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O Tarlow

Publications and source records attributed to O Tarlow.

9 recordsLinked to original sources
PubMed1994

Molecular biology of rotaviruses. IX. Conservation and divergence in genome segment 5.

Nucleotide sequencing of RNA segment 5 from seven strains of group A rotavirus has been carried out to investigate the extent of diversity and conservation, as well as possible selective pressures involved in driving the fixation of sequence changes in this gene. Analyses of the derived sequences revealed that sequence conservation could not be correlated either with rotavirus serotype or the species of origin of the virus strain. These sequences together with other published and unpublished sequences of this gene have raised the total number available for comparison to 17. Alignment of all the available sequences revealed that only 88 amino acid positions (17.6%) in the protein encoded by gene 5 (VP5) are absolutely conserved but that the metal-binding motif reported by others is conserved in all sequences. Despite the high degree of sequence divergence, alignment of secondary structure predictions for VP5 showed a high level of conservation, suggesting that constraints on sequence divergence may operate at the level of overall higher-order structure of the encoded protein.

Amino Acid Sequence↗
PubMed1993

Genomic concatemerization/deletion in rotaviruses: a new mechanism for generating rapid genetic change of potential epidemiological importance.

Three variants of group A rotavirus with large changes in their gene 5 structures have been analyzed at the molecular level. The first of these, P9 delta 5, was obtained during plaque purification undertaken as part of the biological cloning of a field isolate of virus. The gene 5 homolog in this isolate migrated just ahead of the normal segment 6 RNA, giving an estimated size of 1,300 bp. Molecular cloning and sequencing of this homolog revealed it to have a single 308-bp deletion in the center of the normal gene 5 sequence extending between nucleotides 460 and 768 of the normal gene sequence. This deletion caused a frameshift in the gene such that a stop codon was encountered 8 amino acids downstream of the deletion point, giving a predicted size for the protein product of this gene of 150 amino acids compared with the 490 amino acids of its normal-size counterpart. Attempts to detect this shortened protein in virus-infected cells were not successful, indicating that it was much less stable than the full-length protein and/or had suffered a large change in its antigenicity. The second two variants, brvA and brvE, were generated in an earlier study following the high-multiplicity passage of the UKtc strain of bovine rotavirus. Polyacrylamide gel electrophoresis analysis of these nondefective variants showed that brvA had a gene 5 homolog approximately equal in size to the normal RNA segment 2 (approximately 2,700 bp) and that brvE had a size of approximately 2,300 bp. Both variants showed changes in their gene 5 protein products, with brvA mimicking P9 delta 5 in failing to produce a detectable product whereas brvE produced a new virus-specific protein approximately 80 kDa in size. Full-length cDNA clones of the brvE gene 5 homolog were isolated, and analysis of their structure revealed a head-to-tail concatemerization of the normal gene 5 sequence with the first copy of the concatemer covering nucleotides 1 to 808 and the second covering nucleotides 92 to 1579, giving a total length of 2,296 bp. Sequencing across the junction region of the two copies of the gene showed that they were joined in frame to give a predicted combined open reading frame of 728 amino acids with the amino-terminal region consisting of amino acids 1 to 258 fused at the carboxy terminus to amino acids 21 to 490.(ABSTRACT TRUNCATED AT 400 WORDS)

Amino Acid Sequence↗
PubMed1989

Detailed structural analysis of a genome rearrangement in bovine rotavirus.

A genome rearrangement involving RNA segment 11 of a bovine rotavirus has been analysed by molecular cloning and sequencing. This revealed that the rearranged genome segment was generated by a head to tail concatemerisation of two almost full length copies of segment 11. The upstream copy of the gene has lost its 3' end and the downstream copy its 5' end. The truncation of the upstream copy of the gene occurs within the termination codon for VP11 converting it from a UAG to a UGA, the rearranged gene is therefore still able to encode a normal VP11. The possible mechanisms by which this rearrangement may have been generated are discussed.

Amino Acid Sequence↗
PubMed1988

Molecular cloning and sequencing of the gene (M2) encoding the major virion structural protein (mu 1-mu 1C) of serotypes 1 and 3 of mammalian reovirus.

Full-length c-DNA copies of the M2 gene from the Lang strain of type 1 and the Dearing strain of type 3 reovirus have been cloned in the Escherichia coli plasmid pAT153. DNA sequencing of these clones showed that the type 3 gene was 2207 nucleotides long and the single long open reading frame encoded a primary translation product (mu 1) of 709 amino acids with a molecular weight of 76,000. The type 1 gene was three nucleotides shorter at 2204 with the deletions occurring near the center of the coding sequence so that the primary translation product of this gene was one amino acid shorter at 708. Sequence homology between the two genes had an overall value of 85%, rising to 95% when only the noncoding sequences were compared. The 334 nucleotide changes between the two genes were distributed throughout the sequence with no apparent areas of concentration. Comparison of the predicted amino acid sequences showed that there were 24 differences between the two giving a homology of 96.6% at the protein level. The amino acid changes of which only 9 were nonconservative were again spread fairly evenly throughout the coding sequence although there was one small patch of 5 changes in a stretch of 10 amino acids near the carboxyl terminus. The post-translational cleavage to convert mu 1 to the major virion protein mu 1C is revealed as involving the removal of 42 amino acids exclusively from the amino terminus of mu 1. Simple addition of trypsin-sensitive cleavage sites or predicted secondary structure failed to show the cause of the large difference known to exist in the protease sensitivities of virions carrying these two proteins.

Amino Acid Sequence↗