Relative affinity of the human parainfluenza virus type 3 hemagglutinin-neuraminidase for sialic acid correlates with virus-induced fusion activity
Autor: | Anne Moscona, Richard W. Peluso |
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Rok vydání: | 1993 |
Předmět: |
Paramyxoviridae
viruses Immunology Hemagglutinin (influenza) In Vitro Techniques Microbiology Cell Line Cell Fusion chemistry.chemical_compound Virology Chlorocebus aethiops Animals HN Protein Cell fusion biology Lipid bilayer fusion biology.organism_classification Fusion protein Parainfluenza Virus 3 Human Cell biology Sialic acid chemistry Insect Science Sialic Acids biology.protein Receptors Virus Viral Fusion Proteins Hemagglutinin-neuraminidase Research Article |
Zdroj: | Journal of Virology. 67:6463-6468 |
ISSN: | 1098-5514 0022-538X |
Popis: | The ability of enveloped viruses to cause disease depends on their ability to enter the host cell via membrane fusion events. An understanding of these early events in infection, crucial for the design of methods of blocking infection, is needed for viruses that mediate membrane fusion at neutral pH, such as paramyxoviruses and human immunodeficiency virus. Sialic acid is the receptor for the human parainfluenza virus type 3 (HPF3) hemagglutinin-neuraminidase (HN) glycoprotein, the molecule responsible for binding of the virus to cell surfaces. In order for the fusion protein (F) of HPF3 to promote membrane fusion, the HN must interact with its receptor. In the present report, two variants of HPF3 with increased fusion-promoting phenotypes were selected and used to study the function of the HN glycoprotein in membrane fusion. Increased fusogenicity correlated with single amino acid changes in the HN protein that resulted in increased binding of the variant viruses to the sialic acid receptor. These results suggest that the avidity of binding of the HN protein to its receptor regulates the level of F protein-mediated fusion and begin to define one role of the receptor-binding protein of a paramyxovirus in the membrane fusion process. |
Databáze: | OpenAIRE |
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