Molecular relationships between 21 human rhinovirus serotypes.

We have analysed, by PCR using consensus primers followed by sequencing, 12 human rhinoviruses (HRVs) in a genomic region including that corresponding to the immunogenic site NIm-II. Together with published information, 21 sequences are available for comparison. In the region analysed, which encodes 112 amino acids, the majority (18) of the serotypes exhibited at least 70% amino acid identity to one another and some serotypes are very closely related. These include HRV-36, -58 and -89, known to exhibit antigenic cross reactivity, which were shown to differ at only three amino acid positions. Three serotypes, HRV-3, -14 and -72, share at least 84% identity with one another but are less than 66% identical to the majority group. Interestingly, membership of these two molecular clusters correlates with the groupings determined by sensitivity to antivirus drugs, suggesting that they reflect a fundamental division of HRVs. In contrast, there is no correlation with receptor grouping, since the majority group contains members belonging to both HRV receptor groups.

[1]  J. Fox Is a rhinovirus vaccine possible? , 1976, American journal of epidemiology.

[2]  J. Fox,et al.  Antigenic groupings of 90 rhinovirus serotypes , 1982, Infection and immunity.

[3]  R. Mountford,et al.  The complete nucleotide sequence of a common cold virus: human rhinovirus 14. , 1984, Nucleic acids research.

[4]  R. Colonno,et al.  Many rhinovirus serotypes share the same cellular receptor , 1984, Journal of virology.

[5]  Rodger Staden,et al.  Measurements of the effects that coding for a protein has on a DNA sequence and their use for finding genes , 1984, Nucleic Acids Res..

[6]  R. Mountford,et al.  The complete nucleotide sequence of a common cold virus: human rhinovlrus 14 , 1984 .

[7]  R Staden Computer methods to locate signals in nucleic acid sequences , 1984, Nucleic Acids Res..

[8]  John E. Johnson,et al.  Structure of a human common cold virus and functional relationship to other picornaviruses , 1985, Nature.

[9]  F. Fraundorfer,et al.  Human rhinovirus 2: complete nucleotide sequence and proteolytic processing signals in the capsid protein region. , 1985, Nucleic acids research.

[10]  B. Sherry,et al.  Use of monoclonal antibodies to identify four neutralization immunogens on a common cold picornavirus, human rhinovirus 14 , 1986, Journal of virology.

[11]  G Vriend,et al.  The site of attachment in human rhinovirus 14 for antiviral agents that inhibit uncoating. , 1986, Science.

[12]  W. Sommergruber,et al.  Evolutionary relationships within the human rhinovirus genus: comparison of serotypes 89, 2, and 14. , 1987, Proceedings of the National Academy of Sciences of the United States of America.

[13]  G. Werner,et al.  Different rhinovirus serotypes neutralized by antipeptide antibodies , 1987, Nature.

[14]  B. Clarke,et al.  A synthetic peptide which elicits neutralizing antibody against human rhinovirus type 2. , 1987, The Journal of general virology.

[15]  M. Murcko,et al.  Evidence for the direct involvement of the rhinovirus canyon in receptor binding. , 1988, Proceedings of the National Academy of Sciences of the United States of America.

[16]  P. Minor,et al.  The nucleotide sequence of human rhinovirus 1B: molecular relationships within the rhinovirus genus. , 1988, The Journal of general virology.

[17]  G. Stanway,et al.  Polymerase chain reaction amplification of rhinovirus nucleic acids from clinical material. , 1988, Nucleic acids research.

[18]  M. Rossmann,et al.  Conservation of the putative receptor attachment site in picornaviruses. , 1988, Virology.

[19]  D. Staunton,et al.  A cell adhesion molecule, ICAM-1, is the major surface receptor for rhinoviruses , 1989, Cell.

[20]  G. Hagen Molecular approaches to understanding auxin action. , 1989, The New biologist.

[21]  A. Mcclelland,et al.  The major human rhinovirus receptor is ICAM-1 , 1989, Cell.

[22]  M S Chapman,et al.  Crystal structure of human rhinovirus serotype 1A (HRV1A). , 1989, Journal of molecular biology.

[23]  G. Stanway,et al.  Amplification of rhinovirus specific nucleic acids from clinical samples using the polymerase chain reaction , 1989, Journal of medical virology.

[24]  J. Tomassini,et al.  cDNA cloning reveals that the major group rhinovirus receptor on HeLa cells is intercellular adhesion molecule 1. , 1989, Proceedings of the National Academy of Sciences of the United States of America.

[25]  D. Filman,et al.  Structural factors that control conformational transitions and serotype specificity in type 3 poliovirus. , 1989, The EMBO journal.

[26]  A. Treasurywala,et al.  Conformational change in the floor of the human rhinovirus canyon blocks adsorption to HeLa cell receptors , 1989, Journal of virology.

[27]  G. Stanway Structure, function and evolution of picornaviruses. , 1990, The Journal of general virology.

[28]  P. Lewi,et al.  Two groups of rhinoviruses revealed by a panel of antiviral compounds present sequence divergence and differential pathogenicity , 1990, Journal of virology.

[29]  Horsnell Pr Molecular approaches to understanding biological diversity in rhino- and enteroviruses. , 1990 .

[30]  R. Colonno,et al.  The major and minor group receptor families contain all but one human rhinovirus serotype. , 1991, Virology.

[31]  M G Rossmann,et al.  Structure of a human rhinovirus complexed with its receptor molecule. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[32]  M S Chapman,et al.  A comparison of the anti-rhinoviral drug binding pocket in HRV14 and HRV1A. , 1994, Journal of molecular biology.

[33]  R. Rueckert,et al.  The structure of human rhinovirus 16. , 1993, Structure.

[34]  E. Kuechler,et al.  Rhinoviral receptor discrimination: mutational changes in the canyon regions of human rhinovirus types 2 and 14 indicate a different site of interaction. , 1993, The Journal of general virology.

[35]  E. Kuechler,et al.  Members of the low density lipoprotein receptor family mediate cell entry of a minor-group common cold virus. , 1994, Proceedings of the National Academy of Sciences of the United States of America.