Since the outbreak in humans of an H5N1 avian influenza virus in Hong Kong in 1997, poultry entering the live-bird markets of Hong Kong have been closely monitored for infection with avian influenza. In March 1999, this monitoring system detected geese that were serologically positive for H5N1 avian influenza virus, but the birds were marketed before they could be sampled for virus. However, viral isolates were obtained by swabbing the cages that housed the geese.

Avian influenza virus (AIV) A/turkey/Oregon/71-SEPRL (TK/OR/71-SEPRL) (H7N3) encodes a full-length NS1 protein and is a weak inducer of interferon (IFN).

No abstract

Mutations were introduced into mouse adenovirus type 1 (MAV-1) early region 3 (E3) initiator codons by homologous recombination between viral DNA and a plasmid containing a mutagenized E3 region. The resulting mutant virus, pmE312, contained ATG --> TTA mutations at codon positions 1 and 4 and was expected to be null for the expression of the E3 proteins. However, gp11K, an MAV-1 E3 glycoprotein of 14K molecular weight, was detected in mutant-infected cell lysates at levels about 10-12% of that of wild-type (wt) virus at late times in infection. The gp11K polypeptide produced by pmE312 at late times was immunoprecipitated with two E3-specific antisera prepared against different regions of the protein. Like gp11K produced by wt virus infections, it was sensitive to endoglycosidase H (endo H) and thus resident in the endoplasmic reticulum (ER). In pmE312-infected cells treated with cytosine arabinoside (araC), an inhibitor of DNA replication, the gp11K protein was not detected by immunoprecipitation. This indicates that gp11K expression in pmE312-infected cells at late times was dependent on DNA replication and that it was thus translated from a late transcript. In vitro translation of poly(A)+ RNA from mock-, wild-type-, and pmE312-infected cells showed that gp11K was translated from late mRNA as an approximately 28K fusion between a late protein and gp11K. Our data are consistent with a model in which gp11K is expressed at late times as a late protein-gp11K chimera in both wt- and mutant-infected cells. This chimera is then processed: removal of a large N-terminal sequence results in the observed 14K ER-localized gp11K.