institute Of Texas , University Of Texas Board Regents , Centers For Disease , National Institutes Of Health , Electron Microscopy Data Bank , Department Of The Army , Welch Foundation , Protein Data Bank , University Of Texas College Natural Sciences , Clayton Foundation , Ig Seq Lin , United Kingdom , Creative Commons Attribution , Infectious Disease , Military Infectious Diseases Research Program , Disease Control ,

New Artificial Intelligence Tool May Speed Up Drug Discovery Using Images

New Artificial Intelligence Tool May Speed Up Drug Discovery Using Images
New Artificial Intelligence Tool May Speed Up Drug Discovery Using Images
Japanese researchers are using artificial intelligence (AI) to gain insights from cryo-electron microscopy.
Artificial intelligence (AI) machine learning is transforming pharmaceutical drug discovery. Advances in deep learning, a subset of machine learning, is enabling researchers to identify patterns in fields where there are large amounts of complex data, such as imaging.
In a recent study published in Nature Machine Intelligence, researchers in Japan created an AI deep neural network to extract information on protein dynamics from images captured using cryo-electron microscopy (cryo-EM). ....

New York , United States , United Kingdom , Shigeyuki Matsumoto , Kei Terayama , Jacques Dubochet , Takayuki Kato , Yasushi Okuno , Mitsugu Araki , Richard Henderson , Shoichi Ishida , Joachim Frank At Columbia University , Laboratory Of Molecular Biology In Cambridge , University Of Lausanne , Electron Microscopy Data Bank , Nature Machine Intelligence , Joachim Frank , Columbia University , Molecular Biology , Nobel Prize , Rosso All , New Artificial Intelligence Tool May Speed Up Drug Discovery Using Images , புதியது யார்க் , ஒன்றுபட்டது மாநிலங்களில் , ஒன்றுபட்டது கிஂக்டம் , ரிச்சர்ட் ஹென்டர்சன் ,

The neutralizing antibody, LY-CoV555, protects against SARS-CoV-2 infection in nonhuman primates

Among the most promising therapeutic options for individuals with coronavirus disease 2019 (COVID-19) are monoclonal antibodies (mAbs). In this study, Jones et al . identified, characterized, and tested one such mAb, LY-CoV555, in vitro and in vivo. They found that LY-CoV555 bound to the severe acute respiratory distress syndrome coronavirus-2 (SARS-CoV-2) spike protein and prevented its interaction with angiotensin-converting enzyme 2. Prophylactic treatment with LY-CoV555 protected the upper and lower respiratory tracts of nonhuman primates from becoming infected with SARS-CoV-2. Together, these data support the clinical use of LY-CoV555 for treating patients with COVID-19.

Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) poses a public health threat for which preventive and therapeutic agents are urgently needed. Neutralizing antibodies are a key class of therapeutics that may bridge widespread vaccination campaigns and offer a treatment solution in populations le ....

South Africa , United States , United Kingdom , K Huntington Eli Lilly , Gatan Solarus , Isoplates Perkinelmer , Eli Lilly , Oxford Cryosystems , Carterra Epitope , Us Department Of Defense , National Institute Of Allergy , Grossman School Of Medicine Startup , Lilly Research Laboratories Collaborative Access Team , Burroughs Wellcome Fund Postdoctoral Enrichment Program Award , Us Department Of Energy , International Patent Application No , Electron Microscopy Sciences , Office Of Science , Committee Of Bioqual Inc , Argonne National Laboratory , Centers For Disease , European Union Horizon , Laboratory Animals , Abcellera Biologics Inc , National Institutes Of Health , P Sipahimalani Abcellera Biologics Inc ,

Structural impact on SARS-CoV-2 spike protein by D614G substitution

Abstract
Substitution for aspartic acid by glycine at position 614 in the spike (S) protein of severe acute respiratory syndrome coronavirus 2 appears to facilitate rapid viral spread. The G614 strain and its recent variants are now the dominant circulating forms. We report here cryo-EM structures of a full-length G614 S trimer, which adopts three distinct prefusion conformations differing primarily by the position of one receptor-binding domain. A loop disordered in the D614 S trimer wedges between domains within a protomer in the G614 spike. This added interaction appears to prevent premature dissociation of the G614 trimer, effectively increasing the number of functional spikes and enhancing infectivity, and to modulate structural rearrangements for membrane fusion. These findings extend our understanding of viral entry and suggest an improved immunogen for vaccine development. ....

United Kingdom , United States , South Africa , James Chou , Structural Biology Of Harvard Medical School , Protein Data Bank , Massachusetts Consortium On Pathogen Readiness Mass , Nancy Lurie Marks Family Foundation , Harvard Center , Electron Microscopy Data Bank , Creative Commons Attribution , Structural Biology , Harvard Medical , Massachusetts Consortium , Pathogen Readiness , Emergent Ventures , Hummingbird Bioscience , Data Bank , Boston Children , ஒன்றுபட்டது கிஂக்டம் , ஒன்றுபட்டது மாநிலங்களில் , ஜேம்ஸ் ச Ou , கட்டமைப்பு உயிரியல் ஆஃப் ஹார்வர்ட் மருத்துவ பள்ளி , ப்ரோடீந் தகவல்கள் வங்கி , மாசசூசெட்ஸ் கூட்டமைப்பு ஆன் நோய்க்கிருமி ரெடிநெஸ் நிறை , நான்சி லூரி மதிப்பெண்கள் குடும்பம் அடித்தளம் ,