Norovirus protein structure and function.

Noroviruses are positive strand RNA viruses that have received increased attention in recent years because their role as etiologic agents in acute gastroenteritis outbreaks is now clearly established. Much has been learned about the epidemiology of these viruses and the extent of genetic diversity among circulating strains. In contrast, progress on understanding the basic mechanisms of virus replication has been far slower due to the inability to cultivate virus in the laboratory. Despite this limitation, significant progress has been made in defining some basic functions of the norovirus proteins, and the structures of two have been solved to near atomic resolution. This minireview summarizes these recent advances in understanding the structure and function of the norovirus proteins and provides speculation about what roles they may play in the virus replication cycle.

[1]  A. Klip,et al.  Identification of a human homologue of the vesicle-associated membrane protein (VAMP)-associated protein of 33 kDa (VAP-33): a broadly expressed protein that binds to VAMP. , 1998, The Biochemical journal.

[2]  I. Brierley,et al.  Identification of a protein linked to the genomic and subgenomic mRNAs of feline calicivirus and its role in translation. , 1997, The Journal of general virology.

[3]  M. Hardy,et al.  Norwalk Virus Nonstructural Protein p48 Forms a Complex with the SNARE Regulator VAP-A and Prevents Cell Surface Expression of Vesicular Stomatitis Virus G Protein , 2003, Journal of Virology.

[4]  G. Meyers,et al.  Rabbit hemorrhagic disease virus: identification of a cleavage site in the viral polyprotein that is not processed by the known calicivirus protease. , 2002, Virology.

[5]  G. Belliot,et al.  Feline Calicivirus VP2 Is Essential for the Production of Infectious Virions , 2005, Journal of Virology.

[6]  D. Baltimore,et al.  Poliovirus mutant that contains a cold-sensitive defect in viral RNA synthesis , 1988, Journal of virology.

[7]  C. Cameron,et al.  Isolation of Enzymatically Active Replication Complexes from Feline Calicivirus-Infected Cells , 2002, Journal of Virology.

[8]  E. Wimmer,et al.  Polypeptide p41 of a Norwalk-Like Virus Is a Nucleic Acid-Independent Nucleoside Triphosphatase , 2001, Journal of Virology.

[9]  Larissa B. Thackray,et al.  Replication of Norovirus in Cell Culture Reveals a Tropism for Dendritic Cells and Macrophages , 2004, PLoS biology.

[10]  K. Green,et al.  Mutagenesis of Tyrosine 24 in the VPg Protein Is Lethal for Feline Calicivirus , 2004, Journal of Virology.

[11]  C. Wirblich,et al.  Genetic map of the calicivirus rabbit hemorrhagic disease virus as deduced from in vitro translation studies , 1996, Journal of virology.

[12]  J. Neill Nucleotide sequence of a region of the feline calicivirus genome which encodes picornavirus-like RNA-dependent RNA polymerase, cysteine protease and 2C polypeptides. , 1990, Virus research.

[13]  A. Gorbalenya,et al.  Norwalk Virus N-Terminal Nonstructural Protein Is Associated with Disassembly of the Golgi Complex in Transfected Cells , 2004, Journal of Virology.

[14]  K. Green,et al.  RNA transcripts derived from a cloned full-length copy of the feline calicivirus genome do not require VpG for infectivity. , 1995, Virology.

[15]  G. Meyers Translation of the Minor Capsid Protein of a Calicivirus Is Initiated by a Novel Termination-dependent Reinitiation Mechanism* , 2003, Journal of Biological Chemistry.

[16]  K. Kirkegaard,et al.  Inhibition of endoplasmic reticulum-to-Golgi traffic by poliovirus protein 3A: genetic and ultrastructural analysis , 1997, Journal of virology.

[17]  E. Wimmer,et al.  The 5'-terminal structures of poliovirion RNA and poliovirus mRNA differ only in the genome-linked protein VPg. , 1977, Proceedings of the National Academy of Sciences of the United States of America.

[18]  S. Harrison,et al.  Tomato bushy stunt virus at 5.5-Å resolution , 1977, Nature.

[19]  R. Lloyd,et al.  Calicivirus 3C-Like Proteinase Inhibits Cellular Translation by Cleavage of Poly(A)-Binding Protein , 2004, Journal of Virology.

[20]  A. Paul,et al.  Protein-primed RNA synthesis by purified poliovirus RNA polymerase , 1998, Nature.

[21]  T. Miyamura,et al.  Identification of Active-Site Amino Acid Residues in the Chiba Virus 3C-Like Protease , 2002, Journal of Virology.

[22]  C. Fraser,et al.  The genome‐linked protein VPg of the Norwalk virus binds eIF3, suggesting its role in translation initiation complex recruitment , 2003, The EMBO journal.

[23]  M. Estes,et al.  Three-dimensional structure of baculovirus-expressed Norwalk virus capsids , 1994, Journal of virology.

[24]  M G Rossmann,et al.  X-ray crystallographic structure of the Norwalk virus capsid. , 1999, Science.

[25]  B. Semler,et al.  Protein 3CD is the major poliovirus proteinase responsible for cleavage of the P1 capsid precursor. , 1988, Virology.

[26]  K. Green,et al.  Identification and genomic mapping of the ORF3 and VPg proteins in feline calicivirus virions. , 2000, Virology.

[27]  T. Miyamura,et al.  Interaction of Recombinant Norwalk Virus Particles with the 105-Kilodalton Cellular Binding Protein, a Candidate Receptor Molecule for Virus Attachment , 2000, Journal of Virology.

[28]  J. Laliberté,et al.  Complex Formation between Potyvirus VPg and Translation Eukaryotic Initiation Factor 4E Correlates with Virus Infectivity , 2000, Journal of Virology.

[29]  C. Wobus,et al.  STAT1-Dependent Innate Immunity to a Norwalk-Like Virus , 2003, Science.

[30]  F. Parra,et al.  Identification of the Amino Acid Residue Involved in Rabbit Hemorrhagic Disease Virus VPg Uridylylation* , 2001, The Journal of Biological Chemistry.

[31]  L. McCaig,et al.  Food-related illness and death in the United States. , 1999, Emerging infectious diseases.

[32]  D. Graham,et al.  Expression, self-assembly, and antigenicity of the Norwalk virus capsid protein , 1992, Journal of virology.

[33]  M. Hardy,et al.  Substrate specificity of the Norwalk virus 3C-like proteinase. , 2002, Virus research.

[34]  F. Parra,et al.  Expression of Enzymatically Active Rabbit Hemorrhagic Disease Virus RNA-Dependent RNA Polymerase in Escherichia coli , 1998, Journal of Virology.

[35]  A. Haenni,et al.  Proteins attached to viral genomes are multifunctional. , 2001, Advances in virus research.

[36]  K. Ng,et al.  Crystal Structure of Norwalk Virus Polymerase Reveals the Carboxyl Terminus in the Active Site Cleft* , 2004, Journal of Biological Chemistry.

[37]  P. J. Wright,et al.  Variation in ORF3 of genogroup 2 Norwalk-like viruses , 1999, Archives of Virology.

[38]  J. Neill,et al.  Further characterization of the virus-specific RNAs in feline calicivirus infected cells , 1988, Virus Research.

[39]  G. Belliot,et al.  In Vitro Proteolytic Processing of the MD145 Norovirus ORF1 Nonstructural Polyprotein Yields Stable Precursors and Products Similar to Those Detected in Calicivirus-Infected Cells , 2003, Journal of Virology.

[40]  Laura J. White,et al.  Norwalk Virus Open Reading Frame 3 Encodes a Minor Structural Protein , 2000, Journal of Virology.

[41]  Marion Koopmans,et al.  Viral Gastroenteritis Outbreaks in Europe, 1995–2000 , 2003, Emerging infectious diseases.

[42]  Marc Allaire,et al.  Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases , 1994, Nature.

[43]  J. Meller,et al.  Mutations within the P2 Domain of Norovirus Capsid Affect Binding to Human Histo-Blood Group Antigens: Evidence for a Binding Pocket , 2003, Journal of Virology.

[44]  M. Rossmann,et al.  X-ray Crystallographic Structure of the Norwalk Virus , 1999 .

[45]  M. James,et al.  Crystal Structures of Active and Inactive Conformations of a Caliciviral RNA-dependent RNA Polymerase* , 2002, The Journal of Biological Chemistry.

[46]  P. J. Wright,et al.  Open Reading Frame 1 of the Norwalk-Like Virus Camberwell: Completion of Sequence and Expression in Mammalian Cells , 1999, Journal of Virology.

[47]  C. Cameron,et al.  Proteinase-Polymerase Precursor as the Active Form of Feline Calicivirus RNA-Dependent RNA Polymerase , 2001, Journal of Virology.

[48]  F. Brown,et al.  Presence of a covalently linked protein on calicivirus RNA. , 1978, The Journal of general virology.

[49]  M. Estes,et al.  Replication and packaging of Norwalk virus RNA in cultured mammalian cells. , 2005, Proceedings of the National Academy of Sciences of the United States of America.

[50]  G. Stanway,et al.  The 2A proteins of three diverse picornaviruses are related to each other and to the H-rev107 family of proteins involved in the control of cell proliferation. , 2000, The Journal of general virology.

[51]  D. Matthews,et al.  Structure of human rhinovirus 3C protease reveals a trypsin-like polypeptide fold, RNA-binding site, and means for cleaving precursor polyprotein , 1994, Cell.

[52]  J. Ziebuhr,et al.  Virus-encoded proteinases and proteolytic processing in the Nidovirales. , 2000, The Journal of general virology.

[53]  M. Estes,et al.  Taxonomy of the caliciviruses. , 2000, The Journal of infectious diseases.

[54]  G. Viljoen,et al.  Identification of further proteolytic cleavage sites in the Southampton calicivirus polyprotein by expression of the viral protease in E. coli. , 1999, The Journal of general virology.

[55]  K. Kasschau,et al.  Loss-of-Susceptibility Mutants of Arabidopsis thaliana Reveal an Essential Role for eIF(iso)4E during Potyvirus Infection , 2002, Current Biology.

[56]  D. R. Taylor,et al.  Hepatitis C virus RNA polymerase and NS5A complex with a SNARE-like protein. , 1999, Virology.

[57]  M. James,et al.  The refined crystal structure of the 3C gene product from hepatitis A virus: specific proteinase activity and RNA recognition , 1997, Journal of virology.

[58]  M. Estes,et al.  Structural Requirements for the Assembly of Norwalk Virus-Like Particles , 2002, Journal of Virology.

[59]  I. Clarke,et al.  Polyprotein processing in Southampton virus: identification of 3C-like protease cleavage sites by in vitro mutagenesis , 1996, Journal of virology.

[60]  J. Arnold,et al.  Norovirus Proteinase-Polymerase and Polymerase Are Both Active Forms of RNA-Dependent RNA Polymerase , 2005, Journal of Virology.