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.
Explore this paper's citation graph
Summary
A homology model for SARS coronavirus fusion core is constructed based on biochemical analysis and the MHV fusion core structure is determined, which proposes an important target site for fusion inhibitor design and several strategies, which have been successfully used in fusion inhibitors design for human immunodeficiency virus (HIV), for the treatment of SARS infection.
- Type
- article
- Published
- 2004-10-13
- Cited by
- 58
- References
- 34
- OpenAlex
- https://openalex.org/W2012521659
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:15113152
Keywords
Heptad repeat, Coronavirus, Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), Core (optical fiber), Severe acute respiratory syndrome coronavirus
References
- Coiled coils in both intracellular vesicle and viral membrane fusion.
- Structural characterization of the human respiratory syncytial virus fusion protein core.
- Biochemical and biophysical analysis of heptad repeat regions from the fusion protein of Menangle virus, a newly emergent paramyxovirus
- Core structure of the envelope glycoprotein GP2 from Ebola virus at 1.9-A resolution.
- Structure of influenza haemagglutinin at the pH of membrane fusion
- Basis for fusion inhibition by peptides: analysis of the heptad repeat regions of the fusion proteins from Nipah and Hendra viruses, newly emergent zoonotic paramyxoviruses.
- HIV entry and its inhibition.
- Structural Characterization of the SARS-Coronavirus Spike S Fusion Protein Core
- Membrane fusion mediated by coiled coils: a hypothesis.
- Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection.
- The fusion protein core of measles virus forms stable coiled-coil trimer.
- Atomic structure of the ectodomain from HIV-1 gp41
- Structural basis for paramyxovirus-mediated membrane fusion.
- Protein Design of an HIV-1 Entry Inhibitor
- The Fusion glycoprotein shell of Semliki Forest virus: an icosahedral assembly primed for fusogenic activation at endosomal pH.
- Inhibiting HIV-1 entry: discovery of D-peptide inhibitors that target the gp41 coiled-coil pocket.
- The Coronavirus Spike Protein Is a Class I Virus Fusion Protein: Structural and Functional Characterization of the Fusion Core Complex
- Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin.
- Coronavirus IBV: structural characterization of the spike protein.
- Interaction between heptad repeat 1 and 2 regions in spike protein of SARS-associated coronavirus: implications for virus fusogenic mechanism and identification of fusion inhibitors
Cited by
- Dissection of the Fusion Machine of Sars-Coronavirus
- Development of Instantaneous Protection against SARS-CoV with Implications for Multiple RNA Viruses
- Influence of hydrophobic and electrostatic residues on SARS-coronavirus S2 protein stability: Insights into mechanisms of general viral fusion and inhibitor design
- Structure of SARS Coronavirus Spike Receptor-Binding Domain Complexed with Receptor
- Characterization of neutralizing monoclonal antibodies recognizing a 15-residues epitope on the spike protein HR2 region of severe acute respiratory syndrome coronavirus (SARS-CoV)
- Biophysical characterization of HRC peptide analogs interaction with heptad repeat regions of the SARS-coronavirus Spike fusion protein core
- Central ions and lateral asparagine/glutamine zippers stabilize the post-fusion hairpin conformation of the SARS coronavirus spike glycoprotein
- A second SARS-CoV S2 glycoprotein internal membrane-active peptide. Biophysical characterization and membrane interaction.
- iPEP: peptides designed and selected for interfering with protein interaction and function.
- Identification of synthetic vaccine candidates against SARS CoV infection
- Membrane insertion of the three main membranotropic sequences from SARS-CoV S2 glycoprotein
- Characterization of HCoV-229E fusion core: Implications for structure basis of coronavirus membrane fusion
- Substitution at Aspartic Acid 1128 in the SARS Coronavirus Spike Glycoprotein Mediates Escape from a S2 Domain-Targeting Neutralizing Monoclonal Antibody
- Role of hydrophobic and electrostatic interactions in coiled coil stability and specificity.
- Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein
- Biochemical and biophysical characterization of the transmissible gastroenteritis coronavirus fusion core
- Middle East respiratory syndrome coronavirus (MERS-CoV) entry inhibitors targeting spike protein
- Positive aspects of negative design: simultaneous selection of specificity and interaction stability.
- Ready, Set, Fuse! The Coronavirus Spike Protein and Acquisition of Fusion Competence
- Interaction of a peptide from the pre-transmembrane domain of the severe acute respiratory syndrome coronavirus spike protein with phospholipid membranes.
Related papers
- Coronavirus Main Proteinase (3CLpro) Structure: Basis for Design of Anti-SARS Drugs
- Progress About Coronavirus Main Proteinase and Its Inhibitors
- Bioinfomatics analysis on genome and protein of Bat SARS coronavirus HKU3-1
- Study on Characteristics of SARS Coronavirus Based on Z Curve
- Prediction of the Function of SARS Proteins by Using a Support Vector Machine Program SVMProt
- Prediction of quaternary assembly of SARS coronavirus peplomer
- A Perspective of Viruses and the Outbreak of a Novel Coronavirus SARS-CoV- 2
- The Identification of the Nucleocapsid Protein of the SARS Coronavirus by Mass Spectrometor
- Continuously active disinfectant inactivates severe acute respiratory coronavirus virus 2 (SARS-CoV-2) and human coronavirus 229E two days after the disinfectant was applied and following wear exposures