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Homo sapiens


Group: Retrovirus packaging cell line. Transfected with: UniProtKB; P00552; Transposon Tn5 neo. Transformant: NCBI_TaxID; 28285; Adenovirus 5. Transformant: NCBI_TaxID; 1891767; Simian virus 40 (SV40) [tsA]. Discontinued: ATCC; CRL-11270. DT Created: 04-04-12; Last updated: 24-05-19; Version: 14

Proper Citation

ATCC Cat# CRL-11270, RRID:CVCL_4401




Transformed cell line DT Created: 04-04-12; Last updated: 24-05-19; Version: 14


DT Created: 04-04-12; Last updated: 24-05-19; Version: 14


Bosc-23, BOSC 23, Bosc 23, BOSC23, Bosc23, Lenti-X 293T DT Created: 04-04-12, Last updated: 24-05-19, Version: 14



Cat Num


Cross References

BTO; BTO:0004573 ATCC; CRL-11270 IBRC; C10142 TOKU-E; 3585 Wikidata; Q4836226 DT Created: 04-04-12; Last updated: 24-05-19; Version: 14


DT Created: 04-04-12; Last updated: 24-05-19; Version: 14

Originate from Same Individual

DT Created: 04-04-12; Last updated: 24-05-19; Version: 14

Empty conformers of HLA-B preferentially bind CD8 and regulate CD8+ T cell function.

  • Geng J
  • Elife
  • 2018 May 9

Literature context:


When complexed with antigenic peptides, human leukocyte antigen (HLA) class I (HLA-I) molecules initiate CD8+ T cell responses via interaction with the T cell receptor (TCR) and co-receptor CD8. Peptides are generally critical for the stable cell surface expression of HLA-I molecules. However, for HLA-I alleles such as HLA-B*35:01, peptide-deficient (empty) heterodimers are thermostable and detectable on the cell surface. Additionally, peptide-deficient HLA-B*35:01 tetramers preferentially bind CD8 and to a majority of blood-derived CD8+ T cells via a CD8-dependent binding mode. Further functional studies reveal that peptide-deficient conformers of HLA-B*35:01 do not directly activate CD8+ T cells, but accumulate at the immunological synapse in antigen-induced responses, and enhance cognate peptide-induced cell adhesion and CD8+ T cell activation. Together, these findings indicate that HLA-I peptide occupancy influences CD8 binding affinity, and reveal a new set of regulators of CD8+ T cell activation, mediated by the binding of empty HLA-I to CD8.

Funding information:
  • NIAID NIH HHS - R01 AI044115()
  • NIH Office of the Director - AI044115()
  • NIH Office of the Director - R01AI044115()
  • PHS HHS - P01-155258(United States)

Proteolytic processing of palmitoylated Hedgehog peptides specifies the 3-4 intervein region of the Drosophila wing.

  • Schürmann S
  • Elife
  • 2018 Mar 9

Literature context:


Cell fate determination during development often requires morphogen transport from producing to distant responding cells. Hedgehog (Hh) morphogens present a challenge to this concept, as all Hhs are synthesized as terminally lipidated molecules that form insoluble clusters at the surface of producing cells. While several proposed Hh transport modes tie directly into these unusual properties, the crucial step of Hh relay from producing cells to receptors on remote responding cells remains unresolved. Using wing development in Drosophila melanogaster as a model, we show that Hh relay and direct patterning of the 3-4 intervein region strictly depend on proteolytic removal of lipidated N-terminal membrane anchors. Site-directed modification of the N-terminal Hh processing site selectively eliminated the entire 3-4 intervein region, and additional targeted removal of N-palmitate restored its formation. Hence, palmitoylated membrane anchors restrict morphogen spread until site-specific processing switches membrane-bound Hh into bioactive forms with specific patterning functions.

Funding information:
  • Cells-in-Motion Cluster of Excellence - FF-2015-02()
  • Deutsche Forschungsgemeinschaft - GR1748/4-1()
  • Deutsche Forschungsgemeinschaft - GR1748/5-1()
  • Deutsche Forschungsgemeinschaft - GRK1549/1()
  • Howard Hughes Medical Institute - R01 GM052339(United States)

Intrinsic Immunity Shapes Viral Resistance of Stem Cells.

  • Wu X
  • Cell
  • 2018 Jan 25

Literature context:


Stem cells are highly resistant to viral infection compared to their differentiated progeny; however, the mechanism is mysterious. Here, we analyzed gene expression in mammalian stem cells and cells at various stages of differentiation. We find that, conserved across species, stem cells express a subset of genes previously classified as interferon (IFN) stimulated genes (ISGs) but that expression is intrinsic, as stem cells are refractory to interferon. This intrinsic ISG expression varies in a cell-type-specific manner, and many ISGs decrease upon differentiation, at which time cells become IFN responsive, allowing induction of a broad spectrum of ISGs by IFN signaling. Importantly, we show that intrinsically expressed ISGs protect stem cells against viral infection. We demonstrate the in vivo importance of intrinsic ISG expression for protecting stem cells and their differentiation potential during viral infection. These findings have intriguing implications for understanding stem cell biology and the evolution of pathogen resistance.

Funding information:
  • NIAID NIH HHS - R01 AI091707()
  • NIAID NIH HHS - U19 AI111825()
  • NIDDK NIH HHS - R01 DK100810()
  • NINDS NIH HHS - R01 NS046789-09S1(United States)

Diverse Viruses Require the Calcium Transporter SPCA1 for Maturation and Spread.

  • Hoffmann HH
  • Cell Host Microbe
  • 2017 Oct 11

Literature context:


Respiratory and arthropod-borne viral infections are a global threat due to the lack of effective antivirals and vaccines. A potential strategy is to target host proteins required for viruses but non-essential for the host. To identify such proteins, we performed a genome-wide knockout screen in human haploid cells and identified the calcium pump SPCA1. SPCA1 is required by viruses from the Paramyxoviridae, Flaviviridae, and Togaviridae families, including measles, dengue, West Nile, Zika, and chikungunya viruses. Calcium transport activity is required for SPCA1 to promote virus spread. SPCA1 regulates proteases within the trans-Golgi network that require calcium for their activity and are critical for virus glycoprotein maturation. Consistent with these findings, viral glycoproteins fail to mature in SPCA1-deficient cells preventing viral spread, which is evident even in cells with partial loss of SPCA1. Thus, SPCA1 is an attractive antiviral host target for a broad spectrum of established and emerging viral infections.

Funding information:
  • NIDDK NIH HHS - F32 DK095666()
  • NIGMS NIH HHS - GM43644(United States)

Ancestral Reconstruction Approach to Acetylcholine Receptor Structure and Function.

  • Prinston JE
  • Structure
  • 2017 Aug 1

Literature context:


Acetylcholine receptors (AChRs) are members of a superfamily of proteins called pentameric ligand-gated ion channels, which are found in almost all forms of life and thus have a rich evolutionary history. Muscle-type AChRs are heteropentameric complexes assembled from four related subunits (α, β, δ, and ɛ). Here we reconstruct the amino acid sequence of a β subunit ancestor shared by humans and cartilaginous fishes (i.e., Torpedo). Then, by resurrecting this ancestral β subunit and co-expressing it with human α, δ, and ɛ subunits, we show that despite 132 substitutions, the ancestral subunit is capable of forming human/ancestral hybrid AChRs. Whole-cell currents demonstrate that the agonist acetylcholine has reduced potency for hybrid receptors, while single-channel recordings reveal that hybrid receptors display reduced conductance and open probability. Our results outline a promising strategy for studies of AChR evolution aimed at identifying the amino acid origins of AChR structure and function.

Mesenchyme Homeobox 2 Enhances Migration of Endothelial Colony Forming Cells Exposed to Intrauterine Diabetes Mellitus.

  • Gohn CR
  • J. Cell. Physiol.
  • 2017 May 15

Literature context:


Diabetes mellitus (DM) during pregnancy has long-lasting implications for the fetus, including cardiovascular morbidity. Previously, we showed that endothelial colony forming cells (ECFCs) from DM human pregnancies have decreased vasculogenic potential. Here, we evaluate whether the molecular mechanism responsible for this phenotype involves the transcription factor, Mesenchyme Homeobox 2 (MEOX2). In human umbilical vein endothelial cells, MEOX2 upregulates cyclin-dependent kinase inhibitor expression, resulting in increased senescence and decreased proliferation. We hypothesized that dysregulated MEOX2 expression in neonatal ECFCs from DM pregnancies decreases network formation through increased senescence and altered cell cycle progression. Our studies show that nuclear MEOX2 is increased in ECFCs from DM pregnancies. To determine if MEOX2 is sufficient and/or required to induce impaired network formation, MEOX2 was overexpressed and depleted in ECFCs from control and DM pregnancies, respectively. Surprisingly, MEOX2 overexpression in control ECFCs resulted in increased network formation, altered cell cycle progression, and increased senescence. In contrast, MEOX2 knockdown in ECFCs from DM pregnancies led to decreased network formation, while cell cycle progression and senescence were unaffected. Importantly, migration studies demonstrated that MEOX2 overexpression increased migration, while MEOX2 knockdown decreased migration. Taken together, these data suggest that altered migration may be mediating the impaired vasculogenesis of ECFCs from DM pregnancies. While initially believed to be maladaptive, these data suggest that MEOX2 may serve a protective role, enabling increased vessel formation despite exposure to a DM intrauterine environment. J. Cell. Physiol. 232: 1885-1892, 2017. © 2016 Wiley Periodicals, Inc.