Structure of a human common cold virus and functional relationship to other picornaviruses

  title={Structure of a human common cold virus and functional relationship to other picornaviruses},
  author={Michael G. Rossmann and Eddy Arnold and John W. Erickson and Elizabeth A. Frankenberger and James P. Griffith and Hans J{\"u}rgen Hecht and John E. Johnson and Greg Kamer and Ming Luo and Anne G. Mosser and Roland R. Rueckert and Barbara Sherry and Gerrit Vriend},
We report the first atomic resolution structure of an animal virus, human rhinovirus 14. It is strikingly similar to known icosahedral plant RNA viruses. Four neutralizing immunogenic regions have been identified. These, and corresponding antigenic sequences of polio and foot-and-mouth disease viruses, reside on external protrusions. A large cleft on each icosahedral face is probably the host cell receptor binding site. 

Structural insight into insect viruses

The first structure of an insect picorna-(small RNA-containing) virus is now available and is associated with the small, internal, functionally essential, VP4 protein.

Crystal Structure of Human Enterovirus 71

The structure of a virus linked to neurological disease reveals how drugs targeting viruses in this family can be modified. Enterovirus 71 is a picornavirus associated with fatal neurological illness

The Structure and Host Entry of an Invertebrate Parvovirus

Structural comparisons show that vertebrate and invertebrate parvoviruses have evolved independently, although there are common structural features among all parVovirus capsid proteins.

The crystal structure of cricket paralysis virus: the first view of a new virus family

The genome sequence indicates that the insect picorna-like viruses represent a distinct lineage compared to true picornaviruses, and the capsid structure demonstrates that the two groups are related.

Functional aspects of the capsid structure of Mengo virus.

  • D. Scraba
  • Biology
    Journal of structural biology
  • 1990

Structure of Ljungan virus provides insight into genome packaging of this picornavirus

The atomic structure of Ljungan virus, the type member of the genus Parechovirus B, which has been linked to diabetes and myocarditis in humans, is reported, showing remarkable features, including an extended VP1 C terminus, forming a major protuberance on the outer surface of the virus.

Picornaviruses at the Molecular Level

Picornaviruses include the etiological agents of a large number of human and animal diseases such as hepatitis A, poliomyelitis, common cold, foot-and-mouth disease (FAMD) of cloven-foot animals, encephalomyocarditis (EMC), among others.

Implications for viral uncoating from the structure of bovine enterovirus

We have determined the crystal structure of a bovine enterovirus, revealing that the topologies of the major capsid proteins and the overall architecture of the virion are similar to those of related

Common Features in the Design of Small RNA Viruses

This chapter summarizes what is known about the design of icosahedral, positive-strand RNA viruses, and discusses possible functional reasons for the common structural features.

The structure of human parvovirus B19.

The structure of recombinant B19-like particles has been determined to approximately 3.5-A resolution by x-ray crystallography and, to the authors' knowledge, represents the first near-atomic structure of an Erythrovirus.



Location and primary structure of a major antigenic site for poliovirus neutralization

A major antigenic site for virusneutralization on the capsid protein VP1 of poliovirus type 3 is determined, providing the basis for an improved understanding of the molecular basis of virus neutralization.

The complete nucleotide sequence of a common cold virus: human rhinovlrus 14

Comparison of the nucleotide sequence and the predicted amino acid sequence with those of the polioviruses reveals a surprising degree of homology which may allow recognition of regions of antigenic importance and prediction of the virus polyprotein cleavage sites.

Critical role of an eight-amino acid sequence of VP1 in neutralization of poliovirus type 3

The three serotypes of poliovirus are members of the picornaviradae, a group of viruses which cause a variety of diseases of considerable importance in man and animals. We have previously used

Preliminary studies of crystals of poliovirus type I.

  • J. Hogle
  • Chemistry
    Journal of molecular biology
  • 1982

Antibodies against a preselected peptide recognize and neutralize foot and mouth disease virus.

A major antibody combining site on foot and mouth disease virus (FMDV) serotype O1K has been identified in a predicted surface helix of viral protein 1 (VP1) between amino acid residues 144 and 159, which elicits high titers of antibodies that specifically recognize and neutralize FMDV.

Similarity in gene organization and homology between proteins of animal picornaviruses and a plant comovirus suggest common ancestry of these virus families.

The amino acid sequences deduced from the nucleic acid sequences of several animal picornaviruses and cowpea mosaic virus and CPMV, a plant virus, were compared to conclude that the proteinases encoded by these viruses are probably cysteine proteinases, mechanistically related, but not homologous to papain.

Immunogenic and cell attachment sites of FMDV: further evidence for their location in a single capsid polypeptide.

Treatment of strains from five other serotypes of the virus with the two enzymes cleaved only VP1 in each instance and there was a corresponding loss of infectivity and a lower immunogenicity.

Synthetic peptides from four separate regions of the poliovirus type 1 capsid protein VP1 induce neutralizing antibodies.

The neutralizing determinants on VP1 reside in specific noncontiguous regions of the protein and can be defined by specific peptides from these regions.