tetano
Editor, Senior Moderator
Cell Mol Immunol. 2020 Mar 19. doi: 10.1038/s41423-020-0400-4. [Epub ahead of print]
Characterization of the receptor-binding domain (RBD) of 2019 novel coronavirus: implication for development of RBD protein as a viral attachment inhibitor and vaccine.
Tai W[SUP]1[/SUP], He L[SUP]2[/SUP], Zhang X[SUP]1[/SUP], Pu J[SUP]1,[/SUP][SUP]3[/SUP], Voronin D[SUP]1[/SUP], Jiang S[SUP]4,[/SUP][SUP]5[/SUP], Zhou Y[SUP]6[/SUP], Du L[SUP]7[/SUP].
Author information
Abstract
The outbreak of Coronavirus Disease 2019 (COVID-19) has posed a serious threat to global public health, calling for the development of safe and effective prophylactics and therapeutics against infection of its causative agent, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), also known as 2019 novel coronavirus (2019-nCoV). The CoV spike (S) protein plays the most important roles in viral attachment, fusion and entry, and serves as a target for development of antibodies, entry inhibitors and vaccines. Here, we identified the receptor-binding domain (RBD) in SARS-CoV-2 S protein and found that the RBD protein bound strongly to human and bat angiotensin-converting enzyme 2 (ACE2) receptors. SARS-CoV-2 RBD exhibited significantly higher binding affinity to ACE2 receptor than SARS-CoV RBD and could block the binding and, hence, attachment of SARS-CoV-2 RBD and SARS-CoV RBD to ACE2-expressing cells, thus inhibiting their infection to host cells. SARS-CoV RBD-specific antibodies could cross-react with SARS-CoV-2 RBD protein, and SARS-CoV RBD-induced antisera could cross-neutralize SARS-CoV-2, suggesting the potential to develop SARS-CoV RBD-based vaccines for prevention of SARS-CoV-2 and SARS-CoV infection.
KEYWORDS:
2019 novel coronavirus; SARS-CoV-2; cross-neutralization; receptor-binding domain; spike protein; viral inhibitor
PMID:32203189DOI:10.1038/s41423-020-0400-4
Characterization of the receptor-binding domain (RBD) of 2019 novel coronavirus: implication for development of RBD protein as a viral attachment inhibitor and vaccine.
Tai W[SUP]1[/SUP], He L[SUP]2[/SUP], Zhang X[SUP]1[/SUP], Pu J[SUP]1,[/SUP][SUP]3[/SUP], Voronin D[SUP]1[/SUP], Jiang S[SUP]4,[/SUP][SUP]5[/SUP], Zhou Y[SUP]6[/SUP], Du L[SUP]7[/SUP].
Author information
Abstract
The outbreak of Coronavirus Disease 2019 (COVID-19) has posed a serious threat to global public health, calling for the development of safe and effective prophylactics and therapeutics against infection of its causative agent, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), also known as 2019 novel coronavirus (2019-nCoV). The CoV spike (S) protein plays the most important roles in viral attachment, fusion and entry, and serves as a target for development of antibodies, entry inhibitors and vaccines. Here, we identified the receptor-binding domain (RBD) in SARS-CoV-2 S protein and found that the RBD protein bound strongly to human and bat angiotensin-converting enzyme 2 (ACE2) receptors. SARS-CoV-2 RBD exhibited significantly higher binding affinity to ACE2 receptor than SARS-CoV RBD and could block the binding and, hence, attachment of SARS-CoV-2 RBD and SARS-CoV RBD to ACE2-expressing cells, thus inhibiting their infection to host cells. SARS-CoV RBD-specific antibodies could cross-react with SARS-CoV-2 RBD protein, and SARS-CoV RBD-induced antisera could cross-neutralize SARS-CoV-2, suggesting the potential to develop SARS-CoV RBD-based vaccines for prevention of SARS-CoV-2 and SARS-CoV infection.
KEYWORDS:
2019 novel coronavirus; SARS-CoV-2; cross-neutralization; receptor-binding domain; spike protein; viral inhibitor
PMID:32203189DOI:10.1038/s41423-020-0400-4