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Structure and function study of paramyxovirus fusion protein heptad repeat peptides
- Source :
-
Archives of Biochemistry & Biophysics . Apr2005, Vol. 436 Issue 2, p316-322. 7p. - Publication Year :
- 2005
-
Abstract
- Abstract: Paramyxovirus might adopt a molecular mechanism of membrane fusion similar to that of other class I viruses in which the heptad repeat (HR) regions of fusion protein (F) HR1 and HR2 form a six-helix bundle structure inducing membrane fusion. In this study, we examined the structure and function of HR1 and HR2 from the avian paramyxovirus-2 (APMV-2) F protein. The study showed that APMV-2 HR1 and HR2 formed a stable six-helix bundle. Only a soluble APMV-2 HR2 peptide showed potent and specific virus-cell fusion inhibition activity. Cross-inhibiting activity with APMV-1 (Newcastle disease virus, NDV) was not found. A possible mechanism of membrane fusion inhibition by the paramyxovirus HR2 peptide is discussed. [Copyright &y& Elsevier]
- Subjects :
- *BIOLOGICAL membranes
*CELL membranes
*VIRUSES
*NEWCASTLE disease
*PARAMYXOVIRUSES
Subjects
Details
- Language :
- English
- ISSN :
- 00039861
- Volume :
- 436
- Issue :
- 2
- Database :
- Academic Search Index
- Journal :
- Archives of Biochemistry & Biophysics
- Publication Type :
- Academic Journal
- Accession number :
- 16837573
- Full Text :
- https://doi.org/10.1016/j.abb.2005.02.004