Measles Virus Fusion Protein: Structure, Function and Inhibition
| Autor: | Hector C. Aguilar, Michael Herren, Philippe Plattet, Lisa Alves |
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| Rok vydání: | 2016 |
| Předmět: |
Models
Molecular 0301 basic medicine Protein Folding structural changes Paramyxoviridae Protein Conformation membrane fusion lcsh:QR1-502 Review inhibitors and mechanisms of adaptation Antiviral Agents Measles neuroinvasion lcsh:Microbiology Virus Measles virus Structure-Activity Relationship 03 medical and health sciences Morbillivirus Viral entry Virology Drug Discovery fusion protein medicine Humans Protein Interaction Domains and Motifs cell entry Viral Fusion Protein Inhibitors Binding Sites biology Virus Internalization biology.organism_classification medicine.disease 3. Good health Vaccination 030104 developmental biology Infectious Diseases measles virus Host-Pathogen Interactions Immunology Receptors Virus Protein Multimerization Viral Fusion Proteins Protein Binding |
| Zdroj: | Viruses Plattet, Philippe; Alves, Lisa; Herren, Michael; Aguilar, Hector C (2016). Measles Virus Fusion Protein: Structure, Function and Inhibition. Viruses, 8(4), p. 112. Molecular Diversity Preservation International MDPI 10.3390/v8040112 Viruses, Vol 8, Iss 4, p 112 (2016) |
| DOI: | 10.3390/v8040112 |
| Popis: | Measles virus (MeV), a highly contagious member of the Paramyxoviridae family, causes measles in humans. The Paramyxoviridae family of negative single-stranded enveloped viruses includes several important human and animal pathogens, with MeV causing approximately 120,000 deaths annually. MeV and canine distemper virus (CDV)-mediated diseases can be prevented by vaccination. However, sub-optimal vaccine delivery continues to foster MeV outbreaks. Post-exposure prophylaxis with antivirals has been proposed as a novel strategy to complement vaccination programs by filling herd immunity gaps. Recent research has shown that membrane fusion induced by the morbillivirus glycoproteins is the first critical step for viral entry and infection, and determines cell pathology and disease outcome. Our molecular understanding of morbillivirus-associated membrane fusion has greatly progressed towards the feasibility to control this process by treating the fusion glycoprotein with inhibitory molecules. Current approaches to develop anti-membrane fusion drugs and our knowledge on drug resistance mechanisms strongly suggest that combined therapies will be a prerequisite. Thus, discovery of additional anti-fusion and/or anti-attachment protein small-molecule compounds may eventually translate into realistic therapeutic options. |
| Databáze: | OpenAIRE |
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