Structural Studies of the Parainfluenza Virus 5 Hemagglutinin-Neuraminidase Tetramer in Complex with Its Receptor, Sialyllactose

Title: Structural Studies of the Parainfluenza Virus 5 Hemagglutinin-Neuraminidase Tetramer in Complex with Its Receptor, Sialyllactose

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Abstract

The paramyxovirus hemagglutinin-neuraminidase (HN) functions in virus attachment to cells, cleavage of sialic acid from oligosaccharides, and stimulating membrane fusion during virus entry into cells. The structural basis for these diverse functions remains to be fully understood. We report the crystal structures of the parainfluenza virus 5 (SV5) HN and its complexes with sialic acid, the inhibitor DANA, and the receptor sialyllactose. SV5 HN shares common structural features with HN of Newcastle disease virus (NDV) and human parainfluenza 3 (HPIV3), but unlike the previously determined HN structures, the SV5 HN forms a tetramer in solution, which is thought to be the physiological oligomer. The sialyllactose complex reveals intact receptor within the active site, but no major conformational changes in the protein. The SV5 HN structures do not support previously proposed models for HN action in membrane fusion and suggest alternative mechanisms by which HN may promote virus entry into cells.

Authors:

Yuan, Ping; Thompson, Thomas B; Wurzburg, Beth A; Paterson, Reay G; Lamb, Robert A; Jardetzky, Theodore S ^[1]

Publication Date:: 2010-03-08

Research Org.:: Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Sponsoring Org.:: USDOE

OSTI Identifier:: 1008596

Resource Type:: Journal Article

Journal Name:: Structure

Additional Journal Information:: Journal Volume: 13; Journal Issue: (5) ; 05, 2005

Country of Publication:: United States

Language:: ENGLISH

Subject:: 36 MATERIALS SCIENCE; CLEAVAGE; CONFORMATIONAL CHANGES; CRYSTAL STRUCTURE; MEMBRANES; NEWCASTLE DISEASE; OLIGOSACCHARIDES; SIALIC ACID

Citation Formats


                    Yuan, Ping, Thompson, Thomas B, Wurzburg, Beth A, Paterson, Reay G, Lamb, Robert A, and Jardetzky, Theodore S. Structural Studies of the Parainfluenza Virus 5 Hemagglutinin-Neuraminidase Tetramer in Complex with Its Receptor, Sialyllactose.  United States: N. p., 2010. 
        Web.

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                    Yuan, Ping, Thompson, Thomas B, Wurzburg, Beth A, Paterson, Reay G, Lamb, Robert A, & Jardetzky, Theodore S. Structural Studies of the Parainfluenza Virus 5 Hemagglutinin-Neuraminidase Tetramer in Complex with Its Receptor, Sialyllactose.  United States.

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                    Yuan, Ping, Thompson, Thomas B, Wurzburg, Beth A, Paterson, Reay G, Lamb, Robert A, and Jardetzky, Theodore S. Mon .  
        "Structural Studies of the Parainfluenza Virus 5 Hemagglutinin-Neuraminidase Tetramer in Complex with Its Receptor, Sialyllactose".  United States.

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@article{osti_1008596,

  title        = {Structural Studies of the Parainfluenza Virus 5 Hemagglutinin-Neuraminidase Tetramer in Complex with Its Receptor, Sialyllactose},

  author       = {Yuan, Ping and Thompson, Thomas B and Wurzburg, Beth A and Paterson, Reay G and Lamb, Robert A and Jardetzky, Theodore S},

  abstractNote = {The paramyxovirus hemagglutinin-neuraminidase (HN) functions in virus attachment to cells, cleavage of sialic acid from oligosaccharides, and stimulating membrane fusion during virus entry into cells. The structural basis for these diverse functions remains to be fully understood. We report the crystal structures of the parainfluenza virus 5 (SV5) HN and its complexes with sialic acid, the inhibitor DANA, and the receptor sialyllactose. SV5 HN shares common structural features with HN of Newcastle disease virus (NDV) and human parainfluenza 3 (HPIV3), but unlike the previously determined HN structures, the SV5 HN forms a tetramer in solution, which is thought to be the physiological oligomer. The sialyllactose complex reveals intact receptor within the active site, but no major conformational changes in the protein. The SV5 HN structures do not support previously proposed models for HN action in membrane fusion and suggest alternative mechanisms by which HN may promote virus entry into cells.},

  doi          = {},

  url          = {https://www.osti.gov/biblio/1008596},
  journal      = {Structure},
number       = (5) ; 05, 2005,

  volume       = 13,

  place        = {United States},

  year         = {2010},

  month        = {3}

}

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