4.4 Article

Engineered Multivalent Nanobodies Potently and Broadly Neutralize SARS-CoV-2 Variants

Related references

Note: Only part of the references are listed.
Review Biochemistry & Molecular Biology

Immunogenicity and humanization of single-domain antibodies

Martin A. Rossotti et al.

Summary: Single-domain antibodies have desirable properties as biologic drugs, but their sequences may increase immunogenicity risks. While most clinical trials show minimal immunogenicity, special caution is needed for highly potent sdAbs. Further research is needed to establish humanization thresholds to maximize human sequence content without compromising binding affinity or stability.

FEBS JOURNAL (2022)

Article Medicine, General & Internal

SARS-CoV-2 Neutralizing Antibody LY-CoV555 in Outpatients with Covid-19

Peter Chen et al.

Summary: LY-CoV555, a neutralizing antibody, showed promising results in reducing viral load, improving symptoms, and lowering the risk of hospitalization among patients with mild or moderate Covid-19. While one of the doses appeared to accelerate the decline in viral load, others did not show significant effects by day 11.

NEW ENGLAND JOURNAL OF MEDICINE (2021)

Article Multidisciplinary Sciences

Structure-guided multivalent nanobodies block SARS-CoV-2 infection and suppress mutational escape

Paul-Albert Koenig et al.

Summary: In this study, new neutralizing nanobodies targeting the SARS-CoV-2 spike protein were developed, showing enhanced neutralizing activity through engineering technology and successfully suppressing the emergence of escape mutants. The findings suggest that nanobodies can neutralize through receptor binding competition and also render virions noninfectious.

SCIENCE (2021)

Article Biochemistry & Molecular Biology

Rational affinity maturation of anti-amyloid antibodies with high conformational and sequence specificity

Alec A. Desai et al.

Summary: This study developed a systematic directed evolution procedure to generate high-affinity antibodies against Alzheimer's A beta fibrils, with strict conformational and sequence specificity, based on a lead conformational antibody. The resulting antibodies showed similar or higher affinities than clinical-stage A beta antibodies and retained high conformational specificity for A beta aggregates.

JOURNAL OF BIOLOGICAL CHEMISTRY (2021)

Article Multidisciplinary Sciences

Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7

Pengfei Wang et al.

Summary: The COVID-19 pandemic has had global repercussions, with promising vaccines and monoclonal antibody therapies. However, newly detected variants of SARS-CoV-2 present challenges to these treatment options.

NATURE (2021)

Article Multidisciplinary Sciences

Estimated transmissibility and impact of SARS-CoV-2 lineage B.1.1.7 in England

Nicholas G. Davies et al.

Summary: A new variant of SARS-CoV-2 has emerged in England, with a higher reproduction number and potential for large resurgences of COVID-19 cases. Without stringent control measures, it is projected that COVID-19 hospitalizations and deaths in England for the first 6 months of 2021 will exceed those in 2020. The variant has spread globally and exhibited similar transmission increases in Denmark, Switzerland, and the United States.

SCIENCE (2021)

Article Biochemistry & Molecular Biology

SARS-CoV-2 variants B.1.351 and P.1 escape from neutralizing antibodies

Markus Hoffmann et al.

Summary: The emerging SARS-CoV-2 variants may exhibit resistance to existing neutralizing antibodies and treatments, which could have significant implications for pandemic containment efforts.
Article Biochemistry & Molecular Biology

Sensitivity of infectious SARS-CoV-2 B.1.1.7 and B.1.351 variants to neutralizing antibodies

Delphine Planas et al.

Summary: The ability of convalescent sera from individuals with coronavirus disease 2019 and those vaccinated with BNT162b2 to neutralize SARS-CoV-2 variants B1.1.7 and B.1.351 decreases, but increases after two vaccine doses. The study found that the B.1.1.7 and B.1.351 variants may have acquired partial resistance to neutralizing antibodies generated by natural infection or vaccination, particularly in individuals with low antibody levels. This suggests that the B.1.351 variant may pose a greater risk of infection in immunized individuals.

NATURE MEDICINE (2021)

Editorial Material Biochemistry & Molecular Biology

Nailing Down a Notoriously Elusive Cancer Target: Direct Inhibition of MYC by a Covalent Small Molecule

Matthew J. Henley et al.

Summary: The researchers identified a covalent MYC inhibitor that selectively targets a single cysteine residue in an unstructured region of the protein, providing a potential new approach for inhibiting MYC in cancer drug discovery.

CELL CHEMICAL BIOLOGY (2021)

Article Multidisciplinary Sciences

Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation

Daniel Wrapp et al.

SCIENCE (2020)

Article Biochemistry & Molecular Biology

Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein

Alexandra C. Walls et al.

Article Multidisciplinary Sciences

A human neutralizing antibody targets the receptor-binding site of SARS-CoV-2

Rui Shi et al.

NATURE (2020)

Article Multidisciplinary Sciences

Cross-neutralization ofSARS-CoV-2 by a human monoclonal SARS-CoV antibody

Dora Pinto et al.

NATURE (2020)

Article Biochemistry & Molecular Biology

Neutralizing nanobodies bind SARS-CoV-2 spike RBD and block interaction with ACE2

Jiangdong Huo et al.

NATURE STRUCTURAL & MOLECULAR BIOLOGY (2020)

Article Multidisciplinary Sciences

Broad neutralization of SARS-related viruses by human monoclonal antibodies

Anna Z. Wec et al.

SCIENCE (2020)

Article Multidisciplinary Sciences

SARS-CoV-2 neutralizing antibody structures inform therapeutic strategies

Christopher O. Barnes et al.

NATURE (2020)

Article Multidisciplinary Sciences

An alpaca nanobody neutralizes SARS-CoV-2 by blocking receptor interaction

Leo Hanke et al.

NATURE COMMUNICATIONS (2020)

Article Multidisciplinary Sciences

Humanized single domain antibodies neutralize SARS-CoV-2 by targeting the spike receptor binding domain

Xiaojing Chi et al.

NATURE COMMUNICATIONS (2020)

Article Biochemistry & Molecular Biology

Picomolar SARS-CoV-2 Neutralization Using Multi-Arm PEG Nanobody Constructs

Ainhoa Moliner-Morro et al.

BIOMOLECULES (2020)

Article Multidisciplinary Sciences

An ultrapotent synthetic nanobody neutralizes SARS-CoV-2 by stabilizing inactive Spike

Michael Schoof et al.

SCIENCE (2020)

Article Multidisciplinary Sciences

Versatile and multivalent nanobodies efficiently neutralize SARS-CoV-2

Yufei Xiang et al.

SCIENCE (2020)

Article Multidisciplinary Sciences

Selection, biophysical and structural analysis of synthetic nanobodies that effectively neutralize SARS-CoV-2

Tania F. Custodio et al.

NATURE COMMUNICATIONS (2020)

Article Biochemistry & Molecular Biology

Novel half-life extended anti-MIF nanobodies protect against endotoxic shock

Amanda Sparkes et al.

FASEB JOURNAL (2018)

Article Multidisciplinary Sciences

Biophysical properties of the clinical-stage antibody landscape

Tushar Jain et al.

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2017)

Article Virology

Five of Five VHHs Neutralizing Poliovirus Bind the Receptor-Binding Site

Mike Strauss et al.

JOURNAL OF VIROLOGY (2016)

Article Medicine, Research & Experimental

A strategy for risk mitigation of antibodies with fast clearance

Isidro Hoetzel et al.

Article Immunology

Nanobodies With In Vitro Neutralizing Activity Protect Mice Against H5N1 Influenza Virus Infection

Lorena Itati Ibanez et al.

JOURNAL OF INFECTIOUS DISEASES (2011)

Article Biochemical Research Methods

Transient expression and purification of chimeric heavy chain antibodies

Jianbing Zhang et al.

PROTEIN EXPRESSION AND PURIFICATION (2009)

Article Medicine, General & Internal

Human monoclonal antibody combination against SARS coronavirus: Synergy and coverage of escape mutants

Jan ter Meulen et al.

PLOS MEDICINE (2006)

Article Oncology

Efficient tumor targeting by single-domain antibody fragments of camels

V Cortez-Retamozo et al.

INTERNATIONAL JOURNAL OF CANCER (2002)