A Heterogeneous Nuclear Ribonucleoprotein A/B-Related Protein Binds to Single-Stranded DNA near the 5′ End or within the Genome of Feline Parvovirus and Can Modify Virus Replication

Wang, Dai; Parrish, Colin R.

doi:10.1128/jvi.73.9.7761-7768.1999

Cited by 23 publications

(10 citation statements)

References 57 publications

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“… 16 Of the other identified proteins, to our knowledge none has been described in the context of AAV so far. However, heterogeneous ribonucleoproteins including HNRNPA2B1 and HNRNPAB were shown to interact with the capsid of feline parvovirus 17 and to be involved in viral replication and assembly of human papillomavirus (HPV), HIV, mouse hepatitis virus (MHV), Japanese encephalitis virus (JEV), and Junin virus. 18–22 Moreover, HTATSF1 and HSP90B1 have been linked to HIV transcription, 23 splicing, 24 and infectivity, 25 respectively.…”

Section: Discussionmentioning

confidence: 99%

Comparative Analysis of Cesium Chloride- and Iodixanol-Based Purification of Recombinant Adeno-Associated Viral Vectors for Preclinical Applications

Strobel

Miller

Rist

et al. 2015

Human Gene Therapy Methods

130

115

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Cesium chloride (CsCl)- and iodixanol-based density gradients represent the core step in most protocols for serotype-independent adeno-associated virus (AAV) purification established to date. However, despite controversial reports about the purity and bioactivity of AAV vectors derived from each of these protocols, systematic comparisons of state-of-the-art variants of these methods are sparse. To define exact conditions for such a comparison, we first fractionated both gradients to analyze the distribution of intact, bioactive AAVs and contaminants, respectively. Moreover, we tested four different polishing methods (ultrafiltration, size-exclusion chromatography, hollow-fiber tangential flow filtration, and polyethylene glycol precipitation) implemented after the iodixanol gradient for their ability to deplete iodixanol and protein contaminations. Last, we conducted a side-by-side comparison of the CsCl and iodixanol/ultrafiltration protocol. Our results demonstrate that iodixanol-purified AAV preparations show higher vector purity but harbor more (∼20%) empty particles as compared with CsCl-purified vectors (<1%). Using mass spectrometry, we analyzed prominent protein impurities in the AAV vector product, thereby identifying known and new, possibly AAV-interacting proteins as major contaminants. Thus, our study not only provides a helpful guide for the many laboratories entering the AAV field, but also builds a basis for further investigation of cellular processes involved in AAV vector assembly and trafficking.

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Section: Discussionmentioning

confidence: 99%

Comparative Analysis of Cesium Chloride- and Iodixanol-Based Purification of Recombinant Adeno-Associated Viral Vectors for Preclinical Applications

Strobel

Miller

Rist

et al. 2015

Human Gene Therapy Methods

130

115

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“…Apobec‐1‐binding protein participates in mRNA‐editing through binding in the nucleus to both apobec‐1 (the catalytic component of editosome) and its substrate apolipoprotein B mRNA [48]. On the other hand, DBP 40 protein binds to specific sequences of feline parvovirus single‐stranded DNA and blocks viral DNA replication [49]. Other members of this family have been characterized to function by binding to DNA mostly as transcription factors: type A/B hnRNP‐like protein p40 activates the serine protease inhibitor 2 genes (accession no: ).…”

Section: Discussionmentioning

confidence: 99%

S1 proteins C2 and D2 are novel hnRNPs similar to the transcriptional repressor, CArG box motif‐binding factor A

Inoue

Omori

Ichinose

et al. 2001

European Journal of Biochemistry

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S1 proteins A±D are liberated from thoroughly washed nuclei by mild digestion with DNase I or RNase A, and extracted selectively at pH 4.9 from the reaction supernatants. Here, we characterized the S1 proteins, focusing on protein D2, the most abundant S1 protein in the rat liver, and on protein C2 as well. Using a specific antibody, McAb 351, they were shown to occur in the extranucleolar nucleoplasm, and to be extracted partly in the nuclear soluble fraction. We demonstrate that the S1 proteins in this fraction exist constituting heterogeneous nuclear ribonucleoproteins (hnRNPs), through direct binding to hnRNAs, as revealed by centrifugation on density gradients, immunoprecipitation, and UV cross-linking. In hnRNPs, protein D2 occurred at nuclease-hypersensitive sites and C2 in the structures that gave rise to 40 S RNP particles. By microsequencing, protein D2 was identified with a known protein, CArG box motif-binding factor A (CBF-A), which has been characterized as a transcriptional repressor, and C2 as its isoform protein. In fact, CBF-A expressed from its cDNA was indistinguishable from protein D2 in molecular size and immunoreactivity to McAb 351. Thus, the present results demonstrate that S1 proteins C2 and D2 are novel hnRNP proteins, and suggest that the proteins C2 and D2 act in both transcriptional and post-transcriptional processes in gene expression.

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“…A functional role has been proposed for some of these proteins (ssDBF as a liver-specific transcription factor [21], CBF-A ± and probably the almost identical hnRNP 38 from rat ± as a muscle-specific transcription factor [27], and human ABBP1 as an RNA-editing factor [28]) whereas for the feline DBP40 the ability to interact with the 5 H -terminal sequence of a panleukopenia virus has been shown [29]. Nothing is known about the functions of the human-type A/B hnRNP [30], CRP1 [22], rat hnRNP 40 and PRM10.…”

Section: Discussionmentioning

confidence: 99%

A chicken hnRNP of the A/B family recognizes the single‐stranded d(CCCTAA)_n telomeric repeated motif

Marsich¹,

Bandiera²,

Tell³

et al. 2001

European Journal of Biochemistry

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With the aim of identifying proteins able to interact with the C-rich single-stranded telomeric repeated motif, three nuclear polypeptides, CBNPa, CBNPb and CBNPg, with apparent mobilities in SDS/PAGE of 38, 44 and 55 kDa, respectively, were isolated from mature chicken erythrocytes by affinity chromatography. In situ UV-cross-linking experiments demonstrated that CBNPa and CBNPg interact directly with the telomeric d(CCCTAA) n repeat, whereas CBNPb does not. Moreover, they provided information on the protein components responsible for each electrophoretic mobility-shift assay signal. Ion spray and matrix-assisted laser desorption ionization MS allowed us to identify CBNPa with single-stranded D-box-binding factor (ssDBF), a protein previously characterized as a transcription factor belonging to the A/B family of heterogeneous nuclear ribonucleoproteins, and CBNPb with an isoform of this protein containing an extra exon. Similarly, CBNPg was shown to be probably the chicken homolog of hnRNP K, a ribonuclear protein able to bind to polyC oligonucleotides. The relation of CBNPa (i.e. ssDBF), CBNPb and CBNPg to a number of similar proteins in the protein and nucleotide sequence databank is discussed. A rather diversified spectrum of functional roles has been assigned to some of these proteins despite the strong sequence homology among them.Keywords: heterogeneous ribonucleoproteins (hnRNPs); nuclear proteins; ssDNA recognition; telomeric C-rich motif.Since the discovery of the special features of repetitive DNA which constitutes the majority of telomeres of eukaryotic organisms, and of its specific replication machinery, considerable attention has also been directed to identifying and characterizing nuclear proteins that specifically bind to this DNA, in the normal Watson±Crick duplex form, as well as to the protruding single-stranded G-rich 3 H overhang at the telomere terminus. Many proteins such as TRF1 and TRF2 that bind to duplex telomeric DNA in mammalian cells [1] and Rap1p in yeast [2] have been reported to be involved in telomere length maintenance and regulation of telomerase activity. In unicellular organisms, several proteins, such as ab protein from Oxytricha , also bind to the single-stranded G-rich telomeric motif, although their function has not been fully ascertained. The last of these, however, is the first ssDNA-binding protein shown to be directly involved in mammalian telomere biogenesis, suggesting a possible mechanism by which telomere length can be modulated [13]. Much less attention has been given to identifying nuclear components able to recognize the complementary single-stranded C-rich DNA repeat. Interestingly, a protein from Trypanosoma, ST-1, binds to the telomeric double-stranded repeat as well as to its singlestranded C-rich component [14]. In vertebrates, the nuclear protein from rat hepatocytes, qTBP42, has been shown to recognize each of the single-stranded forms of the telomeric repeat [9]. Several proteins that interact with polypyrimidine ssDNA have been described. They includ...

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A Heterogeneous Nuclear Ribonucleoprotein A/B-Related Protein Binds to Single-Stranded DNA near the 5′ End or within the Genome of Feline Parvovirus and Can Modify Virus Replication

Cited by 23 publications

References 57 publications

Comparative Analysis of Cesium Chloride- and Iodixanol-Based Purification of Recombinant Adeno-Associated Viral Vectors for Preclinical Applications

Comparative Analysis of Cesium Chloride- and Iodixanol-Based Purification of Recombinant Adeno-Associated Viral Vectors for Preclinical Applications

S1 proteins C2 and D2 are novel hnRNPs similar to the transcriptional repressor, CArG box motif‐binding factor A

A chicken hnRNP of the A/B family recognizes the single‐stranded d(CCCTAA)_n telomeric repeated motif

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A Heterogeneous Nuclear Ribonucleoprotein A/B-Related Protein Binds to Single-Stranded DNA near the 5′ End or within the Genome of Feline Parvovirus and Can Modify Virus Replication

Cited by 23 publications

References 57 publications

Comparative Analysis of Cesium Chloride- and Iodixanol-Based Purification of Recombinant Adeno-Associated Viral Vectors for Preclinical Applications

Comparative Analysis of Cesium Chloride- and Iodixanol-Based Purification of Recombinant Adeno-Associated Viral Vectors for Preclinical Applications

S1 proteins C2 and D2 are novel hnRNPs similar to the transcriptional repressor, CArG box motif‐binding factor A

A chicken hnRNP of the A/B family recognizes the single‐stranded d(CCCTAA)n telomeric repeated motif

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A chicken hnRNP of the A/B family recognizes the single‐stranded d(CCCTAA)_n telomeric repeated motif