A Trimerizing GxxxG Motif Is Uniquely Inserted in the Severe Acute Respiratory Syndrome (SARS) Coronavirus Spike Protein Transmembrane Domain†

Biochemistry ◽  
2006 ◽  
Vol 45 (38) ◽  
pp. 11349-11356 ◽  
Author(s):  
Eyal Arbely ◽  
Zvi Granot ◽  
Itamar Kass ◽  
Joseph Orly ◽  
Isaiah T. Arkin
Keyword(s):  
Severe Acute Respiratory Syndrome ◽  
Transmembrane Domain ◽  
Spike Protein ◽  
Sars Coronavirus ◽  
Gxxxg Motif

scholarly journals GxxxG Motif of Severe Acute Respiratory Syndrome Coronavirus Spike Glycoprotein Transmembrane Domain Is Not Involved in Trimerization and Is Not Important for Entry

2007 ◽  
Vol 81 (15) ◽  
pp. 8352-8355 ◽  
Author(s):  
Jeroen Corver ◽  
Rene Broer ◽  
Puck van Kasteren ◽  
Willy Spaan
Keyword(s):  
Severe Acute Respiratory Syndrome ◽  
Transmembrane Domain ◽  
Vital Role ◽  
Sars Coronavirus ◽  
Spike Glycoprotein ◽  
S Protein ◽  
Mutant Proteins ◽  
Gxxxg Motif

ABSTRACT Recently, a paper was published in which it was proposed that the GxxxG motif of the severe acute respiratory syndrome (SARS) coronavirus spike (S) protein transmembrane domain plays a vital role in oligomerization of the protein (E. Arbely, Z. Granot, I. Kass, J. Orly, and I. T. Arkin, Biochemistry 45:11349-11356, 2006). Here, we show that the GxxxG motif is not involved in SARS S oligomerization by trimerization analysis of S GxxxG mutant proteins. In addition, the capability of S to mediate entry of SARS S-pseudotyped particles overall was affected moderately in the mutant proteins, also arguing for a nonvital role for the GxxxG motif in SARS coronavirus entry.

scholarly journals Heterologous viral RNA export elements improve expression of severe acute respiratory syndrome (SARS) coronavirus spike protein and protective efficacy of DNA vaccines against SARS

Virology ◽  
2007 ◽  
Vol 363 (2) ◽  
pp. 288-302 ◽  
Author(s):  
Benoît Callendret ◽  
Valérie Lorin ◽  
Pierre Charneau ◽  
Philippe Marianneau ◽  
Hugues Contamin ◽  
...  
Keyword(s):  
Severe Acute Respiratory Syndrome ◽  
Dna Vaccines ◽  
Protective Efficacy ◽  
Viral Rna ◽  
Spike Protein ◽  
Sars Coronavirus ◽  
Rna Export

scholarly journals Important Role for the Transmembrane Domain of Severe Acute Respiratory Syndrome Coronavirus Spike Protein during Entry

2006 ◽  
Vol 80 (3) ◽  
pp. 1302-1310 ◽  
Author(s):  
Rene Broer ◽  
Bertrand Boson ◽  
Willy Spaan ◽  
François-Loïc Cosset ◽  
Jeroen Corver
Keyword(s):  
Severe Acute Respiratory Syndrome ◽  
Membrane Fusion ◽  
Cell Fusion ◽  
Transmembrane Domain ◽  
Cytoplasmic Tail ◽  
Transmembrane Domains ◽  
Spike Protein ◽  
Fusion Activity ◽  
Wild Type ◽  
Cell Cell

ABSTRACT The spike protein (S) of severe acute respiratory syndrome coronavirus (SARS-CoV) is responsible for receptor binding and membrane fusion. It contains a highly conserved transmembrane domain that consists of three parts: an N-terminal tryptophan-rich domain, a central domain, and a cysteine-rich C-terminal domain. The cytoplasmic tail of S has previously been shown to be required for assembly. Here, the roles of the transmembrane and cytoplasmic domains of S in the infectivity and membrane fusion activity of SARS-CoV have been studied. SARS-CoV S-pseudotyped retrovirus (SARSpp) was used to measure S-mediated infectivity. In addition, the cell-cell fusion activity of S was monitored by a Renilla luciferase-based cell-cell fusion assay. Svsv-cyt, an S chimera with a cytoplasmic tail derived from vesicular stomatitis virus G protein (VSV-G), and Smhv-tmdcyt, an S chimera with the cytoplasmic and transmembrane domains of mouse hepatitis virus, displayed wild-type-like activity in both assays. Svsv-tmdcyt, a chimera with the cytoplasmic and transmembrane domains of VSV-G, was impaired in the SARSpp and cell-cell fusion assays, showing 3 to 25% activity compared to the wild type, depending on the assay and the cells used. Examination of the oligomeric state of the chimeric S proteins in SARSpp revealed that Svsv-tmdcyt trimers were less stable than wild-type S trimers, possibly explaining the lowered fusogenicity and infectivity.

scholarly journals Recombinant Protein-Based Assays for Detection of Antibodies to Severe Acute Respiratory Syndrome Coronavirus Spike and Nucleocapsid Proteins

2007 ◽  
Vol 14 (3) ◽  
pp. 331-333 ◽  
Author(s):  
Lia M. Haynes ◽  
Congrong Miao ◽  
Jennifer L. Harcourt ◽  
Joel M. Montgomery ◽  
Mai Quynh Le ◽  
...  
Keyword(s):  
Severe Acute Respiratory Syndrome ◽  
Recombinant Protein ◽  
Sensitivity And Specificity ◽  
Immunoglobulin G ◽  
High Sensitivity ◽  
Kinetic Studies ◽  
Spike Protein ◽  
Sars Coronavirus ◽  
Nucleocapsid Proteins

ABSTRACT Recombinant severe acute respiratory syndrome (SARS) nucleocapsid and spike protein-based immunoglobulin G immunoassays were developed and evaluated. Our assays demonstrated high sensitivity and specificity to the SARS coronavirus in sera collected from patients as late as 2 years postonset of symptoms. These assays will be useful not only for routine SARS coronavirus diagnostics but also for epidemiological and antibody kinetic studies.

Interaction of a Peptide from the Pre-transmembrane Domain of the Severe Acute Respiratory Syndrome Coronavirus Spike Protein with Phospholipid Membranes

2007 ◽  
Vol 111 (49) ◽  
pp. 13714-13725 ◽  
Author(s):  
Jaime Guillén ◽  
Miguel R. Moreno ◽  
Ana J. Pérez-Berná ◽  
Angela Bernabeu ◽  
José Villalaín
Keyword(s):  
Severe Acute Respiratory Syndrome ◽  
Transmembrane Domain ◽  
Spike Protein ◽  
Phospholipid Membranes

scholarly journals Immunological imprinting of the antibody response in COVID-19 patients

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Teresa Aydillo ◽  
Alexander Rombauts ◽  
Daniel Stadlbauer ◽  
Sadaf Aslam ◽  
Gabriela Abelenda-Alonso ◽  
...  
Keyword(s):  
Immune Response ◽  
Severe Acute Respiratory Syndrome ◽  
Antibody Response ◽  
Humoral Immune Response ◽  
Nucleocapsid Protein ◽  
Spike Protein ◽  
Ongoing Research ◽  
Variable Regions ◽  
Humoral Immune ◽  
Human Coronaviruses

AbstractIn addition to severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), humans are also susceptible to six other coronaviruses, for which consecutive exposures to antigenically related and divergent seasonal coronaviruses are frequent. Despite the prevalence of COVID-19 pandemic and ongoing research, the nature of the antibody response against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is unclear. Here we longitudinally profile the early humoral immune response against SARS-CoV-2 in hospitalized coronavirus disease 2019 (COVID-19) patients and quantify levels of pre-existing immunity to OC43, HKU1 and 229E seasonal coronaviruses, and find a strong back-boosting effect to conserved but not variable regions of OC43 and HKU1 betacoronaviruses spike protein. However, such antibody memory boost to human coronaviruses negatively correlates with the induction of IgG and IgM against SARS-CoV-2 spike and nucleocapsid protein. Our findings thus provide evidence of immunological imprinting by previous seasonal coronavirus infections that can potentially modulate the antibody profile to SARS-CoV-2 infection.

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