Adaptation of Canine Distemper Virus to Canine Footpad Keratinocytes Modifies Polymerase Activity and Fusogenicity Through Amino Acid Substitutions in the P/V/C and H Proteins.
From: Institut de Biotechnologie, Bâtiment de Biologie, University of Lausanne, CH-1015 Lausanne, Switzerland.
Virology
- Publish Date: Mar 2007
- ISSN: 0042-6822
- Volume: 359
- Issue: 1
- Pages: 6-18
- Medium: Print
- Language: English
- Citation (JAMA): Rivals Jean-Paul, Plattet Philippe, Currat-Zweifel Christine, et al. Adaptation of Canine Distemper Virus to Canine Footpad Keratinocytes Modifies Polymerase Activity and Fusogenicity Through Amino Acid Substitutions in the P/V/C and H Proteins.. Virology Mar 2007;359:6-18
Abstract
The wild-type canine distemper virus (CDV) strain A75/17 induces a non-cytocidal infection in cultures of canine footpad keratinocytes (CFKs) but produces very little progeny virus. After only three passages in CFKs, the virus produced 100-fold more progeny and induced a limited cytopathic effect. Sequence analysis of the CFK-adapted virus revealed only three amino acid differences, of which one was located in each the P/V/C, M and H proteins. In order to assess which amino acid changes were responsible for the increase of infectious virus production and altered phenotype of infection, we generated a series of recombinant viruses. Their analysis showed that the altered P/V/C proteins were responsible for the higher levels of virus progeny formation and that the amino acid change in the cytoplasmic tail of the H protein was the major determinant of cytopathogenicity.
Mesh Headings (Keywords): Adaptation, Biological, Amino Acid Substitution, Animals, Cell Line, Cells, Cultured, Cytopathogenic Effect, Viral, DNA Mutational Analysis, DNA-Directed RNA Polymerases, Distemper Virus, Canine, Dogs, Keratinocytes, Mutation, Missense, Plaque Assay, Proteins, Recombination, Genetic, Viral Proteins
Check for Full Text / PubMed Unique Identifier (PMID): 17046044
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