Non-AUG Translation Initiation in a Plant RNA Virus: a Forty-Amino-Acid Extension Is Added to the N Terminus of the Soil-Borne Wheat Mosaic Virus Capsid Protein

ABSTRACT RNA 2 of soil-borne wheat mosaic virus (SBWMV), the type species of the genus Furovirus, encodes a protein previously hypothesized to be initiated at an in-frame non-AUG codon upstream of the AUG initiation codon (nucleotide positions 334 to 336) for the 19-kDa capsid protein. Site-directed mutagenesis and in vitro transcription and translation analysis indicated that CUG (nucleotides 214 to 216) is the initiation codon for a protein with a calculated molecular mass of 25 kDa composed of a 40-amino-acid extension to the N terminus of the 19-kDa capsid protein. A stable deletion mutant, which was isolated after extensive passages of a wild-type SBWMV, contained a mixture of two deleted RNA 2’s, only one of which coded for the 25-kDa protein. The amino acid sequence of the N-terminal extension was moderately conserved and the CUG initiation codon was preserved among three SBWMV isolates from Japan and the United States. This amino acid sequence conservation, as well as the retention of expression of the 25-kDa protein in the stable deletion mutant, suggests that the 25-kDa protein is functional in the life cycle of SBWMV. This is the first report of a non-AUG translation initiation in a plant RNA virus genome.

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Host Range and Characterization of Sunflower mosaic virus

Phytopathology ◽

10.1094/phyto.2002.92.7.694 ◽

2002 ◽

Vol 92 (7) ◽

pp. 694-702 ◽

Cited By ~ 18

Author(s):

T. J. Gulya ◽

P. J. Shiel ◽

T. Freeman ◽

R. L. Jordan ◽

T. Isakeit ◽

...

Keyword(s):

Amino Acid ◽

Coat Protein ◽

Amino Acid Sequence ◽

Host Range ◽

Mosaic Virus ◽

Cytoplasmic Inclusion ◽

The United States ◽

Enzyme Linked Immunosorbent Assay ◽

Protein Amino Acid ◽

The Family

Sunflower mosaic is caused by a putative member of the family Potyviridae. Sunflower mosaic virus (SuMV) was characterized in terms of host range, physical and biological characteristics, and partial nucleotide and amino acid sequence. Cells infected with SuMV had cytoplasmic inclusion bodies typical of potyviruses. Of 74 genera tested, only species in Helianthus, Sanvitalia, and Zinnia, all Asteraceae, were systemic hosts. Commercial sunflower hybrids from the United States, Europe, and South Africa were all equally susceptible. The mean length of purified particles is approximately 723 nm. The virus was transmitted by Myzus persicae and Capitphorus elaegni, and also was seedborne in at least one sunflower cultivar. Indirect enzyme-linked immunosorbent assay tests with a broad-spectrum potyvirus monoclonal antibody were strongly positive. SuMV-specific polyclonal antisera recognized SuMV and, to a lesser extent, Tobacco etch virus (TEV). When tested against a panel of 31 potyvirus-differentiating monoclonal antibodies, SuMV was distinct from any potyvirus previously tested. SuMV shared four epitopes with TEV, but had a reaction profile more similar to Tulip breaking virus (TBV). SuMV did not possess epitopes unique only to TBV. The predicted coat protein had a molecular weight of 30.5 kDa. The 3′ end of the virus genome was cloned and sequenced. Phylogenetic analysis of the coat protein amino acid sequence revealed that SuMV is a distinct species within the family Potyviridae, most closely related to TEV.

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Peptide vaccine against canine parvovirus: identification of two neutralization subsites in the N terminus of VP2 and optimization of the amino acid sequence.

Journal of Virology ◽

10.1128/jvi.69.11.7274-7277.1995 ◽

1995 ◽

Vol 69 (11) ◽

pp. 7274-7277 ◽

Cited By ~ 34

Author(s):

J I Casal ◽

J P Langeveld ◽

E Cortés ◽

W W Schaaper ◽

E van Dijk ◽

...

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Peptide Vaccine ◽

Canine Parvovirus ◽

N Terminus

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Association of the brain anion exchanger, AE3, with the repeat domain of ankyrin

Journal of Cell Science ◽

10.1242/jcs.105.4.1137 ◽

1993 ◽

Vol 105 (4) ◽

pp. 1137-1142 ◽

Cited By ~ 2

Author(s):

C.W. Morgans ◽

R.R. Kopito

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Anion Exchanger ◽

Deletion Mutant ◽

Tandem Repeats ◽

Structural Homology ◽

Terminal Domain ◽

Repeat Domain ◽

The Brain

The 89 kDa NH2-terminal domain of erythrocyte ankyrin is composed almost entirely of 22 tandem repeats of a 33 amino acid sequence and constitutes the binding site for the cytoplasmic NH2-terminal domain of the erythrocyte anion exchanger, AE1. We have developed an assay to evaluate the in vivo interaction between a fragment of ankyrin corresponding to this domain (ANK90) and two non-erythroid anion exchangers, AE2 and AE3, that share considerable structural homology with AE1. Association was assessed by co-immunoprecipitation of ANK90-anion exchanger complexes from detergent extracts of cells cotransfected with plasmids encoding the ankyrin fragment and the anion exchanger or mutants thereof. ANK90 was co-immunoprecipitated with AE1 but not with an AE1 deletion mutant lacking the cytoplasmic NH2-terminal domain. Using this assay, we show that the brain anion exchanger AE3, but not the closely related homologue, AE2, is capable of binding to ankyrin.

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Die primäre Proteinstruktur von Stämmen des Tabakmosaikvirus

Zeitschrift für Naturforschung B ◽

10.1515/znb-1963-1207 ◽

1963 ◽

Vol 18 (12) ◽

pp. 1032-1049 ◽

Cited By ~ 13

Author(s):

B. Wittmann-Liebold ◽

H. G. Wittmann

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Amino Acid Sequence ◽

Tobacco Mosaic Virus ◽

Mosaic Virus ◽

Amino Acid Sequences ◽

Tryptic Peptides

The amino acid sequence of dahlemense, a naturally occuring strain of tobacco mosaic virus, has been determined and compared with that of the strain vulgare (Fig. 7). In this communication the experimental details are given for the elucidation of the amino acid sequences within two tryptic peptides with 65 amino acids.

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The amino acid sequence of S-antigen: N-terminus and uveitogenic peptides

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology ◽

10.1016/0167-4838(89)90160-x ◽

1989 ◽

Vol 994 (2) ◽

pp. 191-193 ◽

Cited By ~ 2

Author(s):

Susumu Tsunasawa ◽

Hitoshi Shichi

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

N Terminus

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Novel N-terminal amino acid sequence required for retention of a hepatitis B virus glycoprotein in the endoplasmic reticulum

Molecular and Cellular Biology ◽

10.1128/mcb.9.10.4459-4466.1989 ◽

1989 ◽

Vol 9 (10) ◽

pp. 4459-4466 ◽

Cited By ~ 3

Author(s):

K Kuroki ◽

R Russnak ◽

D Ganem

Keyword(s):

Endoplasmic Reticulum ◽

Amino Acid ◽

Hepatitis B Virus ◽

Hepatitis B ◽

Amino Acid Sequence ◽

Essential Element ◽

Viral Gene ◽

Er Retention ◽

B Virus ◽

N Terminus

The preS1 surface glycoprotein of hepatitis B virus is targeted to the endoplasmic reticulum (ER) and is retained in this organelle when expressed in the absence of other viral gene products. The protein is also acylated at its N terminus with myristic acid. Sequences responsible for its ER retention have been identified through examination of mutants bearing lesions in the preS1 coding region. These studies reveal that such sequences map to the N terminus of the molecule, between residues 6 and 19. Molecules in which this region was present remained in the ER; those in which it had been deleted were secreted from the cell. Although all deletions which allowed efficient secretion also impaired acylation of the polypeptide, myristylation alone was not sufficient for ER retention: point mutations which eliminated myristylation did not lead to secretion. These data indicate that an essential element for ER retention resides in a 14-amino-acid sequence that is unrelated to previously described ER retention signals.

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