Plant Transformation Vectors Having Street Rabies Virus (Indian Strain) Glycoprotein Gene

2005 ◽  
Vol 14 (2) ◽  
pp. 81-87 ◽  
Author(s):  
Sweta Agrawal ◽  
A. K. Shasany ◽  
S. P. S. Khanuja
Keyword(s):  
Rabies Virus ◽  
Plant Transformation ◽  
Glycoprotein Gene ◽  
Indian Strain ◽  
Transformation Vectors

scholarly journals A Recombinant Rabies Virus Encoding Two Copies of the Glycoprotein Gene Confers Protection in Dogs against a Virulent Challenge

PLoS ONE ◽  
2014 ◽  
Vol 9 (2) ◽  
pp. e87105 ◽  
Author(s):  
Xiaohui Liu ◽  
Youtian Yang ◽  
Zhaojin Sun ◽  
Jing Chen ◽  
Jun Ai ◽  
...  
Keyword(s):  
Rabies Virus ◽  
Glycoprotein Gene ◽  
Virulent Challenge

Molecular genetic characterization of rabies virus glycoprotein gene sequences from rabid dogs in Bangkok and neighboring provinces in Thailand, 2013–2014

2016 ◽  
Vol 161 (5) ◽  
pp. 1261-1271 ◽  
Author(s):  
Surachet Benjathummarak ◽  
Chanon Fa-ngoen ◽  
Chonlatip Pipattanaboon ◽  
Khwanchit Boonha ◽  
Pongrama Ramasoota ◽  
...  
Keyword(s):  
Rabies Virus ◽  
Genetic Characterization ◽  
Molecular Genetic ◽  
Gene Sequences ◽  
Rabies Virus Glycoprotein ◽  
Virus Glycoprotein ◽  
Glycoprotein Gene ◽  
Molecular Genetic Characterization

scholarly journals Zinc Finger Nuclease and Homing Endonuclease-Mediated Assembly of Multigene Plant Transformation Vectors

2011 ◽  
Vol 158 (1) ◽  
pp. 132-144 ◽  
Author(s):  
Vardit Zeevi ◽  
Zhuobin Liang ◽  
Uri Arieli ◽  
Tzvi Tzfira
Keyword(s):  
Zinc Finger ◽  
Plant Transformation ◽  
Homing Endonuclease ◽  
Zinc Finger Nuclease ◽  
Transformation Vectors

Structure and transcription of the glycoprotein gene of attenuated HEP-Flury strain of rabies virus

Virology ◽  
1989 ◽  
Vol 173 (2) ◽  
pp. 465-477 ◽  
Author(s):  
Kinjiro Morimoto ◽  
Akemi Ohkubo ◽  
Akihiko Kawai
Keyword(s):  
Rabies Virus ◽  
Glycoprotein Gene

scholarly journals Protection from rabies by a vaccinia virus recombinant containing the rabies virus glycoprotein gene.

1984 ◽  
Vol 81 (22) ◽  
pp. 7194-7198 ◽  
Author(s):  
T. J. Wiktor ◽  
R. I. Macfarlan ◽  
K. J. Reagan ◽  
B. Dietzschold ◽  
P. J. Curtis ◽  
...  
Keyword(s):  
Vaccinia Virus ◽  
Rabies Virus ◽  
Rabies Virus Glycoprotein ◽  
Virus Glycoprotein ◽  
Glycoprotein Gene ◽  
Virus Recombinant ◽  
Vaccinia Virus Recombinant

Transposable elements as plant transformation vectors for long stretches of foreign DNA

1995 ◽  
Vol 91-91 (6-7) ◽  
pp. 899-906 ◽  
Author(s):  
E. G. Lebel ◽  
J. Masson ◽  
A. Bogucki ◽  
J. Paszkowski
Keyword(s):  
Transposable Elements ◽  
Plant Transformation ◽  
Foreign Dna ◽  
Transformation Vectors

scholarly journals Mutations Conferring Resistance to Neutralization by a Soluble Form of the Neurotrophin Receptor (p75NTR) Map outside of the Known Antigenic Sites of the Rabies Virus Glycoprotein

2002 ◽  
Vol 76 (21) ◽  
pp. 10756-10765 ◽  
Author(s):  
Christelle Langevin ◽  
Christine Tuffereau
Keyword(s):  
Rabies Virus ◽  
Protein A ◽  
Neurotrophin Receptor ◽  
Soluble Form ◽  
Single Mutation ◽  
Soluble Receptor ◽  
Fc Fragment ◽  
Glycoprotein Gene ◽  
Antigenic Sites ◽  
Resistant Mutants

ABSTRACT The neurotrophin receptor (p75NTR) serves as a receptor for rabies virus (RV). We expressed and purified a soluble chimera consisting of the p75NTR ectodomain fused to the human immunoglobulin G1 (IgG1) Fc fragment (p75-Fc). Although p75-Fc interacts with RV, the infectivity of RV did not decrease significantly when it was incubated in the presence of the soluble receptor alone. However, when it was subsequently incubated with an antihuman IgG directed against the Fc fragment of p75-Fc, the infectivity of RV was significantly lowered (>90%), whereas incubation with antihuman IgG alone had no effect. We then selected eight independent RV mutants that were not neutralized by p75-Fc and antihuman IgG (srr [soluble receptor resistant] mutants). Each mutant carried a single mutation in the glycoprotein gene leading to one amino acid substitution in the protein. A total of four different substitutions were found. Two of the mutations were located at position 318 (phenylalanine replaced by a serine or a valine residue), and two were located at position 352 (histidine replaced by a tyrosine or an arginine residue). All of the mutations prevented the interaction with p75NTR as either a soluble or a membrane-anchored form. Two mutants (F318S) and (H352R) resulted in the formation of small plaques on BSR cells, probably due to the slower maturation of the glycoprotein. Immunoprecipitation, immunofluorescence, and neutralization assays showed that the four mutated glycoproteins still interacted with representative anti-RV glycoprotein monoclonal antibodies (MAbs), indicating that p75NTR binds outside of the known RV glycoprotein antigenic sites.

scholarly journals Rescue of Rabies Virus from Cloned cDNA and Identification of the Pathogenicity-Related Gene: Glycoprotein Gene Is Associated with Virulence for Adult Mice

2001 ◽  
Vol 75 (19) ◽  
pp. 9121-9128 ◽  
Author(s):  
Naoto Ito ◽  
Mutsuyo Takayama ◽  
Kentaro Yamada ◽  
Makoto Sugiyama ◽  
Nobuyuki Minamoto
Keyword(s):  
Rabies Virus ◽  
Reverse Genetics ◽  
Biological Properties ◽  
Open Reading Frame ◽  
Chimeric Virus ◽  
Viral Gene ◽  
Reading Frame ◽  
Intracerebral Inoculation ◽  
Glycoprotein Gene ◽  
Adult Mice

ABSTRACT In order to identify the viral gene related to the pathogenicity of rabies virus, we tried to establish a reverse genetics system of the attenuated RC-HL strain, which causes nonlethal infection in adult mice after intracerebral inoculation. A full-length genome plasmid encoding the complete antigenomic cDNA of the RC-HL strain and helper plasmids containing cDNAs of the complete open reading frame of the N, P, and L genes, respectively, were constructed. After transfection of these plasmids into BHK-21 cells infected with the T7 RNA polymerase-expressing vaccinia virus, infectious rabies virus with almost the same biological properties as those of the wild-type RC-HL strain was rescued. Using this reverse genetics system of the RC-HL strain, we generated a chimeric virus with the open reading frame of the glycoprotein gene from the parent Nishigahara strain, which kills adult mice after intracerebral inoculation, in the background of the RC-HL genome. Since the chimeric virus killed adult mice following intracerebral inoculation, it became evident that the open reading frame of the glycoprotein gene is related to the pathogenicity of the Nishigahara strain for adult mice.

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