Measles virus attachment proteins with impaired ability to bind CD46 interact more efficiently with the homologous fusion protein

Journal Article · Mon Jan 05 00:00:00 EST 2009 · Virology

DOI:https://doi.org/10.1016/j.virol.2008.10.018· OSTI ID:21182791

Corey, Elizabeth A ^[1]; Iorio, Ronald M ^[1]

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1. Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655 (United States)

Fusion promotion by measles virus (MV) depends on an interaction between the hemagglutinin (H) and fusion (F) glycoproteins. Amino acid substitutions in MV H that drastically reduce hemagglutinating activity result in an increase in the amount of H (primarily the 74 kDa isoform) detectable in a complex with F at the cell surface. This is in direct contrast to the loss of the ability to detect a complex between the fusion protein of Newcastle disease virus and most attachment proteins that lack receptor binding activity. These opposing results provide support for the existence of different mechanisms for the regulation of fusion by these two paramyxoviruses.

• OSTI ID: 21182791
• Journal Information: Virology, Vol. 383, Issue 1; Other Information: DOI: 10.1016/j.virol.2008.10.018; PII: S0042-6822(08)00686-7; Copyright (c) 2008 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0042-6822
• Country of Publication: United States
• Language: English

Related Subjects

62 RADIOLOGY AND NUCLEAR MEDICINE
AMINO ACIDS
GLYCOPROTEINS
MEASLES VIRUS
NEWCASTLE DISEASE
RECEPTORS