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Emergence of influenza A virus variants after prolonged shedding from pheasants.
Humberd J, Boyd K, Webster RG
(2007) J Virol 81: 4044-51
MeSH Terms: Amino Acid Sequence, Amino Acid Substitution, Animals, Antibodies, Viral, Antigens, Viral, Birds, Bursa of Fabricius, Cecum, Chick Embryo, Ferrets, Genetic Drift, Genetic Variation, Hemagglutinin Glycoproteins, Influenza Virus, Histocytochemistry, Influenza A virus, Influenza in Birds, Intestine, Large, Male, Molecular Sequence Data, Mutation, Missense, Neuraminidase, Trachea, Viral Proteins, Virus Replication, Virus Shedding
Show Abstract · Added March 5, 2014
We previously demonstrated the susceptibility of pheasants to infection with influenza A viruses of 15 hemagglutinin (HA) subtypes: 13/23 viruses tested were isolated for >or=14 days, all in the presence of serum-neutralizing antibodies; one virus (H10) was shed for 45 days postinfection. Here we confirmed that 20% of pheasants shed low-pathogenic influenza viruses for prolonged periods. We aimed to determine why the antibody response did not clear the virus in the usual 3 to 10 days, because pheasants serve as a long-term source of influenza viruses in poultry markets. We found evidence of virus replication and histological changes in the large intestine, bursa of Fabricius, and cecal tonsil. The virus isolated 41 days postinfection was antigenically distinct from the parental H10 virus, with corresponding changes in the HA and neuraminidase. Ten amino acid differences were found between the parental H10 and the pheasant H10 virus; four were in potential antigenic sites of the HA molecule. Prolonged shedding of virus by pheasants results from a complex interplay between the diversity of virus variants and the host response. It is often argued that vaccination pressure is a mechanism that contributes to the generation of antigenic-drift variants in poultry. This study provided evidence that drift variants can occur naturally in pheasants after prolonged shedding of virus, thus strengthening our argument for the removal of pheasants from live-bird retail markets.
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25 MeSH Terms
Identification of downstream-initiated c-Myc proteins which are dominant-negative inhibitors of transactivation by full-length c-Myc proteins.
Spotts GD, Patel SV, Xiao Q, Hann SR
(1997) Mol Cell Biol 17: 1459-68
MeSH Terms: Animals, Bursa of Fabricius, Cell Division, Cell Nucleus, Chickens, Codon, Initiator, Humans, Lymphoma, Mice, Molecular Weight, Peptide Chain Initiation, Translational, Phosphorylation, Proto-Oncogene Proteins c-myc, Recombinant Fusion Proteins, Species Specificity, Transcriptional Activation, Tumor Cells, Cultured
Show Abstract · Added March 5, 2014
The c-myc gene has been implicated in multiple cellular processes including proliferation, differentiation, and apoptosis. In addition to the full-length c-Myc 1 and 2 proteins, we have found that human, murine, and avian cells express smaller c-Myc proteins arising from translational initiation at conserved downstream AUG codons. These c-Myc short (c-Myc S) proteins lack most of the N-terminal transactivation domain but retain the C-terminal protein dimerization and DNA binding domains. As with full-length c-Myc proteins, the c-Myc S proteins appear to be localized to the nucleus, are relatively unstable, and are phosphorylated. Significant levels of c-Myc S, often approaching the levels of full-length c-Myc, are transiently observed during the rapid growth phase of several different types of cells. Optimization of the upstream initiation codons resulted in greatly reduced synthesis of the c-Myc S proteins, suggesting that a "leaky scanning" mechanism leads to the translation of these proteins. In some hematopoietic tumor cell lines having altered c-myc genes, the c-Myc S proteins are constitutively expressed at levels equivalent to that of full-length c-Myc. As predicted, the c-Myc S proteins are unable to activate transcription and inhibited transactivation by full-length c-Myc proteins, suggesting a dominant-negative inhibitory function. While these transcriptional inhibitors would not be expected to function as full-length c-Myc, the occurrence of tumors which express constitutive high levels of c-Myc S and their transient synthesis during rapid cell growth suggest that these proteins do not interfere with the growth-promoting functions of full-length c-Myc.
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17 MeSH Terms