The spike protein (S) of SARS coronavirus (SARS-CoV) attaches the virus to its cellular receptor, angiotensin-converting enzyme 2 (ACE2). A defined receptor-binding domain (RBD) on S mediates this interaction. The crystal structure at 2.9 angstrom resolution of the RBD bound with the peptidase domain of human ACE2 shows that the RBD presents a gently concave surface, which cradles the N-terminal lobe of the peptidase. The atomic details at the interface between the two proteins clarify the importance of residue changes that facilitate efficient cross-species infection and human-to-human transmission. The structure of the RBD suggests ways to make truncated disulfide-stabilized RBD variants for use in the design of coronavirus vaccines.

Structure of SARS Coronavirus Spike Receptor-Binding Domain Complexed with Receptor

The trimeric SARS coronavirus (SARS-CoV) surface spike (S) glycoprotein consisting of three S1-S2 heterodimers binds the cellular receptor angiotensin-converting enzyme 2 (ACE2) and mediates fusion of the viral and cellular membranes through a pre- to postfusion conformation transition. Here, we report the structure of the SARS-CoV S glycoprotein in complex with its host cell receptor ACE2 revealed by cryo-electron microscopy (cryo-EM). The complex structure shows that only one receptor-binding domain of the trimeric S glycoprotein binds ACE2 and adopts a protruding “up” conformation. In addition, we studied the structures of the SARS-CoV S glycoprotein and its complexes with ACE2 in different in vitro conditions, which may mimic different conformational states of the S glycoprotein during virus entry. Disassociation of the S1-ACE2 complex from some of the prefusion spikes was observed and characterized. We also characterized the rosette-like structures of the clustered SARS-CoV S2 trimers in the postfusion state observed on electron micrographs. Structural comparisons suggested that the SARS-CoV S glycoprotein retains a prefusion architecture after trypsin cleavage into the S1 and S2 subunits and acidic pH treatment. However, binding to the receptor opens up the receptor-binding domain of S1, which could promote the release of the S1-ACE2 complex and S1 monomers from the prefusion spike and trigger the pre- to postfusion conformational transition.

/pdf/cryo-em-structure-of-the-sars-coronavirus-spike-glycoprotein-3r6kpa89h9.pdf

Cryo-EM structure of the SARS coronavirus spike glycoprotein in complex with its host cell receptor ACE2

Middle East respiratory syndrome coronavirus (MERS-CoV) entry inhibitors targeting spike protein

Severe acute respiratory syndrome (SARS) was the first natural disaster that challenged the Chinese people at the beginning of the twenty-first century. It was caused by a novel animal coronavirus, never recognized or characterized before. This SARS coronavirus (SARS-CoV) exploited opportunities provided by 'wet markets' in southern China to adapt to the palm civet and human. Under the positive selection pressure of human host, certain mutated lineages of the virus became readily transmissible between humans and thus caused the epidemic of 2002-2003. This review will provide first-hand information, particularly from Guangdong, China, about the initial epidemiology, the identification of the aetiological agent of the disease, the molecular evolution study of the virus, the finding of SARS-like CoV in horseshoe bats and the mechanistic analysis for the cross-host tropism transition. The substantial scientific contributions made by the Chinese scientists towards understanding the virus and the disease will be emphasized. Along with the description of the scientific discoveries and analyses, the significant impact of these researches upon the public health measurement or regulations will be highlighted. It is aimed to appreciate the concerted and coordinated global response that controlled SARS within a short period of time as well as the research strategy and methodology developed along with this process, which can be applied in response to other public health challenges, particularly the future emerging/re-merging infectious diseases.

/pdf/sars-molecular-epidemiology-a-chinese-fairy-tale-of-let159r4fb.pdf

SARS molecular epidemiology: a Chinese fairy tale of controlling an emerging zoonotic disease in the genomics era

Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein

Severe acute respiratory syndrome coronavirus (SARS-CoV) is a newly emergent virus responsible for a worldwide epidemic in 2003. The coronavirus spike proteins belong to class I fusion proteins, and are characterized by the existence of two heptad repeat (HR) regions, HR1 and HR2. The HR1 region in coronaviruses is predicted to be considerably longer than that in other type I virus fusion proteins. Therefore the exact binding sequence to HR2 from the HR1 is not clear. In this study, we defined the region of HR1 that binds to HR2 by a series of biochemical and biophysical measures. Subsequently the defined HR1 (902−952) and HR2 (1145−1184) chains, which are different from previously defined binding regions, were linked together by a flexible linker to form a single-chain construct, 2-Helix. This protein was expressed in Escherichia coli and forms a typical six-helix coiled coil bundle. Highly conserved HR regions between mouse hepatitis virus (MHV) and SARS-CoV spike proteins suggest a similar three-dimensional structure for the two fusion cores. Here, we constructed a homology model for SARS coronavirus fusion core based on our biochemical analysis and determined the MHV fusion core structure. We also propose an important target site for fusion inhibitor design and several strategies, which have been successfully used in fusion inhibitor design for human immunodeficiency virus (HIV), for the treatment of SARS infection.

Characterization of the Heptad Repeat Regions, HR1 and HR2, and Design of a Fusion Core Structure Model of the Spike Protein from Severe Acute Respiratory Syndrome (SARS) Coronavirus†

Governed by MHC Class Restriction Human TCR-Binding Affinity is

Insights into CTL Escape Immunogenic SIV Epitopes and Mamu-A*01 Complexed with Two MHC Class I: Crystal Structures of Presentation by Rhesus Macaque First Glimpse of the Peptide

L'invention concerne un recepteur de lymphocyte T soluble recombine (TCR), lequel est replie et comprend un domaine extracellulaire de TCR recombine a chaine α ou η, possedant un premier peptide heterologue C-terminal de dimerisation, ainsi qu'un domaine extracellulaire de TCR recombine a chaine β ou δ, possedant un second peptide C-terminal de dimerisation, lequel est heterodimerise de maniere specifique a l'aide du premier peptide de dimerisation, afin de former un domaine d'heterodimerisation qui peut etre un domaine bispirale. L'invention concerne egalement des sequences d'acides nucleiques codant le TCR recombine, ainsi qu'un procede de production de ce TCR recombine. On peut marquer ce TCR a l'aide d'un marqueur detectable, de maniere a permettre la detection de complexes peptidiques a CMH specifique. Dans un autre mode de realisation, on peut lier le TCR a un agent therapeutique, tel qu'un agent cytotoxique ou un immunostimulant, afin d'apporter un tel agent sur le site d'un complexe peptidique a CMH specifique.

Recepteur de lymphocyte t soluble

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Characterization of the Heptad Repeat Regions, HR1 and HR2, and Design of a Fusion Core Structure Model of the Spike Protein from Severe Acute Respiratory Syndrome (SARS) Coronavirus†

Governed by MHC Class Restriction Human TCR-Binding Affinity is

Insights into CTL Escape Immunogenic SIV Epitopes and Mamu-A*01 Complexed with Two MHC Class I: Crystal Structures of Presentation by Rhesus Macaque First Glimpse of the Peptide

Recepteur de lymphocyte t soluble