Biological functions of the bacteriophage T3 SAMase gene

Krueger, D H; Presber, W; Hansen, Sigrid; Rosenthal, H. A.

doi:10.1128/jvi.16.2.453-455.1975

Cited by 38 publications

(15 citation statements)

References 14 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…To further evaluate the requirement of SAM as a cofactor of viperin, we reduced the intracellular SAM levels by means of a SAM-cleaving enzyme, SAMase (also called S-adenosyl-L-methionine hydrolase or AdoMetase). The cDNA sequence of the Escherichia coli bacteriophage T3 (Hausmann, 1967;Krueger et al, 1975; C. Immunoblot analysis of cells transfected with FLAG-ΔMx, FLAG-viperin and SAMase using antisera specific for the FLAG epitope (staining FLAG-tagged ΔMx and viperin), or actin. Hughes et al, 1987) was chemically synthesized and cloned into the eukaryotic expression vector pI.18 (see Experimental procedures).…”

Section: Antiviral Action Of Viperin Is Based On the Radical Sam Domamentioning

confidence: 99%

Viperin is an iron-sulfur protein that inhibits genome synthesis of tick-borne encephalitis virus via radical SAM domain activity

et al. 2013

View full text Add to dashboard Cite

SummaryViperin is an interferon-induced protein with a broad antiviral activity. This evolutionary conserved protein contains a radical S-adenosyl-Lmethionine (SAM) domain which has been shown in vitro to hold a [4Fe-4S] cluster. We identified tick-borne encephalitis virus (TBEV) as a novel target for which human viperin inhibits production of the viral genome RNA. Wt viperin was found to require ER localization for full antiviral activity and to interact with the cytosolic Fe/S protein assembly factor CIAO1. Radiolabelling in vivo revealed incorporation of

show abstract

Section: Antiviral Action Of Viperin Is Based On the Radical Sam Domamentioning

confidence: 99%

Viperin is an iron-sulfur protein that inhibits genome synthesis of tick-borne encephalitis virus via radical SAM domain activity

et al. 2013

View full text Add to dashboard Cite

show abstract

“…It is possible that bacteriophage T7 and the T3 SAMmutants only partially inhibit, or alter the specificity of, the methylation enzymes of the host cell. Krueger et al (13) have found that in poorly growing cells, T3 SAMand T7 both give rapid, productive responses, whereas T3 SAM' phage particles are only slowly expressed. In mixed infections of T3 SAMand T3 SAM' or T7 and T3 SAM', the virus types having no SAMase activity (and, presumably, methylated DNA) are dominant, yielding rapid lysis and a high burst size.…”

mentioning

confidence: 99%

Superinfection exclusion by bacteriophage T7

McAllister¹,

Barrett²

1977

J Virol

View full text Add to dashboard Cite

show abstract

“…SAMase (GOLD et al. 1964, HAUSMA" 1967, KRUGER et al 1975, 1977c, STUDIER and MOWA 1976. Previously "non-classical" modification and restriction of phages has within 3 months and is down to although these strains differ significantly in their ability to modify T3.…”

Section: Resultsmentioning

confidence: 99%

Virus adaptation to host cells: The non‐classical modification of phage T3

Krüger¹,

Hansen²,

Schroeder³

1980

J of Basic Microbiology

View full text Add to dashboard Cite

Bacterial virus T3 undergoes host-controlled modification which is not based on "classical" processes of DNA modification and restriction. The adsorption and thus the growth of T3 on Escherichia coli W cells (E. coli K12 derivative) decisively depends on the host strain on which the virus was previously propagated. Depending on the modification conferred to the virus by its last host, its efficiency of plating (e.0.p.) on E. coli W varies by six orders of magnitude between lo-' and lo-'. This does not reflect the appearance of T3 host-range mutants, but a fully reversible modification of genotypically unchanged T3 wild-type phage.The behaviour of T3 in the described host system constitutes a second case of so-called nonclassical modification and restriction ( KRUGER et al. 1977, Molec. gen. Genet. 153, 107-110) of bacteriophages. Non-classical modification (protein modification) is additive to and independent of DNA modification and restriction as demonstrated with the ocr-phage T3/R7. -Furthermore, our results suggest that the adsorption specificity of T3 is determined by a t least two independent genetic factors; in both of these factors T3 differs from T7.When bacteriophage T7 is passaged between different E. coli B strains all possessing the EcoB DNA specificity it is subject to a clear phenotypical modification and restriction (KRUGER et al. 1976). This phenomenon was termed "non-classical" modification and restriction by us, since it is not based on the "classical" mechanism of modification and restriction of phage DNA but on reversible changes in the phage's adsorption behaviour, depending on coat protein modification by the last host cell (KRUGER et al. 1977a Table 6). We report here that, in contrast to the stable host-range behaviour of T7 and the T3hw mutant, adsorption and thus the plating efficiency (e.0.p.) of T3 wild type on E. coli W depend on the host on which the phage was last grown. The e.0.p. varies from lo-' to 10-1 while being fully reversible, excluding the selection of host-range mutants. A preliminary report of these results was published elsewhere (KRUGER et al. 1980). il.lccterittb und methodsCell and virus strains: The bacteria strains are presented in Table 1. Phages T3 and T7 are from the collection of our institute. The host-range mutant T3hw is described by KRUGER et al. (1979).

show abstract

Biological functions of the bacteriophage T3 SAMase gene

Cited by 38 publications

References 14 publications

Viperin is an iron-sulfur protein that inhibits genome synthesis of tick-borne encephalitis virus via radical SAM domain activity

Viperin is an iron-sulfur protein that inhibits genome synthesis of tick-borne encephalitis virus via radical SAM domain activity

Superinfection exclusion by bacteriophage T7

Virus adaptation to host cells: The non‐classical modification of phage T3

Contact Info

Product

Resources

About