Structure analysis of the receptor binding of 2019-nCoV.

Yun Chen, Yao Guo, Yihang Pan, Zhizhuang Joe Zhao

February 2020 Biochem Biophys Res Commun

Synopsis of Social media discussions

The discussions revolve around detailed molecular insights, such as the conserved glycosylation site N343 and the stronger binding of the virus to the ACE2 receptor. The tone reflects curiosity and scientific curiosity, with examples like references to structural comparisons between SARS-CoV and 2019-nCoV, emphasizing the relevance of the research for understanding viral transmission and potential treatments.

A
Agreement
 Moderate agreement

Most discussions support the findings of the structural analysis, emphasizing the importance of the receptor binding details and its implications.

I
Interest
 High level of interest

The conversations demonstrate high interest, with many users engaging deeply through technical details and scientific references.

E
Engagement
 Moderate level of engagement

Participants reference specific amino acid residues, molecular modeling, and broader implications, showing moderate but meaningful engagement.

I
Impact
 Moderate level of impact

The discussions highlight the significance of the study in understanding virus-host interactions and potential transmission routes, indicating a moderate impact.

Social Mentions

YouTube

2 Videos

Facebook

1 Posts

Twitter

10 Posts

News

2 Articles

Metrics

Video Views

2,189

Total Likes

22

Extended Reach

135,029

Social Features

15

Timeline: Posts about article

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  • Leek a Week
    @leekaweek (Twitter)

    https://t.co/EGC9V7ThEA A structural analysis of the #SARSCoV2 virus confirms that "N330 corresponds to N343 in the spike glycoprotein of 2019-nCoV [SARS-CoV-2] and is a conserved glycosylation site" - so what was called N330 on SARS-CoV is still around, now called N343. 10/n
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    December 27, 2021

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    @pharmad_281 (Twitter)

    Structure analysis of the receptor binding of 2019-nCoV - ScienceDirect https://t.co/Z0Y6X0cZgD
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    May 15, 2020

  • airi.clip
    @AiriClip (Twitter)

    TERAPIA SPERIMENTALE (DOI:10.1016/j.bbrc.2020.02.071) https://t.co/X3tvV6XAqG #Coronavirus #COVID19 #ACE2 #ACE1 #RBD #RBDReceptorBindingDomain #Spike #SpikeProtein
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    March 31, 2020

  • Saba Azarpeik
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    RT @Amirbio2: @mohammadsarmast @sabaazarpeik خیلی دوست داری مقاله علمی بخونی این رو بخون بعد برام تعریف کن ببینم چی به چی شد!! https://t.c…
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    March 18, 2020

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    @mohammadsarmast @sabaazarpeik خیلی دوست داری مقاله علمی بخونی این رو بخون بعد برام تعریف کن ببینم چی به چی شد!! https://t.co/scLEx2yOdg
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    March 18, 2020

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    Trend up+1: *Chen Y* et al (Biochem Biophys Res Commun) __Structure analysis of the receptor binding of 2019-nCoV__ https://t.co/CrmgfeR0tc
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    February 24, 2020

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    Trend up+1: *Chen Y* et al (Biochem Biophys Res Commun) __Structure analysis of the receptor binding of 2019-nCoV__ https://t.co/CrmgfeR0tc
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    February 23, 2020

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    Trend up+6: *Chen Y* et al (Biochem Biophys Res Commun) __Structure analysis of the receptor binding of 2019-nCoV__ https://t.co/CrmgfeR0tc
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    Trend new: *Chen Y* et al (Biochem Biophys Res Commun) __Structure analysis of the receptor binding of 2019-nCoV__ https://t.co/CrmgfeR0tc
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    February 23, 2020

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    New article: Structure analysis of the receptor binding of 2019-nCoV. https://t.co/sM4Iz8DBD4 #coronavirus #wuhan #2019ncov
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    February 22, 2020

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Abstract Synopsis

  • The study analyzes how the COVID-19 virus (2019nCoV) binds to human cells, focusing on its spike protein's receptor binding domain (RBD), which is similar but slightly different from the SARS virus, especially in a flexible loop with a key phenylalanine residue that enhances binding to the ACE2 receptor.
  • Molecular modeling shows that 2019nCoV's RBD binds more strongly to ACE2, which is found in many animals, suggesting that animals could be natural hosts for the virus and that it might infect a wide range of species.
  • The primary transmission is through respiratory droplets, but since ACE2 is also present in the intestines, testis, and kidneys, other routes like fecal-oral transmission are possible; developing antibodies or inhibitors to block the virus-ACE2 interaction is a potential strategy to fight the virus.]