Differential synthesis of proteins by T4 phage and its head protein amber mutant

There was no difference in the incorporation of S-35 label into proteins of T4 and amber B17 phage grown on Escherichia coli B. The head protein peak was absent in the polyacrylamide gel electrophoretic profile of the S-35 labeled proteins of amber B17 grown on non-permissive host, E.coli B. However, an increase of 15–70% in the synthesis of other phage proteins of amber B17 over that of T4 phage was observed. The lysozyme activity increased by two fold in amber B17 in comparison with that of T4 phage grown on E.coli B. These results imply that in the absence of head protein synthesis by amber mutant there was an increase in the synthesis of other phage proteins

Identification and Functional Analysis of Three Isoforms of Bovine BST-2

Human BST-2 (hBST-2) has been identified as a cellular antiviral factor that blocks the release of various enveloped viruses. Orthologues of BST-2 have been identified in several species, including human, monkeys, pig, mouse, cat and sheep. All have been reported to possess antiviral activity. Duplication of the BST-2 gene has been observed in sheep and the paralogues are referred to as ovine BST-2A and BST2-B, although only a single gene corresponding to BST-2 has been identified in most species. In this study, we identified three isoforms of bovine BST-2, named bBST-2A1, bBST-2A2 and bBST-2B, in bovine cells treated with type I interferon, but not in untreated cells. Both bBST-2A1 and bBST-2A2 are posttranslationally modified by N-linked glycosylation and a GPI-anchor as well as hBST-2, while bBST-2B has neither of these modifications. Exogenous expression of bBST-2A1 or bBST-2A2 markedly reduced the production of bovine leukemia virus and vesicular stomatitis virus from cells, while the antiviral activity of bBST-2B was much weaker than those of bBST-2A1 and bBST-2A2. Our data suggest that bBST-2A1 and bBST-2A2 function as part of IFN-induced innate immunity against virus infection. On the other hand, bBST-2B may have a different physiological function from bBST-2A1 and bBST-2A2