Cryo-EM structures and binding of mouse and human ACE2 to SARS-CoV-2 variants of concern indicate that mutations enabling immune escape could expand host range.

Dongchun Ni, Priscilla Turelli, Bertrand Beckert, Sergey Nazarov, Emiko Uchikawa, Alexander Myasnikov, Florence Pojer, Didier Trono, Henning Stahlberg, Kelvin Lau

April 2023 PLoS Pathog

Synopsis of Social media discussions

Many discussions focus on how the structural insights into ACE2 binding relate to the virus's ability to infect new hosts, using phrases like 'mutations enabling immune escape' and 'expand host range,' which convey the significance and potential implications of the findings. The tone balances technical detail with recognition of the study’s importance, reflecting moderate but meaningful engagement.

A
Agreement
 Moderate agreement

Most discussions recognize the importance of the research findings, showing general agreement with its conclusions about host range and mutations.

I
Interest
 Moderate level of interest

The participants show moderate interest, highlighting the relevance for understanding virus evolution and implications for public health.

E
Engagement
 Moderate level of engagement

Comments include references to the methodology and potential consequences, indicating a reasonable level of engagement.

I
Impact
 Moderate level of impact

The discussions acknowledge that the research could influence future studies or strategies related to virus tracking and control, but do not suggest immediate drastic changes.

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20

Total Likes

5

Extended Reach

4,059

Social Features

3

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Posts referencing the article

Cryo-EM Analysis of SARS-CoV-2 Variants Binding to Mouse and Human ACE2 Receptors

Cryo-EM Analysis of SARS-CoV-2 Variants Binding to Mouse and Human ACE2 Receptors

This study investigates how SARS-CoV-2 variants bind to mouse and human ACE2 receptors using cryo-electron microscopy, revealing mutations that could expand host range and facilitate immune escape.

Social RTCL TV

August 2, 2023

20 views

  • Akio Adachi
    @RQpdPyjf1VbJKTe (Twitter)

    #PLOSPathogens: Cryo-EM structures and binding of mouse and human ACE2 to SARS-CoV-2 variants of concern indi ... https://t.co/knkJen9XGb
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    April 5, 2023

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  • Outbreak Science
    @outbreaksci (Twitter)

    New preprint: Cryo-EM structures and binding of mouse and human ACE2 to SARS-CoV-2 variants of concern indicate that mutations enabling immune escape could expand host range https://t.co/rS6OVpX1Bs #coronavirus #COVID19
    view full post

    February 3, 2023

Abstract Synopsis

  • The study investigated how different SARS-CoV-2 variants of concern (VOCs), including Beta and various Omicron subvariants, interact with the mouse ACE2 receptor using cryo-electron microscopy, revealing that certain mutations in the Spike protein allow the virus to bind to mouse cells.
  • The structural analysis shows that a combination of specific Spike mutations is necessary for the virus to effectively attach to mouse ACE2, which could mean the virus might infect a broader range of hosts.
  • Understanding these interactions helps assess the potential risk of the virus jumping to new animal species, which could impact future spillover or spillback events between humans and animals.]