Analysis of a translational enhancer upstream from the coat protein open reading frame of potato virus S

1994 ◽  
Vol 134 (3-4) ◽  
pp. 321-333 ◽  
Author(s):  
R. Turner ◽  
N. Bate ◽  
D. Twell ◽  
G. D. Foster
Keyword(s):  
Coat Protein ◽  
Potato Virus ◽  
Open Reading Frame ◽  
Potato Virus S ◽  
Reading Frame ◽  
Translational Enhancer

scholarly journals Analysis of the nucleotide sequence of the coat protein and 3'-untranslated region of two Brazilian Potato virus Y isolates

2001 ◽  
Vol 26 (1) ◽  
pp. 45-52 ◽  
Author(s):  
ALICE K. INOUE-NAGATA ◽  
M. ESTHER N. FONSECA ◽  
TATIANA O.T.A. LOBO ◽  
ANTÔNIO C. DE ÁVILA ◽  
DAMARES C. MONTE
Keyword(s):  
Coat Protein ◽  
Potato Virus ◽  
Viral Genome ◽  
Untranslated Region ◽  
Phylogenetic Trees ◽  
Potato Virus Y ◽  
Reading Frame ◽  
Common Group ◽  
The Common ◽  
Test Plants

Two Brazilian Potato virus Y (PVY) isolates were biologically characterized as necrotic (PVY-NBR) and common (PVY-OBR) based upon symptoms on test plants. Additional characterization was performed by sequencing a cDNA corresponding to the 3' terminal region of the viral genome. The sequence consisted of 195 nucleotides (nt) coding part of the nuclear inclusion body b (NIb) gene, 804 nt of the coat protein (CP) gene, and 328 nt (PVY-OBR) or 326 nt (PVY-NBR) of the 3'-untranslated region (UTR). Translation of the sequence resulted in one single open reading frame with part of the NIb and a CP of 267 amino acids. The two isolates shared 95.1% similarity in the CP amino acid sequence. The CP and the 3'-UTR sequence of the Brazilian isolates were compared to those of other PVY isolates previously reported and unrooted phylogenetic trees were constructed. The trees revealed a separation of two distinct clusters, one comprising most of the common strains and the other comprising the necrotic strains. PVY-OBR was clustered in the common group and PVY-NBR in the necrotic one.

Molecular cloning and sequencing of the capsid and the nuclear inclusion protein genes of a North American PVYN isolate

1994 ◽  
Vol 40 (9) ◽  
pp. 798-804 ◽  
Author(s):  
A. K. Dhar ◽  
R. P. Singh ◽  
A. Boucher
Keyword(s):  
Potato Virus ◽  
Potato Virus Y ◽  
Open Reading Frame ◽  
Start Codon ◽  
Cleavage Sites ◽  
Amino Acid Residues ◽  
Nuclear Inclusion ◽  
Reading Frame ◽  
Inclusion Protein ◽  
Nontranslated Region

The sequence of the 3′-terminal 3258 nucleotides of a tobacco veinal necrosis strain of a potato virus Y (PVYN) isolate from North America was determined. The sequence revealed an open reading frame of 2931 nucleotides, of which the start codon was not identified. The nontranslated region contains 327 nucleotides upstream of a poly(A) tract. The open reading frame encodes a large polyprotein containing 976 amino acids. The data indicate that the coat protein (CP) and the nuclear inclusion protein (NIb) are derived from the large polypeptide by proteolytic cleavage similar to many other potyviruses. The putative cleavage sites of NIa/NIb and NIb/CP correspond to Q/A and Q/G sequences, respectively, as in other PVYN isolates. The CP and NIb contain 267 and 519 amino acid residues, respectively. Higher sequence homology of CP was observed with other PVYN isolates than with the PVYO isolates.Key words: potato virus Y, nucleotide sequence.

scholarly journals pIIICTX, a Predicted CTXφ Minor Coat Protein, Can Expand the Host Range of Coliphage fd To Include Vibrio cholerae

2003 ◽  
Vol 185 (3) ◽  
pp. 1037-1044 ◽  
Author(s):  
Andrew J. Heilpern ◽  
Matthew K. Waldor
Keyword(s):  
Coat Protein ◽  
Vibrio Cholerae ◽  
Protein Sequences ◽  
Open Reading Frame ◽  
Filamentous Phage ◽  
Host Bacterium ◽  
Reading Frame ◽  
New Evidence ◽  
Minor Coat Protein

ABSTRACT CTXφ is a filamentous bacteriophage that encodes cholera toxin. CTXφ infection of its host bacterium, Vibrio cholerae, requires the toxin-coregulated pilus (TCP) and the products of the V. cholerae tolQRA genes. Here, we have explored the role of OrfU, a predicted CTXφ minor coat protein, in CTXφ infection. Prior to the discovery that it was part of a prophage, orfU was initially described as an open reading frame of unknown function that lacked similarity to known protein sequences. Based on its size and position in the CTXφ genome, we hypothesized that OrfU may function in a manner similar to that of the coliphage fd protein pIII and mediate CTXφ infection as well as playing a role in CTXφ assembly and release. Deletion of orfU from CTXφ dramatically reduced the number of CTXφ virions detected in supernatants from CTXφ-bearing cells. This defect was complemented by expression of orfU in trans, thereby confirming a role for this gene in CTXφ assembly and/or release. To evaluate the requirement for OrfU in CTXφ infection, we introduced fragments of orfU into gIII in an fd derivative to create OrfU-pIII fusions. While fd is ordinarily unable to infect V. cholerae, an fd phage displaying the N-terminal 274 amino acids of OrfU could infect V. cholerae in a TCP- and TolA-dependent fashion. Since our findings indicate that OrfU functions as the CTXφ pIII, we propose to rename OrfU as pIIICTX. Our data also provide new evidence for a conserved pathway for filamentous phage infection.

scholarly journals Interaction between the Open Reading Frame III Product and the Coat Protein Is Required for Transmission of Cauliflower Mosaic Virus by Aphids

2001 ◽  
Vol 75 (1) ◽  
pp. 100-106 ◽  
Author(s):  
Véronique Leh ◽  
Emmanuel Jacquot ◽  
Angèle Geldreich ◽  
Muriel Haas ◽  
Stéphane Blanc ◽  
...  
Keyword(s):  
Coat Protein ◽  
Mosaic Virus ◽  
Direct Interaction ◽  
Cauliflower Mosaic Virus ◽  
Open Reading Frame ◽  
Nonstructural Proteins ◽  
Interaction Domain ◽  
Reading Frame ◽  
Virus Particles ◽  
Terminal Domain

ABSTRACT Transmission of cauliflower mosaic virus (CaMV) by aphids requires two viral nonstructural proteins, the open reading frame (ORF) II and ORF III products (P2 and P3). An interaction between a C-terminal domain of P2 and an N-terminal domain of P3 is essential for transmission. Purified particles of CaMV are efficiently transmitted only if aphids, previously fed a P2-containing solution, are allowed to acquire a preincubated mixture of P3 and virions in a second feed, thus suggesting a direct interaction between P3 and coat protein. Herein we demonstrate that P3 directly interacts with purified viral particles and unassembled coat protein without the need for any other factor and that P3 mediates the association of P2 with purified virus particles. The interaction domain of P3 is located in its C-terminal half, downstream of the P3-P2 interaction domain but overlapping a region which binds nucleic acids. Mutagenesis of P3 which interferes with the interaction between P3 and virions is correlated with the loss of transmission by aphids. Taken together, our results demonstrate that P3 plays a crucial role in the formation of the CaMV transmissible complex by serving as a bridge between P2 and virus particles.

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