Narcissus mosaic virus: a potexvirus with an encapsidated subgenomic messenger RNA for coat protein

1983 ◽  
Vol 3 (9) ◽  
pp. 837-846 ◽  
Author(s):  
Margaret N. Short ◽  
Jeffrey W. Davies
Keyword(s):  
Coat Protein ◽  
Mosaic Virus ◽  
Small Rna ◽  
Gel Electrophoresis ◽  
Messenger Rna ◽  
Wheat Germ ◽  
Polyacrylamide Gel Electrophoresis ◽  
Subgenomic Rna ◽  
Virus Rna ◽  
Narcissus Mosaic Virus

Narcissus-mosaic-virus RNA is translated into a coat-protein-sized product in wheat-germ cell-free extracts. This protein was shown to be very similar to authentic coat protein by partial proteolysis in SDS/polyacrylamide-gel electrophoresis, and by serology. Fractionation of the RNA revealed a small RNA molecule of approx. 840 nucleotides, which alone coded for the coat protein. This subgenomic RNA was found to be encapsidated in a short virus particle.

An encapsidated, subgenomic messenger RNA encodes the coat protein of carnation mottle virus

1984 ◽  
Vol 4 (11) ◽  
pp. 949-956 ◽  
Author(s):  
Sally-Ann Harbison ◽  
T. Michael A. Wilson ◽  
Jeffrey W. Davies
Keyword(s):  
Coat Protein ◽  
Gel Electrophoresis ◽  
Messenger Rna ◽  
Polyacrylamide Gel Electrophoresis ◽  
Mottle Virus ◽  
Free System ◽  
Translation Strategy ◽  
Internal Initiation ◽  
Carnation Mottle Virus

The translation strategy of carnation mottle virus (CarMV) in vitro has been generally assumed to involve internal initiation events on full-length, genomic RNA (4.3 kb). We suggest that this is, at least in part, incorrect. Encapsidated RNA, fractionated on denaturing sucrose gradients, or total RNA from CarMV-infected leaves, fractionated under non-denaturing conditions, was translated in an mRNA-dependent rabbit reticulocyte cell-free system. Evidence for subgenomic RNAs which encode a polypeptide of Mr 38 000 was found. This product was shown to be related to authentic CarMV coat protein by partial proteolysis with α-chymotrypsin and SDS/polyacrylamide-gel electrophoresis.

scholarly journals Specific glycoprotein changes during development of the chick neural retina.

1978 ◽  
Vol 79 (1) ◽  
pp. 132-137 ◽  
Author(s):  
G Mintz ◽  
L Glaser
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Neural Retina ◽  
Cell Type ◽  
Retinal Antigens ◽  
Qualitative Changes

After separation of whole proteins of chick neural retina by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate (SDS), a number of glycoproteins can be detected by staining the gels with 125I-labeled wheat germ agglutinin (WGA) and other lectins. The glycoprotein patterns show both quantitative and qualitative changes between days 7 and 13 of development. Some of these glycoproteins can be separated by chromatography on columns of insolubilized lectins. These observations suggest that purification of some of these glycoproteins identified by staining with radioactive lectins would yield retinal antigens which may be specific for developmental stage and cell type.

Translation of eggplant mosaic virus RNA in wheat germ extracts and reticulocyte lysates

Virology ◽  
1978 ◽  
Vol 91 (2) ◽  
pp. 305-311 ◽  
Author(s):  
Bérénice Ricard ◽  
Hélène Renaudin ◽  
Joseph-marie Bové
Keyword(s):  
Mosaic Virus ◽  
Wheat Germ ◽  
Virus Rna ◽  
Reticulocyte Lysates ◽  
Wheat Germ Extracts

Sequence diversity in the coat protein and 3?-untranslated region of Chinese yam necrotic mosaic virus RNA

2003 ◽  
Vol 69 (6) ◽  
pp. 397-399 ◽  
Author(s):  
Toru Kondo ◽  
Dong-Kyoon Kang ◽  
Shin-ichi Fuji ◽  
Moo-Ung Chang
Keyword(s):  
Coat Protein ◽  
Mosaic Virus ◽  
Untranslated Region ◽  
Sequence Diversity ◽  
Chinese Yam ◽  
Virus Rna

scholarly journals Cis-Preferential Stimulation of Alfalfa Mosaic Virus RNA 3 Accumulation by the Viral Coat Protein

Virology ◽  
1996 ◽  
Vol 220 (1) ◽  
pp. 163-170 ◽  
Author(s):  
E.A.G. van der VOSSEN ◽  
C.B.E.M. REUSKEN ◽  
J.F. BOL
Keyword(s):  
Coat Protein ◽  
Mosaic Virus ◽  
Alfalfa Mosaic Virus ◽  
Viral Coat Protein ◽  
Virus Rna ◽  
Viral Coat ◽  
Stimulation Of

scholarly journals Solution structures of potato virus X and narcissus mosaic virus from Raman optical activity

2002 ◽  
Vol 83 (1) ◽  
pp. 241-246 ◽  
Author(s):  
Ewan W. Blanch ◽  
David J. Robinson ◽  
Lutz Hecht ◽  
Christopher D. Syme ◽  
Kurt Nielsen ◽  
...  
Keyword(s):  
Coat Protein ◽  
Mosaic Virus ◽  
Optical Activity ◽  
Potato Virus ◽  
Potato Virus X ◽  
Protein Subunit ◽  
Helix Bundle ◽  
Raman Optical Activity ◽  
Α Helix ◽  
Narcissus Mosaic Virus

Potato virus X (PVX) and narcissus mosaic virus (NMV) were studied using vibrational Raman optical activity (ROA) in order to obtain new information on the structures of their coat protein subunits. The ROA spectra of the two intact virions are very similar to each other and similar to that of tobacco mosaic virus (TMV) studied previously, being dominated by signals characteristic of proteins with helix bundle folds. In particular, PVX and NMV show strong positive ROA bands at ∼1340 cm−1 assigned to hydrated α-helix and perhaps originating in surface exposed helical residues, together with less strong positive ROA intensity in the range ∼1297–1312 cm−1 assigned to α-helix in a more hydrophobic environment and perhaps originating in residues at helix–helix interfaces. The positive ∼1340 cm−1 ROA band of TMV is less intense than those of PVX and NMV, suggesting that TMV contains less hydrated α-helix. Small differences in other spectral regions reflect differences in some loop, turn and side-chain compositions and conformations among the three viruses. A pattern recognition program based on principal component analysis of ROA spectra indicates that the coat protein subunit folds of PVX and NMV may be very similar to each other and similar to that of TMV. These results suggest that PVX and NMV may have coat protein subunit structures based on folds similar to the TMV helix bundle and hence that the helical architecture of the PVX and NMV particles may be similar to that of TMV but with different structural parameters.

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