Cloning and nucleotide sequence of the capsid protein and the nuclear inclusion protein (NIb) of potato virus A

brief report by Richard Frederick Collins

Publisher: Springer-Verlag in [Vienna]

Written in English
Published: Pages: 142 Downloads: 75
Share This

Subjects:

  • Potato mosaic virus.,
  • Potato virus A.

Edition Notes

Includes bibliographical references.

Statement[by] R.F. Collins, D. Leclerc, and M.G. AbouHaidar.
SeriesArch Virol (1992) 128
The Physical Object
Paginationpp. [135]-142.
Number of Pages142
ID Numbers
Open LibraryOL14615442M

1. Virus enters cell uncoated, releases viral DNA and capsid proteins 2. Host enzymes replicate viral enzyme 3. Host enzymes transcribe the viral genome into viral mRNA; host ribosomes are used to make capsids 4. Viral genomes, capsid proteins self-assemble into new virus particles that exit the cell. Molecular cloning is a set of experimental methods in molecular biology that are used to assemble recombinant DNA molecules and to direct their replication within host organisms. The use of the word cloning refers to the fact that the method involves the replication of one molecule to produce a population of cells with identical DNA molecules. Molecular cloning generally . This is processed into seven smaller proteins: P1, helper component (HC), P3, cylindrical inclusion (CI), nuclear inclusion A (NIa), nuclear inclusion B (NIb), capsid protein (CP) and two small putative proteins known as 6K1 and 6K2. The P3 cistron also encodes a second protein—P3N-PIPO—which is generated by a +2 : Potyviridae. The success of gene therapy depends in part on our understanding of the biology of gene therapy vectors. This knowledge must be used to improve the function, safety, and versatility of the vector system. For decades, we have known which viral proteins are involved in formation of the adenovirus (Ad) capsid, but we are still learning how these proteins can be altered or Cited by:

The capsid protein is the major structural component of the icosahedral Tipula iridescent virus (TIV) (a virus originally isolated from T. paludosa) that replicates in cytoplasmic inclusion bodies of insect cells. TIV capsid protein purified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was digested with trypsin and fractionated by reverse-phase Cited by: The proposed locations of the cleavage sites predict eight to nine proteins consisting of P1 (63K), helper component (HC-Pro, 52K), P3 (46K), cylindrical inclusion protein (C1, 72K), nuclear inclusion protein a (NIa, 48K), nuclear inclusion protein b (NIb, 59K), and coat protein (CP, 35K) [].The P1 protein is encoded by the Potyvirus genome and autocatalytically by: Complementary DNA cloning and expression of the papaya ringspot potyvirus sequences encoding capsid protein and a nuclear inclusion-like protein in .   Fig. Schematic depiction of the expression cassette of plasmid pBIM A. Nucleotide sequence of the DNA fragment encoding the peptide M B. Expression cassette obtained after cloning the Mencoding sequence into plasmid pBI 42 A: Frond regeneration from kanamycin-resistant callus after 10 weeks of growth on NPM regeneration .

Definition of Capsid. 1. Noun. The outer protein shell of a virus. ¹. ¹ Source: Definition of Capsid. 1. the outer shell of a virus particle [n -S]: CAPSIDAL [adj] Medical Definition of Capsid. 1. A protein coat that covers the nucleoprotein core or nucleic acid of a . 6. Proviral genes are transcribed into RNA molecules, which serve as genomes for the next viral generation and as mRNAs for translation into viral protein 7. The viral proteins include capsid proteins and reverse transcriptase (made in the cytosol) and envelope glycoproteins 8. Vesicles transport the glycoproteins to the cell's plasma membrane 9. The viral capsid of a parvovirus is made up of 60 copies of two or more size variants of a single protein sequence, called VP1, VP2 etc., which form a resilient structure with T=1 icosahedral symmetry. These virions are typically resistant to dilute acids, bases, solvents, and temperatures up to 50°C (°F).Parvoviruses do not have envelopes, thus are considered "naked" viruses. Cauliflower mosaic virus (CaMV) is the type species of the family family is grouped together with Hepadnaviruses into the Pararetrovirus group due to its mode of replication via reverse transcription of a pre-genomic RNA intermediate.. CaMV infects mostly plants of the family Brassicaceae (such as cauliflower and turnip) but some CaMV strains (D4 and W) Family: Caulimoviridae.

Cloning and nucleotide sequence of the capsid protein and the nuclear inclusion protein (NIb) of potato virus A by Richard Frederick Collins Download PDF EPUB FB2

Furthermore, there are two AUG codons in frame in front of the capsid protein gene suggesting an alternative mode for the capsid protein expression. The sequence of the 3′-terminal nucleotides of potato virus A (PVA) genome has been determined from cDNA by: 7. Cloning and nucleotide sequence of the capsid protein and the nuclear inclusion protein (NIb) of potato virus A Article (PDF Available) in Archives of Virology ().

Cloning and nucleotide sequence of the capsid protein and the nuclear inclusion protein (NIb) of potato virus A. R F Collins Department of Botany, University of Toronto, Ontario, by: 7. The coding nucleotide sequence and amino acid sequence presented in this paper enable location of the PPV capsid protein gene.

As in other sequenced potyvirus RNAs, the PPV capsid protein gene is at the 3' end of the coding sequence. This protein starts with an alanine codon (GCU) and terminates with a UAG codon.

Comparison with other sequenced potyviruses indicated that each clone contained the 3′-non-coding region (3′NCR), the coat protein (CP) gene and part of the nuclear inclusion protein (NIb) gene. Nucleotide and amino acid sequence comparisons of the 3′-terminal regions of these and other rymoviruses indicate that distinct groups exist.

The open reading frame (ORF) of iridovirus capsid protein. The IJP03 clone contains complete ORF contains nucleotides from start codon ATG to the stop codon TAA.

The IGD01 clone only contains nucleotide 1 - VIROLOGY() Complementary DNA Cloning and Expression of the Papaya Ringspot Potyvirus Sequences Encoding Capsid Protein and a Nuclear Inclusion-like Protein in Escherichia coli1 JULIANNE NAGEL AND ERNEST HIEBERT2 Plant Pathology Department, University of Florida, Gainesville, Florida S2G11 Received November 5, I9Si; accepted February 2, Three cDNA clones that express viral gene products in Escherichia coli Cited by: In order to begin the molecular characterization of these viruses, the nucleotide sequence of the capsid protein gene of two San Miguel sea lion viruses (SMSV), serotypes 1 and 4, was determined.

The coding sequences for the capsid precursor protein were located within the 3' terminal bases of the genomic RNAs of both by: By comparison to other sequenced potyviruses, it was estimated that the clone contained the 3' non-coding (3'-NC) region, the coat protein (CP) gene and the large nuclear inclusion protein.

The potyvirus 3' sequence amplification procedure is simple and rapid, is potentially useful in developing virus specific probes and may be used to differentiate strains and species of potyviruses on the basis ofthe 3' UTR by:   Cloning of the potato virus Y genes encoding the capsid protein CP and the nuclear inclusion protein NIb.

Summary. DNA was synthesized complementary to the RNA genome of potato virus Y (PVY; strain GO 16) and cloned into λ vectors. The size of PVY-specificEco RI-restricted cDNA ranged from to approximately by:   The nucleotide sequence of the RNA of tobacco vein mottling virus, a member of the potyvirus group, was determined.

The RNA was found to be residues in length, excluding a 3'-terminal poly(A) tail. The first three AUG codons from the 5'-terminus were followed by in-frame termination by: Small Nuclear Inclusion Protein Encoded by a Plant Potyvirus Genome Is a Protease. Department of Plant Pathology, North Carolina State University, Raleigh, North Carolina * Corresponding author.

† Present address: Department of Microbiology, Oregon State University, Corvallis, OR Cited by: Nagel J, Hiebert E () Complementary DNA cloning and expression of the papaya ringspot potyvirus sequences encoding capsid protein and a nuclear inclusion-like protein in Escherichia coli.

Virology –Cited by: 7. Sequence analysis of iris severe mosaic potyvirus genomic RNA revealed an unusual E/G cleavage site between the deduced large nuclear-inclusion protein and coat protein sequences.

The latter showed an N-terminus of only 15 amino acids. The 3′ non-translated region of the viral RNA was nucleotides by: 7. terminal portion ofthe capsid protein was determined and comparedtothe nucleotide inferred sequence. Additionally, the aminoacid compositionofthe capsidprotein wasdeter-mined.

Thesequenceof20aminoacids at the NH2terminus of TEVcapsid protein was identical to amino acids through(Figs. 2 and 4) predicted from the nucleotide sequence. No detailed studies have been carried out in India on capsid protein (CP) of extra small viral-like particles associated with MrNV causing WTD in freshwater prawn.

In order to characterize an Indian isolate of XSV, the gene encoding CP was cloned and its sequence compared with available pool of XSV gene sequences in the GenBank/EMBL Cited by: 5. Robaglia C, Durand-Tardif M, Tronchet M, Boudazin G, Astier-Manifacier S, Casse-Delbart F. Nucleotide sequence of potato virus Y (N Strain) genomic RNA.

J Gen Virol. Apr; 70 (Pt 4)– Wefels E, Sommer H, Salamini F, Rohde W. Cloning of the potato virus Y genes encoding the capsid protein CP and the nuclear inclusion protein by: A partial genetic map of these viruses has been established and cistrons have been assigned to. certain virus-encoded proteins; these are, from 5' to Y, the helper component (HC), the.

cytoplasmic inclusion protein (CI), the two nuclear inclusion proteins and the capsid protein. Nagel J, Hiebert E. Complementary DNA cloning and expression of the papaya ringspot potyvirus sequences encoding capsid protein and a nuclear inclusion-like protein in Escherichia coli.

Virology. Jun; (2)– predicted from the nucleotide sequence. These data sup-ported the hypothesis that the sequence coding for the capsid protein was proximal to the 3' terminus of the TEV genome (nucleotides through ) and would encode a protein with a molecular weight of 29, Codon Usage of the Capsid Protein Gene and the Amino Acid.

The kDa protein from the N-terminus of a potyviral polyprotein functions as a third virus-encoded proteinase. Virology () Wefels, E., Sommer, H., Salamini, F.

and Rohde, W.: Cloning of the potato virus Y genes encoding the capsid protein CP and the nuclear inclusion protein Nib. Arch. Virol. () Cited by: VIROLOGY() Nucleotide Sequence at the 3' Terminus of Pepper Mottle Virus Genomic RNA: Evidence for an Alternative Mode of Potyvirus Capsid Protein Gene Organization1 WILLIAM G.

DOUGHERTY,*-2 RICHARD F. ALLISON,* T. DAWN PARKS,+ ROBERT E. JOHNSTON, MARK J. FEILD,+ AND FRANK B.

ARMSTRONG:): Departments of Cited by: Transgenic tobacco plants expressing antisense RNA to the TMV capsid protein coding region and 3 0 -NTR showed resistance to infection only at low levels of virus inocula, while similar plants.

C) The technique does not work in sheep. D) The nuclear material from the egg would influence the clone. E) The clone would exhibit characteristics of the genetic donor, not the surrogate. The clone would not exhibit characteristics of the genetic donor, not the surrogate.

from the four known viral proteins; nuclear inclusion protein 1, nuclear inclusion protein 2, cytoplasmic inclusion protein, and capsid protein. The location of proteins in reference to each other was determined by immunoprecipitating overlapping proteins with two or more.

Robaglia C, Durand-Tardif M, Tronchet M, Boudazin G, Astier-Manifacier S, Casse-Delbart F. Nucleotide sequence of potato virus Y (N Strain) genomic RNA. J Gen Virol. Apr; 70 (Pt 4)– Wefels E, Sommer H, Salamini F, Rohde W. Cloning of the potato virus Y genes encoding the capsid protein CP and the nuclear inclusion protein NIb.

The sequence contained the Q‐G/S amino acid motif that is conserved among potyviruses. This motif was encoded by nucleotides – and thought to represent the cleavage site between the nuclear inclusion b and capsid proteins. The putative capsid protein was encoded by nucleotides – ( amino acids).Cited by: 8.

Since the protein was massively overexpressed under the T7 promoter (around 30% of total protein), overall purification was fold, and yield was 77% (Table 1). The identity of YhbO was confirmed by N-terminal sequencing and mass spectrometry. The N-terminal sequence found was SKKIAVLI, which is.

The nucleotide sequence of the WMVII cDNA clone shows the presence of the large nuclear inclusion protein gene, the coat protein gene and 3' untranslated region. The nucleotide sequence of a ZYMV-F cDNA clone shows the presence of the coat protein gene and 3' untranslated by:.

The assembly and regulation of viral capsid proteins into highly ordered macromolecular complexes is essential for viral replication. Here, we utilize crystal structures of the capsid protein from Cited by: Cloning and nucleotide sequence of the capsid protein and the nuclear inclusion protein (NIb) of potato virus A.

Archives of Virology Collmer CW, Marston MF, Albert SM, Bajaj S, Maville HA, Ruuska SE, Versely EJ and Kyle MM. The nucleotide sequence of the coat protein gene and 3’ untranslated.

Purification of recombinant budgerigar fledgling disease virus VP1 capsid protein and its ability for in vitro capsid assembly.

R E Rodgers, D Chang, X Cai, and R A Consigli Division of Biology, Kansas State University, Manhattan