Biochemical characterization of the mouse ABCF3 protein, a partner of the flavivirus-resistance protein OAS1B

Peterson, Elizabeth; Shippee, Emma; Brinton, Margo A.; Kaur, Parjit

doi:10.1074/jbc.ra119.008477

Cited by 7 publications

(13 citation statements)

References 84 publications

(123 reference statements)

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“…Another impressive finding among recent reports of using TNP-ATP in protein binding studies is the work of Peterson et al. ( 74 ). In their study of TNP-ATP binding to ABCF3 (a member of the ABC superfamily of membrane transporters; Table 4 ), they observed the expected increase in fluorescence intensity and blue shift.…”

Section: Introductionmentioning

confidence: 92%

“…The same concentrations of ADP and AMP were less potent in competing with TNP-ATP. ABCF3 actually has two NBDs that are reported to be cooperative, such that ATP binding to one domain increases the affinity of the other NBD ( 74 ).…”

Section: Introductionmentioning

confidence: 99%

“…A search on PubMed and Web of Science for the years 2019–2020 shows dozens of works in which TNP-ATP was used to study ATP-interacting proteins, using both its fluorescence and its characteristic high affinity. Some of these were discussed above; additional examples listed below show the clever and diverse ways TNP-ATP is being used: Determining K d (or K 0.5 ) for multiple nucleotides (i.e., ATP, ADP, AMP, and TNP-ATP) with several known nucleotide binding proteins, including VNUT (see Table 1 ) ( 47 ), ABCF3 (see Table 4 ) ( 74 ), and ABCA4 ( 149 ). Determining differences in binding of TNP-ATP to wild-type and mutant proteins including Rad51 (a human DNA binding protein ( 150 )), SaUspA (a stress-sensing protein from Sulfolobus acidocaldarius , see Table 4 ( 79 )), and Cek1 (a MAP kinase from Candida albicans ( 151 )).…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

A review of TNP-ATP in protein binding studies: benefits and pitfalls

Woodbury

Whitt²,

Coffman

2021

Biophysical Reports

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Section: Introductionmentioning

confidence: 92%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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A review of TNP-ATP in protein binding studies: benefits and pitfalls

Woodbury

Whitt²,

Coffman

2021

Biophysical Reports

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“…Expression of Oas1b alone is toxic in bacterial cells, but this toxicity is alleviated by co‐expression with ABCF3. The mechanism by which Oas1b confers resistance to flaviviruses is still unknown, but a genetic screen using a toxicity‐rescue approach could help to decipher the role of ABCF3 [155]. The human version of ABCF3 (hABCF3) is highly expressed in liver, heart, and pancreas, and it is associated with cell proliferation.…”

Section: Eukaryotic Abc‐f Translation Factors—protein Quality Controlmentioning

confidence: 99%

ABC‐F translation factors: from antibiotic resistance to immune response

et al. 2020

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Energy-dependent Translational Throttle A (EttA) from E. coli is a paradigmatic ABC-F protein that controls the first step in polypeptide elongation on the ribosome according to the cellular energy status. Biochemical and structural studies have established that ABC-F proteins generally function as translation factors that modulate the conformation of the peptidyl transferase center upon binding to the ribosomal tRNA exit site. These factors, present in both prokaryotes and eukaryotes but not in archaea, use related molecular mechanisms to modulate protein synthesis for heterogenous purposes, ranging from antibiotic resistance and rescue of stalled ribosomes to modulation of the mammalian immune response. Here we review the canonical studies characterizing the phylogeny, regulation, ribosome interactions, and mechanisms of action of the bacterial ABC-F proteins, and discuss the implications of these studies for the molecular function of eukaryotic ABC-F proteins, including the three human family members.

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“…ABCF3 was found to physically interact with the murine OAS1b and to act as a WNV restriction factor in murine cells (Courtney et al 2012). Recently, ABCF3 was shown to have ATPase activity, though how this activity is connected to the antiviral effect is at present unclear (Peterson et al 2019). Whether the Box 1 Unanswered questions in the restriction of flaviviruses.…”

Section: Oas Rnase L and Abcf3mentioning

confidence: 99%

The Restrictome of Flaviviruses

Berthoux

2020

Virol. Sin.

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Flaviviruses are a genus of mostly arthropod-borne RNA viruses that cause a range of pathologies in humans. Basic knowledge on flaviviruses is rapidly expanding, partly due to their status as frequent emerging or re-emerging pathogens. Flaviviruses include the dengue, Zika, West Nile, tick-borne encephalitis and yellow fever viruses (DENV, ZIKV, WNV, TBEV and YFV, respectively). As is the case with other families of viruses, the success of productive infection of human cells by flaviviruses depends in part on the antiviral activity of a heterogeneous group of cellular antiviral proteins called restriction factors. Restriction factors are the effector proteins of the cell-autonomous innate response against viruses, an immune pathway that also includes virus sensors as well as intracellular and extracellular signal mediators such as type I interferons (IFN-I). In this review, I summarize recent progress toward the identification and characterization of flavivirus restriction factors. In particular, I focus on IFI6, Schlafen 11, FMRP, OAS-RNase L, RyDEN, members of the TRIM family of proteins (TRIM5a, TRIM19, TRIM56, TRIM69 and TRIM79a) and a new mechanism of action proposed for viperin. Recent and future studies on this topic will lead to a more complete picture of the flavivirus restrictome, defined as the ensemble of cellular factors with demonstrated anti-flaviviral activity.

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Biochemical characterization of the mouse ABCF3 protein, a partner of the flavivirus-resistance protein OAS1B

Cited by 7 publications

References 84 publications

A review of TNP-ATP in protein binding studies: benefits and pitfalls

A review of TNP-ATP in protein binding studies: benefits and pitfalls

ABC‐F translation factors: from antibiotic resistance to immune response

The Restrictome of Flaviviruses

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