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

2020/08/08 by in news

The SARS-CoV-2 virus is more transmissible than previous coronaviruses and causes a more serious illness than influenza. The SARS-CoV-2 receptor binding domain (RBD) of the spike protein binds to the human angiotensin-converting enzyme 2 (ACE2) receptor as a prelude to viral entry into the cell. Using a naive llama single-domain antibody library and PCR-based maturation, we have produced two closely related nanobodies, H11-D4 and H11-H4, that bind RBD (KD of 39 and 12 nM, respectively) and block its interaction with ACE2. Single-particle cryo-EM revealed that both nanobodies bind to all three RBDs in the spike trimer. Crystal structures of each nanobody–RBD complex revealed how both nanobodies recognize the same epitope, which partly overlaps with the ACE2 binding surface, explaining the blocking of the RBD–ACE2 interaction. Nanobody-Fc fusions showed neutralizing activity against SARS-CoV-2 (4–6 nM for H11-H4, 18 nM for H11-D4) and additive neutralization with the SARS-CoV-1/2 antibody CR3022.

Reference: The Journal of Nature Structural & Molecular Biology

Published: 13 July 2020

Prepare news: Roghaye Mansoori

Membership of Iranian Society of Nanomedicine

The SARS-CoV-2 virus is more transmissible than previous coronaviruses and causes a more serious illness than influenza. The SARS-CoV-2 receptor binding domain (RBD) of the spike protein binds to the human angiotensin-converting enzyme 2 (ACE2) receptor as a prelude to viral entry into the cell. Using a naive llama single-domain antibody library and PCR-based maturation, we have produced two closely related nanobodies, H11-D4 and H11-H4, that bind RBD (KD of 39 and 12 nM, respectively) and block its interaction with ACE2. Single-particle cryo-EM revealed that both nanobodies bind to all three RBDs in the spike trimer. Crystal structures of each nanobody–RBD complex revealed how both nanobodies recognize the same epitope, which partly overlaps with the ACE2 binding surface, explaining the blocking of the RBD–ACE2 interaction. Nanobody-Fc fusions showed neutralizing activity against SARS-CoV-2 (4–6 nM for H11-H4, 18 nM for H11-D4) and additive neutralization with the SARS-CoV-1/2 antibody CR3022.

Reference: The Journal of Nature Structural & Molecular Biology

Published: 13 July 2020

Prepare news: Roghaye Mansoori

membership of Iranian Society of Nanomedicine

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    Introduction:
    The Iranian Society of Nanomedicine (ISNM) is an independent membership organization which represents professionals at M.Sc degree and above in all fields of the nanomedicine science.
    ISNM was established in order to promote and develop medical nanotechnology in Iran.
    We are going to achieve all the goals and following purposes related to medical nanotechnology.
    Purpose of association:
    1. Quantitative and qualitative support of knowledge-base association
    2. Prevalence of earned technical knowledge in universities and industries
    3. Consolidation and improvement of internal and external cooperation through following and implanting of common plans
    4. Giving professional consultation to universities, researching centers and industries related to nanomedicine technology
    5. Holding conferences, seminars, workshops and professional courses

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