Reengineering paramyxovirus tropism

Receptor specificity is a critical determinant of viral tropism, but the capacity of viruses to switch to alternative receptors has not been extensively studied. Here, we engineered the attachment protein of an attenuated measles virus and generated truly retargeted viruses that are blind to the nat...

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Bibliographic Details
Published in:Virology (New York, N.Y.) N.Y.), 2004-11, Vol.329 (2), p.217-225
Main Authors: Hadac, Elizabeth M., Peng, Kah-Whye, Nakamura, Takafumi, Russell, Stephen J.
Format: Article
Language:English
Subjects:
ADP-ribosyl Cyclase - metabolism
ADP-ribosyl Cyclase 1
Animals
Antigens, CD - metabolism
Cercopithecus aethiops
CHO Cells
Cricetinae
Glycoproteins - metabolism
Immunoglobulins - metabolism
Measles virus
Measles virus - genetics
Measles virus - physiology
Membrane Cofactor Protein
Membrane Glycoproteins - metabolism
Paramyxovirus
Receptor specificity
Receptor, Epidermal Growth Factor - metabolism
Receptors, Cell Surface
Receptors, Virus - metabolism
Recombination, Genetic
Signaling Lymphocytic Activation Molecule Family Member 1
Tropism
Vero Cells
Viral Proteins - genetics
Viral Proteins - metabolism
Viral Proteins - physiology
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Summary:Receptor specificity is a critical determinant of viral tropism, but the capacity of viruses to switch to alternative receptors has not been extensively studied. Here, we engineered the attachment protein of an attenuated measles virus and generated truly retargeted viruses that are blind to the native receptors CD46 and SLAM, but which propagate efficiently and exclusively via alternative cellular receptors, epidermal growth factor receptor, or CD38. The engineered receptor tropisms were stably maintained during multiple serial virus passage without reversion to native receptor usage, even on cells offering the choice of both native and alternative receptors. We conclude that paramyxoviruses have a remarkably flexible and adaptable entry mechanism.
ISSN:0042-6822
1096-0341
DOI:10.1016/j.virol.2004.08.036