Differentiation of Allium carlaviruses isolated from different parts of the world based on the viral coat protein sequence

1998 ◽  
Vol 143 (6) ◽  
pp. 1093-1107 ◽  
Author(s):  
T. Tsuneyoshi ◽  
T. Matsumi ◽  
T. C. Deng ◽  
I. Sako ◽  
S. Sumi
Keyword(s):  
Coat Protein ◽  
Protein Sequence ◽  
Coat Protein Sequence ◽  
Viral Coat Protein ◽  
The World ◽  
Viral Coat ◽  
Different Parts

scholarly journals Preliminary molecular characterization of some Citrus tristeza Closterovirus isolates infecting Croatian citrus

2017 ◽  
Vol 38 (SI 2 - 6th Conf EFPP 2002) ◽  
pp. 264-266
Author(s):  
S. Černi ◽  
D. Škorić ◽  
M. Krajačić
Keyword(s):  
Coat Protein ◽  
Protein Sequence ◽  
Coastal Region ◽  
Coat Protein Sequence ◽  
Rt Pcr ◽  
Double Stranded Rna ◽  
The World ◽  
Citrus Tristeza Closterovirus ◽  
Citrus Tristeza

Citrus tristeza Closterovirus (CTV) is widespread in major citrus-growing regions of the world often causing destructive diseases. Citrus samples were taken from orchards in the Croatian coastal region. CTV was detected in two symptomless field trees of Satsuma mandarins and one diseased lemon tree. Double-stranded RNA was isolated from the field trees and the dsRNA patterns were compared in polyacrylamide gels. The same dsRNA extracts were used as templates in RT-PCR experiments amplifying the CTV coat protein sequence. Amplicons were subjected to SSCP and RFLP analyses. The results indicate greater similarity between CTV isolates from Satsuma mandarins than between these two and the lemon isolate.

Banana bunchy top virus DNA-3encodes the viral coat protein

1997 ◽  
Vol 142 (8) ◽  
pp. 1673-1680 ◽  
Author(s):  
R. Wanitchakorn ◽  
R. M. Harding ◽  
J. L. Dale
Keyword(s):  
Coat Protein ◽  
Viral Coat Protein ◽  
Banana Bunchy Top Virus ◽  
Viral Coat

Purification of a viral coat protein by an engineered polyionic sequence

2000 ◽  
Vol 737 (1-2) ◽  
pp. 77-84 ◽  
Author(s):  
K Stubenrauch ◽  
A Bachmann ◽  
R Rudolph ◽  
H Lilie
Keyword(s):  
Coat Protein ◽  
Viral Coat Protein ◽  
Viral Coat

Liquid crystal properties of a self-assembling viral coat protein

2011 ◽  
Vol 38 (9) ◽  
pp. 1153-1157
Author(s):  
S.E. Fiester ◽  
A. Jákli ◽  
C.J. Woolverton
Keyword(s):  
Liquid Crystal ◽  
Coat Protein ◽  
Viral Coat Protein ◽  
Self Assembling ◽  
Crystal Properties ◽  
Viral Coat

scholarly journals Molecular Characterization of a Bacteriophage (Chp2) from Chlamydia psittaci

2000 ◽  
Vol 74 (8) ◽  
pp. 3464-3469 ◽  
Author(s):  
B. L. Liu ◽  
J. S. Everson ◽  
B. Fane ◽  
P. Giannikopoulou ◽  
E. Vretou ◽  
...  
Keyword(s):  
Sequence Analysis ◽  
Coat Protein ◽  
Spatial Location ◽  
Chlamydia Psittaci ◽  
Peptide Sequence ◽  
Structural Protein ◽  
Two Dimensional Gel Electrophoresis ◽  
Viral Coat Protein ◽  
Thin Sections ◽  
Viral Coat

ABSTRACT Comparisons of the proteome of abortifacient Chlamydia psittaci isolates from sheep by two-dimensional gel electrophoresis identified a novel abundant protein with a molecular mass of 61.4 kDa and an isoelectric point of 6.41. C-terminal sequence analysis of this protein yielded a short peptide sequence that had an identical match to the viral coat protein (VP1) of the avian chlamydiaphage Chp1. Electron microscope studies revealed the presence of a 25-nm-diameter bacteriophage (Chp2) with no apparent spike structures. Thin sections of chlamydia-infected cells showed that Chp2 particles were located to membranous structures surrounding reticulate bodies (RBs), suggesting that Chp2 is cytopathic for ovine C. psittaci RBs. Chp2 double-stranded circular replicative-form DNA was purified and used as a template for DNA sequence analysis. The Chp2 genome is 4,567 bp and encodes up to eight open reading frames (ORFs); it is similar in overall organization to the Chp1 genome. Seven of the ORFs (1 to 5, 7, and 8) have sequence homologies with Chp1. However, ORF 6 has a different spatial location and no cognate partner within the Chp1 genome. Chlamydiaphages have three viral structural proteins, VP1, VP2, and VP3, encoded by ORFs 1 to 3, respectively. Amino acid residues in the φX174 procapsid known to mediate interactions between the viral coat protein and internal scaffolding proteins are conserved in the Chp2 VP1 and VP3 proteins. We suggest that VP3 performs a scaffolding-like function but has evolved into a structural protein.

scholarly journals Translation of a nonpolyadenylated viral RNA is enhanced by binding of viral coat protein or polyadenylation of the RNA

2001 ◽  
Vol 98 (25) ◽  
pp. 14286-14291 ◽  
Author(s):  
L. Neeleman ◽  
R. C. L. Olsthoorn ◽  
H. J. M. Linthorst ◽  
J. F. Bol
Keyword(s):  
Coat Protein ◽  
Viral Rna ◽  
Viral Coat Protein ◽  
Viral Coat
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