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CRFK

RRID:CVCL_2426

Organism

Felis catus

Comments

Group: Vaccine production cell line. Part of: Naval Biosciences Laboratory (NBL) collection (transferred to ATCC in 1982). Biotechnology: Widely used to manufacture vaccines for parvoviruses such as feline panleukopenia virus (FPLV) and canine parvoviruses (CPVs). Characteristics: Persistently infected by feline endogenous virus RD-114. Discontinued: ATCC; CRL-6073. DT Created: 04-04-12; Last updated: 06-09-19; Version: 20

Proper Citation

BCRJ Cat# 0072, RRID:CVCL_2426

Category

Spontaneously immortalized cell line DT Created: 04-04-12; Last updated: 06-09-19; Version: 20

Sex

DT Created: 04-04-12; Last updated: 06-09-19; Version: 20

Synonyms

CrFK, Crfk, Crandell Reese Feline Kidney, Crandell Feline Kidney, CCC, Crandell's Cat Cell DT Created: 04-04-12, Last updated: 06-09-19, Version: 20

Vendor

BCRJ

Cat Num

0072

Cross References

CLO; CLO_0002609 CLDB; cl907 CLDB; cl908 ATCC; CCL-94 ATCC; CRL-6073 BCRC; 60151 BCRJ; 0072 CCRID; 3111C0002000000047 CCRID; 3131C0001000400016 CCRID; 3142C0001000000347 CCTCC; GDC0321 ECACC; 86093002 IZSLER; BS CL 22 JCRB; JCRB9035 KCB; KCB 200974YJ KCLB; 10094 Lonza; 801 TOKU-E; 997 Wikidata; Q54814484 DT Created: 04-04-12; Last updated: 06-09-19; Version: 20

Hierarchy

DT Created: 04-04-12; Last updated: 06-09-19; Version: 20

Originate from Same Individual

DT Created: 04-04-12; Last updated: 06-09-19; Version: 20

Publications that use this research resource

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.

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.

Ebola Virus Glycoprotein with Increased Infectivity Dominated the 2013-2016 Epidemic.

  • Diehl WE
  • Cell
  • 2016 Nov 3

Literature context:


Abstract:

The magnitude of the 2013-2016 Ebola virus disease (EVD) epidemic enabled an unprecedented number of viral mutations to occur over successive human-to-human transmission events, increasing the probability that adaptation to the human host occurred during the outbreak. We investigated one nonsynonymous mutation, Ebola virus (EBOV) glycoprotein (GP) mutant A82V, for its effect on viral infectivity. This mutation, located at the NPC1-binding site on EBOV GP, occurred early in the 2013-2016 outbreak and rose to high frequency. We found that GP-A82V had heightened ability to infect primate cells, including human dendritic cells. The increased infectivity was restricted to cells that have primate-specific NPC1 sequences at the EBOV interface, suggesting that this mutation was indeed an adaptation to the human host. GP-A82V was associated with increased mortality, consistent with the hypothesis that the heightened intrinsic infectivity of GP-A82V contributed to disease severity during the EVD epidemic.