The nucleotide sequence of a cloned human leukocyte Interferon cDNA

Mantei, Ned; Schwarzstein, Marco; Streuli, Michel; Panem, Sandra; Nagata, Shinji; Weissmann, Charles

doi:10.1016/0378-1119(80)90137-7

Cited by 157 publications

(44 citation statements)

References 22 publications

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“…[9][10][11][12][13] PCR primers for Fas were based on the published DNA sequences for the primers. 14) PCR primers for IL-1b, IL-6, TNF-a and glycerol-3-phosphate dehydrogenase (G3PDH) were purchased from CLON-TECH Labs.…”

Section: Methodsmentioning

confidence: 99%

Differential mRNA Expression of Inflammatory Cytokines in Cultured Human Fetal Membrane Cells Responding to Influenza Virus Infection.

Uchide

Ohyama

Yuan

et al. 2002

Biological & Pharmaceutical Bulletin

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When a virus encounters a susceptible cell, the virus enters and initiates cytocidal, persistent, latent or abortive infection. We recently reported that influenza virus (IV) induces persistent infection accompanied by cell survival and virus production in cultured amnion cells. In addition, cytocidal infection accompanied by apoptotic cell death and virus production occurred in cultured chorion cells. Both cell cultures were prepared from human fetal membranes. 1)IV induces cytocidal infection in a variety of cultures, such as HeLa and Madin-Darby canine kidney (MDCK) cell lines and human peripheral blood monocytes in vitro, all of which die through the mechanism of apoptosis.2-5) Furthermore, IV infection induces gene expression of inflammatory cytokines such as interleukin (IL)-1, IL-6, tumor necrosis factor (TNF)-a and interferon (IFN)-a/b, and C-C and C-X-C chemokines such as monocyte chemoattractant protein (MCP)-1, macrophage inflammatory protein (MIP)-1a, RANTES (regulated on activation, normal T cell expressed and secreted) and IFN-inducible protein (IP)-10, 6,7) and proapoptotic factors such as Fas and Fas ligand,8) which occur in infected host cells undergoing apoptosis. Apoptosis and inducible gene expression of inflammatory mediators therefore seem to be correlated. However, whether IV induces gene expression of inflammatory mediators during persistent infection remains unknown.We therefore extensively examined expression of mRNAs for inflammatory cytokines such as IL-1b, IL-6, TNF-a, IFN-a, IFN-b, IFN-g, macrophage colony-stimulating factor (M-CSF) and granulocyte macrophage colony-stimulating factor (GM-CSF), and Fas during cytocidal and persistent infections by reverse transcriptase-polymerase chain reaction (RT-PCR) analysis. Of note is the fact that IV infection induced the gene expression of a set of inflammatory cytokines during cytocidal infection accompanied by apoptotic cell death, but this induction was not present during persistent infection in the absence of apoptosis. In this paper we report a noticeable difference in gene expression of a set of inflammatory cytokines between cytocidal and persistent infections. MATERIALS AND METHODSMaterials PCR primers for IFN-a, IFN-b, IFN-g, M-CSF and GM-CSF were originally designed according to published cDNA sequences. 9-13) PCR primers for Fas were based on the published DNA sequences for the primers. 14)PCR primers for IL-1b, IL-6, TNF-a and glycerol-3-phosphate dehydrogenase (G3PDH) were purchased from CLON-TECH Labs. Inc. (CA, U.S.A.). DNA sequences for the PCR primers are shown in Table 1. Neutralizing antibodies against Fas (Medical & Biological Labs. Co., Ltd., Nagoya, Japan), IFN-b (Yamasa Shoyu Co., Ltd., Tokyo, Japan), TNF-a and IFN-g (Genzyme Diagnostic, MA, U.S.A.) were purchased from the listed suppliers.Cell Culture and Virus Infection Primary cultured chorion and amnion cells were prepared from human fetal membranes obtained by cesarean section during the month of normal parturition as described.15) HeLa cell line was obtained from...

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Section: Methodsmentioning

confidence: 99%

Differential mRNA Expression of Inflammatory Cytokines in Cultured Human Fetal Membrane Cells Responding to Influenza Virus Infection.

Uchide

Ohyama

Yuan

et al. 2002

Biological & Pharmaceutical Bulletin

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“…We report here the partial amino acid sequence ofmajor species ofhuman leukocyte interferon. These proteins, which represent a significant fraction of the active interferon produced by these cells, lack the 10 COOH-terminal amino acids suggested previously (11)(12)(13)(14) from the DNA sequences. Each of the three species is active although lacking the 10 COOH-terminal amino acids.…”

mentioning

confidence: 67%

“…Recombinant bacterial plasmids containing interferon cDNAs have been analyzed and reveal different restriction maps and DNA sequences (10)(11)(12)(13)(14). Extensive nucleic acid sequence determination of interferon cDNAs from a virus-induced myeloblast cell line indicates that at least eight distinct species of leukocyte interferon are transcribed during the induction process (14), and this result is corroborated by restriction endonuclease mapping ofinterferon sequences in a human gene bank (15)(16)(17).…”

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confidence: 92%

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Amino acid sequence of a human leukocyte interferon.

Levy¹,

Rubinstein²,

Shively³

et al. 1981

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

102

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The primary structures of three major species of human leukocyte. interferon differ from the structure predicted from the DNA sequence of recombinants containing leukocyte interferon-coding regions. Compared to the recombinant interferon produced in bacteria, three of the purified natural proteins isolated from leukocytes lack the 10 COOH-terminal amino acids suggested by the DNA sequence.Although interferon was discovered 23 years ago (1), the structure of the genes and proteins are only now being elucidated with the aid of recombinant DNA technology, DNA sequence analysis, and advances in protein purification and sequence determination. These results indicate that human leukocyte interferon consists of a family of proteins with similar primary structures.Sensitive methods for protein sequence analysis at the nanomole level (2-5) have revealed NH2-terminal amino acid sequences for lymphoblastoid (6) and leukocyte (7) interferon that differ in 2 out of 20 positions. Powerful protein purification techniques involving high-performance liquid chromatography (HPLC) have been used to resolve at least 10 different species of human leukocyte interferon, and tryptic maps of this family of proteins exhibit remarkable homology (8). Amino acid sequence analysis of tryptic and chymotryptic peptides from human lymphoblastoid interferon suggests the existence ofat least five species (9).The successful cloning of human leukocyte interferon has provided additional evidence in support of this diversity. Recombinant bacterial plasmids containing interferon cDNAs have been analyzed and reveal different restriction maps and DNA sequences (10-14). Extensive nucleic acid sequence determination of interferon cDNAs from a virus-induced myeloblast cell line indicates that at least eight distinct species of leukocyte interferon are transcribed during the induction process (14), and this result is corroborated by restriction endonuclease mapping ofinterferon sequences in a human gene bank (15)(16)(17). All of these reports suggest that every active species of human leukocyte interferon is 165 or 166 amino acids in length, even though many individual amino acid assignments differ within the family of proteins. We report here the partial amino acid sequence ofmajor species ofhuman leukocyte interferon. These proteins, which represent a significant fraction of the active interferon produced by these cells, lack the 10 COOH-terminal amino acids suggested previously (11-14) from the DNA sequences. Each of the three species is active although lacking the 10 COOH-terminal amino acids.EXPERIMENTAL PROCEDURES Human leukocyte interferon species a,, a2, and 81 were isolated and purified from chronic myelogenous leukemia (CML) cells as has been described (8,(18)(19)(20). Samples of interferon (7-12 nmol) were digested with tosylphenylalanine chloromethyl ketone-treated trypsin (TPCK-trypsin, 0.2 nmol, Worthington) for 19 hr at 370C in 50 ul of 0.2 M NaHCO3. Then, 2-mercaptoethanol (2 pb1) was added and the sample was incubated for 1 hr at 37...

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“…However, all bovine IFN-tr proteins carry Arg or Gly and all human IFN-tr subspecies (about 15) with one exception carry Ser or Tyr at this position. The exception is human IFN-ce~ which also contains a Cys at position 86 [8]. Here, we assess the importance of Cys-86 in rat IFN-oq for antiviral activity by substituting this amino acid by Tyr or Ser.…”

Section: Introductionmentioning

confidence: 99%

The cysteines in position 1 and 86 of rat interferon‐α₁ are indispensable for antiviral activity

1989

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The human, bovine, murine and rat interferon (IFN)-~t families contain 4 conserved cysteines located at positions 1, 29, 99 and 139 that are involved in disulfide bridges. Rat and murine IFN-~t subspecies carry a fifth Cys (Cys-86) which is not conserved in bovine and human IFN-ct subspecies except for human IFN-cfi. Changing Cys-86 in rat IFN-cq into Ser or Tyr virtually abolished antiviral activity. As shown by others, the substitution of Cys-86 to Ser in human IFN-cq had no pronounced effect on activity. This suggests that in contrast to human and bovine IFN-~t, Cys-86 in rodent IFN-ct plays a crucial role in receptor binding. Changing Cys-I to Gly in rat IFN-cq also destroyed activity, in agreement with results obtained in the human IFN-cq system.

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The nucleotide sequence of a cloned human leukocyte Interferon cDNA

Cited by 157 publications

References 22 publications

Differential mRNA Expression of Inflammatory Cytokines in Cultured Human Fetal Membrane Cells Responding to Influenza Virus Infection.

Differential mRNA Expression of Inflammatory Cytokines in Cultured Human Fetal Membrane Cells Responding to Influenza Virus Infection.

Amino acid sequence of a human leukocyte interferon.

The cysteines in position 1 and 86 of rat interferon‐α₁ are indispensable for antiviral activity

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The nucleotide sequence of a cloned human leukocyte Interferon cDNA

Cited by 157 publications

References 22 publications

Differential mRNA Expression of Inflammatory Cytokines in Cultured Human Fetal Membrane Cells Responding to Influenza Virus Infection.

Differential mRNA Expression of Inflammatory Cytokines in Cultured Human Fetal Membrane Cells Responding to Influenza Virus Infection.

Amino acid sequence of a human leukocyte interferon.

The cysteines in position 1 and 86 of rat interferon‐α1 are indispensable for antiviral activity

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The cysteines in position 1 and 86 of rat interferon‐α₁ are indispensable for antiviral activity