Assembly of Type C Oncornaviruses: A Model

Bolognesi, D. P.; Montelaro, R. C.; Hensel, Frank; Schäfer, Werner

doi:10.1126/science.202022

Cited by 200 publications

(90 citation statements)

References 47 publications

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“…wt. 80000 to 90000) with the cleavage yielding pl5E and gp70 (Bolognesi et al, 1978;Snyderman & Cianciolo, 1984). Mathes et al (1979) have reported suppression of blastogenesis of feline lymphocytes in vitro to Con A using pl5E.…”

Section: Introductionmentioning

confidence: 99%

Suppression of in vitro Neutrophil Function by Feline Leukaemia Virus (FeLV) and Purified FeLV-p15E

Lafrado¹,

Lewis²,

Mathes

et al. 1987

Journal of General Virology

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Section: Introductionmentioning

confidence: 99%

Suppression of in vitro Neutrophil Function by Feline Leukaemia Virus (FeLV) and Purified FeLV-p15E

Lafrado¹,

Lewis²,

Mathes

et al. 1987

Journal of General Virology

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“…In addition, the positively charged side chain of Arg14 is ideally positioned for electrostatic interactions with the phosphodiester backbone of the nucleic acid. The structural findings provide a rationalization for the general conservation of these hydrophobic and basic residues in CCHC zinc fingers, and are consistent with site-directed mutagenesis results that implicate these residues as direct participants in viral genome recognition.Keywords: human immunodeficiency virus; NMR; nucleocapsid protein; viral genome recognition; zinc finger All retroviruses, including human immunodeficiency virus (HIV), encode a gag precursor polyprotein that functions in the recognition of viral RNA and in the assembly of virus particles (Bolognesi et al, 1978;Dickson et al, 1985). Subsequent to assembly and budding, the gag poly (Berg, 1986) that the arrays function by coordinating zinc (Green & Berg, 1989Roberts et al, 1989;South et al, 1989South et al, , 1990a South et al, ,b, 1991Summers et al, 1990Summers et al, , 1992Fitzgerald & Coleman, 1991;Omichinski et al, 1991).…”

mentioning

confidence: 99%

Zinc‐ and sequence‐dependent binding to nucleic acids by the N‐terminal zinc finger of the HIV‐1 nucleocapsid protein: NMR structure of the complex with the Psi‐site analog, dACGCC

1993

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The nucleic acid interactive properties of a synthetic peptide with sequence of the N-terminal CCHC zinc finger (CCHC = Cys-X,-Cys-X4-His-X,-Cys; X = variable amino acid) of the human immunodeficiency virus (HIV) nucleocapsid protein, Zn(HIV1-Fl), have been studied by 'H NMR spectroscopy. Titration of Zn(HIV1-Fl) with oligodeoxyribonucleic acids containing different nucleotide sequences reveals, for the first time, sequencedependent binding that requires the presence of at least one guanosine residue for tight complex formation. The dynamics of complex formation are sensitive to the nature of the residues adjacent to guanosine, with residues on the 3' side of guanosine having the largest influence. An oligodeoxyribonucleotide with sequence corresponding to a portion of the HIV-1 psi-packaging signal, d(ACGCC), forms a relatively tight complex with Zn(HIV1-F1) (Kd = 5 x M). Two-dimensional nuclear Overhauser effect (NOESY) data indicate that the bound nucleic acid exists predominantly in a single-stranded, A-helical conformation, and the presence of more than a dozen intermolecular NOE cross peaks enabled three-dimensional modeling of the complex. The nucleic acid binds within a hydrophobic cleft on the peptide surface. This hydrophobic cleft is defined by the side chains of residues Val', Phe4, He1,, and AlaI3. Backbone amide protons of Phe4 and AlaI3 and the backbone carbonyl oxygen of Lys' that lie within this cleft appear to form hydrogen bonds with the guanosine 0 6 and NlH atoms, respectively. In addition, the positively charged side chain of Arg14 is ideally positioned for electrostatic interactions with the phosphodiester backbone of the nucleic acid. The structural findings provide a rationalization for the general conservation of these hydrophobic and basic residues in CCHC zinc fingers, and are consistent with site-directed mutagenesis results that implicate these residues as direct participants in viral genome recognition.Keywords: human immunodeficiency virus; NMR; nucleocapsid protein; viral genome recognition; zinc finger All retroviruses, including human immunodeficiency virus (HIV), encode a gag precursor polyprotein that functions in the recognition of viral RNA and in the assembly of virus particles (Bolognesi et al., 1978;Dickson et al., 1985). Subsequent to assembly and budding, the gag poly (Berg, 1986) that the arrays function by coordinating zinc (Green & Berg, 1989Roberts et al., 1989;South et al., 1989South et al., , 1990a South et al., ,b, 1991Summers et al., 1990Summers et al., , 1992Fitzgerald & Coleman, 1991;Omichinski et al., 1991). In particular, recent zinc-edge extended X-ray absorption fine structure (EXAFS) measurements on intact retroviruses reveal that tightly associated viral zinc, which is present in quantities sufficient to populate the arrays , is coordinated t o the CCHC zinc fingers of the NC proteins in mature virions Summers et al., 1992). The three-dimensional structures of the HIVl-NC protein and its constituent zinc finger domains have been determined to...

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“…6). It is not known whether the variations in the envelope proteins are due to glycosylation or to structural differences (25).…”

Section: Discussionmentioning

confidence: 99%

Variations in properties of virus released from morphologically different cell lines transformed in vitro by Friend leukemia virus.

Tsuei¹,

Pogo²,

Friend³

1980

Proc. Natl. Acad. Sci. U.S.A.

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The properties of the virus synthesized by each of three morphologically different cell lines originating from DBA/2J fetal liver cells transformed by the anemic strain of Friend leukemia virus in vitro were analyzed. The cells of line C-1 are malignant in syngeneic DBA/2 mice, grow in suspension, and are erythroid in origin. Cells of lines G-2 and G-3 are adherent, are epithelial in appearance, and produce no tumors in DBA/2J mice. Higher reverse transcriptase activity was detected in the culture fluid of lines G-2 and G-3, although virus from G-1 cells was more leukemogenic. Differences were also found in the virion density and size of the viral genome. RNA from the virions produced by G-2 and G-3 cells sedimented at 75 S in a sucrose gradient; virion RNA from C-1 cells sedimented at 60 S. However, when subjected to polyacrylamide gel electrophoresis, all three virus strains showed identical RNA subunits with an estimated molecular weight of 2.6 X 106. Analysis of virion proteins by slab gel electrophoresis showed differences in envelope protein (gp7l) components but not in the major core protein (p30). The properties of these viruses are stable and remain unchanged after passage in 3T3 cells.The anemic strain of Friend leukemia virus (FLV-A) is a competent virus with the ability to induce erythroleukemia in the absence of spleen focus-forming virus (SFFV) (1). The primary target cell for FLV is most likely an erythroid precursor (2). That infection may also affect other cell types (3) was supported by the finding that permanent lines of morphologically. different cells originated from cultures of fetal liver transformed by FLV-A in vitro. Three of these lines have been characterized (4). The cells of line G-I are immature hematological cells and resemble the erythroleukemia lines established from the spleens of FLV-infected mice (5). They grow in suspension and can be induced to differentiate along the erythroid pathway. The cells of lines G-2 and G-3 are adherent and epithelial. All three lines are chronically infected with virus.In view of the findings that greater levels of virus were produced by the adherent lines and that this virus was less leukemogenic than that produced by the suspension lines, it was important to compare the molecular properties of the virus of each of the three transformed cell lines. The virus produced by the adherent lines was found to differ from that of the suspension line in the virion particle density, sedimentation coefficient of high molecular weight (HMW) RNA, and viral envelope protein components. However, all of the virus strains have identical RNA subunits.MATERIALS AND METHODS Cells and Viruses. Establishment, growth conditions, and characterization of the FLV-A-transformed lines of G-1, G-2, and G-3 (4) as well as of the prototype Friend erythroleukemia cell line 745A (5) and its subclone 5-86 (6, Virus Replication. Virus released into the culture fluid was assayed for syncytia formation on XC cells (9). Generally, leukemogenicity was assayed in 6-to 8-week-...

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Assembly of Type C Oncornaviruses: A Model

Cited by 200 publications

References 47 publications

Suppression of in vitro Neutrophil Function by Feline Leukaemia Virus (FeLV) and Purified FeLV-p15E

Suppression of in vitro Neutrophil Function by Feline Leukaemia Virus (FeLV) and Purified FeLV-p15E

Zinc‐ and sequence‐dependent binding to nucleic acids by the N‐terminal zinc finger of the HIV‐1 nucleocapsid protein: NMR structure of the complex with the Psi‐site analog, dACGCC

Variations in properties of virus released from morphologically different cell lines transformed in vitro by Friend leukemia virus.

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