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MDCK

RRID:CVCL_0422

Organism

Canis lupus familiaris

Comments

Group: Vaccine production cell line. Part of: Naval Biosciences Laboratory (NBL) collection (transferred to ATCC in 1982). Caution: There seems to be two distinct cell lines which were assigned NCBI_Iran catalog number C426. Discontinued: ATCC; CRL-6253. Breed/subspecies: Cocker Spaniel. DT Created: 04-04-12; Last updated: 24-05-19; Version: 25

Proper Citation

CLS Cat# 602280/p823_MDCK_(NBL-2), RRID:CVCL_0422

Category

Spontaneously immortalized cell line DT Created: 04-04-12; Last updated: 24-05-19; Version: 25

Sex

DT Created: 04-04-12; Last updated: 24-05-19; Version: 25

Synonyms

MDCK (NBL-2), NBL-2, Madin-Darby Canine Kidney, Madin Darby Canine Kidney DT Created: 04-04-12, Last updated: 24-05-19, Version: 25

Vendor

CLS

Cat Num

602280/p823_MDCK_(NBL-2)

Cross References

BTO; BTO:0000837 CLO; CLO_0007646 CLO; CLO_0007647 CLO; CLO_0050861 MCCL; MCC:0000319 CLDB; cl3417 CLDB; cl3418 CLDB; cl3419 CLDB; cl3420 CLDB; cl3421 CLDB; cl3422 CLDB; cl3423 CLDB; cl3424 CLDB; cl3425 AddexBio; P0014003/4928 ATCC; CCL-34 ATCC; CRL-6253 BCRC; 60004 BCRJ; 0168 BEI_Resources; NR-2628 CCLV; CCLV-RIE 0083 CCRID; 3111C0001CCC000078 CCRID; 3111C0002000000045 CCRID; 3131C0001000400014 CCRID; 3131C0001000400024 CCRID; 3142C0001000000012 CCRID; 3142C0001000000147 CCTCC; GDC0012 CCTCC; GDC0401 ChEMBL-Cells; CHEMBL3308370 ChEMBL-Targets; CHEMBL614068 CLS; 602280/p823_MDCK_(NBL-2) ECACC; 84121903 ECACC; 85011435 IBRC; C10556 IZSLER; BS CL 64 JCRB; IFO50071 JCRB; JCRB9029 KCB; KCB 2006105YJ KCLB; 10034 Lonza; 153 MeSH; D061985 NCBI_Iran; C426 RCB; RCB0995 TOKU-E; 2403 TOKU-E; 3636 Wikidata; Q28335011 DT Created: 04-04-12; Last updated: 24-05-19; Version: 25

Hierarchy

DT Created: 04-04-12; Last updated: 24-05-19; Version: 25

Originate from Same Individual

DT Created: 04-04-12; Last updated: 24-05-19; Version: 25

Influenza Virus Mounts a Two-Pronged Attack on Host RNA Polymerase II Transcription.

  • Bauer DLV
  • Cell Rep
  • 2018 May 15

Literature context:


Abstract:

Influenza virus intimately associates with host RNA polymerase II (Pol II) and mRNA processing machinery. Here, we use mammalian native elongating transcript sequencing (mNET-seq) to examine Pol II behavior during viral infection. We show that influenza virus executes a two-pronged attack on host transcription. First, viral infection causes decreased Pol II gene occupancy downstream of transcription start sites. Second, virus-induced cellular stress leads to a catastrophic failure of Pol II termination at poly(A) sites, with transcription often continuing for tens of kilobases. Defective Pol II termination occurs independently of the ability of the viral NS1 protein to interfere with host mRNA processing. Instead, this termination defect is a common effect of diverse cellular stresses and underlies the production of previously reported downstream-of-gene transcripts (DoGs). Our work has implications for understanding not only host-virus interactions but also fundamental aspects of mammalian transcription.

Funding information:
  • PHS HHS - NIMH R01 MH094609(United States)

Nuclear TRIM25 Specifically Targets Influenza Virus Ribonucleoproteins to Block the Onset of RNA Chain Elongation.

  • Meyerson NR
  • Cell Host Microbe
  • 2017 Nov 8

Literature context:


Abstract:

TRIM25 is an E3 ubiquitin ligase that activates RIG-I to promote the antiviral interferon response. The NS1 protein from all strains of influenza A virus binds TRIM25, although not all virus strains block the interferon response, suggesting alternative mechanisms for TRIM25 action. Here we present a nuclear role for TRIM25 in specifically restricting influenza A virus replication. TRIM25 inhibits viral RNA synthesis through a direct mechanism that is independent of its ubiquitin ligase activity and the interferon pathway. This activity can be inhibited by the viral NS1 protein. TRIM25 inhibition of viral RNA synthesis results from its binding to viral ribonucleoproteins (vRNPs), the structures containing individual viral RNA segments, the viral polymerase, and multiple viral nucleoproteins. TRIM25 binding does not inhibit initiation of capped-RNA-primed viral mRNA synthesis by the viral polymerase. Rather, the onset of RNA chain elongation is inhibited because TRIM25 prohibits the movement of RNA into the polymerase complex.

Dichotomous Expression of TNF Superfamily Ligands on Antigen-Presenting Cells Controls Post-priming Anti-viral CD4+ T Cell Immunity.

  • Chang YH
  • Immunity
  • 2017 Nov 21

Literature context:


Abstract:

T cell antigen-presenting cell (APC) interactions early during chronic viral infection are crucial for determining viral set point and disease outcome, but how and when different APC subtypes contribute to these outcomes is unclear. The TNF receptor superfamily (TNFRSF) member GITR is important for CD4+ T cell accumulation and control of chronic lymphocytic choriomeningitis virus (LCMV). We found that type I interferon (IFN-I) induced TNFSF ligands GITRL, 4-1BBL, OX40L, and CD70 predominantly on monocyte-derived APCs and CD80 and CD86 predominantly on classical dendritic cells (cDCs). Mice with hypofunctional GITRL in Lyz2+ cells had decreased LCMV-specific CD4+ T cell accumulation and increased viral load. GITR signals in CD4+ T cells occurred after priming to upregulate OX40, CD25, and chemokine receptor CX3CR1. Thus IFN-I (signal 3) induced a post-priming checkpoint (signal 4) for CD4+ T cell accumulation, revealing a division of labor between cDCs and monocyte-derived APCs in regulating T cell expansion.

Funding information:
  • NIA NIH HHS - P01 AG017617(United States)

Helicobacter pylori Employs a Unique Basolateral Type IV Secretion Mechanism for CagA Delivery.

  • Tegtmeyer N
  • Cell Host Microbe
  • 2017 Oct 11

Literature context:


Abstract:

The Helicobacter pylori (Hp) type IV secretion system (T4SS) forms needle-like pili, whose binding to the integrin-β1 receptor results in injection of the CagA oncoprotein. However, the apical surface of epithelial cells is exposed to Hp, whereas integrins are basolateral receptors. Hence, the mechanism of CagA delivery into polarized gastric epithelial cells remains enigmatic. Here, we demonstrate that T4SS pilus formation during infection of polarized cells occurs predominantly at basolateral membranes, and not at apical sites. Hp accomplishes this by secreting another bacterial protein, the serine protease HtrA, which opens cell-to-cell junctions through cleaving epithelial junctional proteins including occludin, claudin-8, and E-cadherin. Using a genetic system expressing a peptide inhibitor, we demonstrate that HtrA activity is necessary for paracellular transmigration of Hp across polarized cell monolayers to reach basolateral membranes and inject CagA. The contribution of this unique signaling cascade to Hp pathogenesis is discussed.

Funding information:
  • NIGMS NIH HHS - GM032877(United States)

Epitranscriptomic Enhancement of Influenza A Virus Gene Expression and Replication.

  • Courtney DG
  • Cell Host Microbe
  • 2017 Sep 13

Literature context:


Abstract:

Many viral RNAs are modified by methylation of the N6 position of adenosine (m6A). m6A is thought to regulate RNA splicing, stability, translation, and secondary structure. Influenza A virus (IAV) expresses m6A-modified RNAs, but the effects of m6A on this segmented RNA virus remain unclear. We demonstrate that global inhibition of m6A addition inhibits IAV gene expression and replication. In contrast, overexpression of the cellular m6A "reader" protein YTHDF2 increases IAV gene expression and replication. To address whether m6A residues modulate IAV RNA function in cis, we mapped m6A residues on the IAV plus (mRNA) and minus (vRNA) strands and used synonymous mutations to ablate m6A on both strands of the hemagglutinin (HA) segment. These mutations inhibited HA mRNA and protein expression while leaving other IAV mRNAs and proteins unaffected, and they also resulted in reduced IAV pathogenicity in mice. Thus, m6A residues in IAV transcripts enhance viral gene expression.

Funding information:
  • NCI NIH HHS - T32 CA009111()
  • NIAID NIH HHS - R21 AI130574()
  • NIGMS NIH HHS - T32 GM007184()

The RNA Exosome Syncs IAV-RNAPII Transcription to Promote Viral Ribogenesis and Infectivity.

  • Rialdi A
  • Cell
  • 2017 May 4

Literature context:


Abstract:

The nuclear RNA exosome is an essential multi-subunit complex that controls RNA homeostasis. Congenital mutations in RNA exosome genes are associated with neurodegenerative diseases. Little is known about the role of the RNA exosome in the cellular response to pathogens. Here, using NGS and human and mouse genetics, we show that influenza A virus (IAV) ribogenesis and growth are suppressed by impaired RNA exosome activity. Mechanistically, the nuclear RNA exosome coordinates the initial steps of viral transcription with RNAPII at host promoters. The viral polymerase complex co-opts the nuclear RNA exosome complex and cellular RNAs en route to 3' end degradation. Exosome deficiency uncouples chromatin targeting of the viral polymerase complex and the formation of cellular:viral RNA hybrids, which are essential RNA intermediates that license transcription of antisense genomic viral RNAs. Our results suggest that evolutionary arms races have shaped the cellular RNA quality control machinery.

Funding information:
  • NIAID NIH HHS - R01 AI099195()
  • NIAID NIH HHS - U19 AI106754()
  • NIH HHS - DP2 OD008651()

Co-option of an endogenous retrovirus envelope for host defense in hominid ancestors.

  • Blanco-Melo D
  • Elife
  • 2017 Apr 11

Literature context:


Abstract:

Endogenous retroviral sequences provide a molecular fossil record of ancient infections whose analysis might illuminate mechanisms of viral extinction. A close relative of gammaretroviruses, HERV-T, circulated in primates for ~25 million years (MY) before apparent extinction within the past ~8 MY. Construction of a near-complete catalog of HERV-T fossils in primate genomes allowed us to estimate a ~32 MY old ancestral sequence and reconstruct a functional envelope protein (ancHTenv) that could support infection of a pseudotyped modern gammaretrovirus. Using ancHTenv, we identify monocarboxylate transporter-1 (MCT-1) as a receptor used by HERV-T for attachment and infection. A single HERV-T provirus in hominid genomes includes an env gene (hsaHTenv) that has been uniquely preserved. This apparently exapted HERV-T env could not support virion infection but could block ancHTenv mediated infection, by causing MCT-1 depletion from cell surfaces. Thus, hsaHTenv may have contributed to HERV-T extinction, and could also potentially regulate cellular metabolism.

Suppressor of cytokine signaling (SOCS)5 ameliorates influenza infection via inhibition of EGFR signaling.

  • Kedzierski L
  • Elife
  • 2017 Feb 14

Literature context:


Abstract:

Influenza virus infections have a significant impact on global human health. Individuals with suppressed immunity, or suffering from chronic inflammatory conditions such as COPD, are particularly susceptible to influenza. Here we show that suppressor of cytokine signaling (SOCS) five has a pivotal role in restricting influenza A virus in the airway epithelium, through the regulation of epidermal growth factor receptor (EGFR). Socs5-deficient mice exhibit heightened disease severity, with increased viral titres and weight loss. Socs5 levels were differentially regulated in response to distinct influenza viruses (H1N1, H3N2, H5N1 and H11N9) and were reduced in primary epithelial cells from COPD patients, again correlating with increased susceptibility to influenza. Importantly, restoration of SOCS5 levels restricted influenza virus infection, suggesting that manipulating SOCS5 expression and/or SOCS5 targets might be a novel therapeutic approach to influenza.