Virus-Derived ssDNA Vectors for the Expression of Foreign Proteins in Plants

2011 ◽  
pp. 19-45 ◽  
Author(s):  
Edward P. Rybicki ◽  
Darrin P. Martin
Keyword(s):  
Foreign Proteins

Enhancing Expression and Accumulation of Foreign Proteins by Using the Signal Peptide of GlutelinGluA-2in Endosperm of Transgenic Rice

2015 ◽  
Vol 41 (4) ◽  
pp. 524
Author(s):  
Hong-Mei WANG ◽  
Chang-Quan ZHANG ◽  
Qian-Feng LI ◽  
Samuel Sing-Min SUN ◽  
Qiao-Quan LIU ◽  
...  
Keyword(s):  
Transgenic Rice ◽  
Signal Peptide ◽  
Foreign Proteins

scholarly journals The passage of antibodies from the maternal circulation into the embryo in rabbits

1948 ◽  
Vol 135 (880) ◽  
pp. 390-403 ◽  
Keyword(s):  
High Titre ◽  
Immune Serum ◽  
Maternal Serum ◽  
Yolk Sac ◽  
Passive Immunity ◽  
Maternal Circulation ◽  
Active Immunity ◽  
Foreign Proteins ◽  
Positive Results ◽  
Rabbit Embryos

Active immunity to Brucella abortus was induced in adult female rabbits. They were mated a week after the last injection of antigen and were killed and the yolk-sac contents of the embryos tested for agglutinins 8½ days after copulation. Specific agglutinins were found to be present in the yolk-sac contents in all cases. The titre varied significantly from embryo to embryo in the same litter, and was in some as high as that in the maternal serum at the time of killing. Passive immunity to Br. abortus was imparted to female rabbits 7 to 9 days pregnant by intravenous injection of immune serum of high titre. The rabbits were killed and the yolk-sac fluid of the embryos tested for agglutinins 10 to 17 hr. after injection. Specific agglutinins were present in most of the embryos from five of the six rabbits injected before 8 days post-coitum. All the embryos in the sixth rabbit were regressing. Specific agglutinins were not found in any of the embryos from two rabbits injected after 9 days post-coitum, by which time the yolk-sac fluid has ceased to increase in volume. Positive results were obtained both when rabbit and bovine immune sera were used. Active immunity to Br. abortus was induced in pregnant rabbits by injections beginning after the 15th day post-coitum. The serum of the newborn young, removed from their immune mothers before they had suckled, was tested and specific agglutinins were found to be present with a titre corresponding to that of the maternal serum. It was concluded that agglutinins, whether actively or passively acquired, pass freely from the maternal circulation into the yolk-sacs of 7- and 8-day rabbit embryos. This constitutes a delicate test of the passage of protein without alteration through the yolk-sac wall. The yolk-sac wall does not appear to be selective, since it is at least as permeable to foreign proteins as it is to those of maternal origin. Agglutinins pass from the maternal circulation into the embryo after the disappearance of the bilaminar wall of the yolk-sac also, either by way of the yolk-sac splanchnopleur or the allantochorionic placenta or both. The bearing of these results on current theories of placental permeability are discussed.

scholarly journals Improving Baculovirus Infectivity by Efficiently Embedding Enhancing Factors into Occlusion Bodies

2017 ◽  
Vol 83 (14) ◽  
Author(s):  
Shili Yang ◽  
Lijuan Zhao ◽  
Ruipeng Ma ◽  
Wei Fang ◽  
Jia Hu ◽  
...  
Keyword(s):  
Protein Expression ◽  
Fluorescent Protein ◽  
Expression System ◽  
Agrotis Segetum ◽  
Foreign Protein ◽  
Content Type ◽  
Occlusion Bodies ◽  
Foreign Proteins ◽  
Novel Strategy

ABSTRACT The relatively low infectivity of baculoviruses to their host larvae limits their use as insecticidal agents on a larger scale. In the present study, a novel strategy was developed to efficiently embed foreign proteins into Autographa californica multiple nucleopolyhedrovirus (AcMNPV) occlusion bodies (OBs) to achieve stable expression of foreign proteins and to improve viral infectivity. A recombinant AcMNPV bacmid was constructed by expressing the 150-amino-acid (aa) N-terminal segment of polyhedrin under the control of the p10 promoter and the remaining C-terminal 95-aa segment under the control of the polyhedrin promoter. The recombinant virus formed OBs in Spodoptera frugiperda 9 cells, in which the occlusion-derived viruses were embedded in a manner similar to that for wild-type AcMNPV. Next, the 95-aa polyhedrin C terminus was fused to enhanced green fluorescent protein, and the recombinant AcMNPV formed fluorescent green OBs and was stably passaged in vitro and in vivo. The AcMNPV recombinants were further modified by fusing truncated Agrotis segetum granulovirus enhancin or truncated Cydia pomonella granulovirus ORF13 (GP37) to the C-terminal 95 aa of polyhedrin, and both recombinants were able to form normal OBs. Bioactivity assays indicated that the median lethal concentrations of these two AcMNPV recombinants were 3- to 5-fold lower than that of the control virus. These results suggest that embedding enhancing factors in baculovirus OBs by use of this novel technique may promote efficient and stable foreign protein expression and significantly improve baculovirus infectivity. IMPORTANCE Baculoviruses have been used as bioinsecticides for over 40 years, but their relatively low infectivity to their host larvae limits their use on a larger scale. It has been reported that it is possible to improve baculovirus infectivity by packaging enhancing factors within baculovirus occlusion bodies (OBs); however, so far, the packaging efficiency has been low. In this article, we describe a novel strategy for efficiently embedding foreign proteins into AcMNPV OBs by expressing N- and C-terminal (dimidiate) polyhedrin fragments (150 and 95 amino acids, respectively) as fusions to foreign proteins under the control of the p10 and polyhedrin promoters, respectively. When this strategy was used to embed an enhancing factor (enhancin or GP37) into the baculovirus OBs, 3- to 5-fold increases in baculoviral infectivity were observed. This novel strategy has the potential to create an efficient protein expression system and a highly efficient virus-based system for insecticide production in the future.

Why Cats Cannot be Sensitized to Foreign Proteins

1963 ◽  
Vol 22 (2) ◽  
pp. 85-86 ◽  
Author(s):  
A. Akcasu
Keyword(s):  
Foreign Proteins

scholarly journals pPE1000: A Versatile Vector for the Expression of Epitope-Tagged Foreign Proteins in Transgenic Plants

BioTechniques ◽  
1997 ◽  
Vol 22 (5) ◽  
pp. 861-865 ◽  
Author(s):  
Kerrie R. Hancock ◽  
Lorelle D. Phillips ◽  
Derek W.R. White ◽  
Paul M. Ealing
Keyword(s):  
Transgenic Plants ◽  
Foreign Proteins

Expression of Foreign Proteins by Vaccinia Virus

1990 ◽  
pp. 99-115
Author(s):  
Geoffrey L. Smith
Keyword(s):  
Vaccinia Virus ◽  
Foreign Proteins

scholarly journals Vectored Immunotherapeutics for Infectious Diseases: Can rAAVs Be The Game Changers for Fighting Transmissible Pathogens?

2021 ◽  
Vol 12 ◽  
Author(s):  
Wei Zhan ◽  
Manish Muhuri ◽  
Phillip W. L. Tai ◽  
Guangping Gao
Keyword(s):  
Infectious Diseases ◽  
Neutralizing Antibodies ◽  
Viral Vectors ◽  
De Novo ◽  
Genomic Variation ◽  
Transduction Efficiency ◽  
Foreign Proteins ◽  
Repeated Dosing

Conventional vaccinations and immunotherapies have encountered major roadblocks in preventing infectious diseases like HIV, influenza, and malaria. These challenges are due to the high genomic variation and immunomodulatory mechanisms inherent to these diseases. Passive transfer of broadly neutralizing antibodies may offer partial protection, but these treatments require repeated dosing. Some recombinant viral vectors, such as those based on lentiviruses and adeno-associated viruses (AAVs), can confer long-term transgene expression in the host after a single dose. Particularly, recombinant (r)AAVs have emerged as favorable vectors, given their high in vivo transduction efficiency, proven clinical efficacy, and low immunogenicity profiles. Hence, rAAVs are being explored to deliver recombinant antibodies to confer immunity against infections or to diminish the severity of disease. When used as a vaccination vector for the delivery of antigens, rAAVs enable de novo synthesis of foreign proteins with the conformation and topology that resemble those of natural pathogens. However, technical hurdles like pre-existing immunity to the rAAV capsid and production of anti-drug antibodies can reduce the efficacy of rAAV-vectored immunotherapies. This review summarizes rAAV-based prophylactic and therapeutic strategies developed against infectious diseases that are currently being tested in pre-clinical and clinical studies. Technical challenges and potential solutions will also be discussed.

scholarly journals Lamprey VLRB response to influenza virus supports universal rules of immunogenicity and antigenicity

eLife ◽  
2015 ◽  
Vol 4 ◽  
Author(s):  
Meghan O Altman ◽  
Jack R Bennink ◽  
Jonathan W Yewdell ◽  
Brantley R Herrin
Keyword(s):  
Influenza Virus ◽  
Animal Models ◽  
Convergent Evolution ◽  
Influenza A ◽  
Organic Molecules ◽  
Protein Antigens ◽  
Antigenic Sites ◽  
Foreign Proteins ◽  
Variable Lymphocyte Receptor ◽  
Globular Head

Immunoglobulins (Igs) are a crown jewel of jawed vertebrate evolution. Through recombination and mutation of small numbers of genes, Igs can specifically recognize a vast variety of natural and man-made organic molecules. Jawless vertebrates evolved a parallel system of humoral immunity, which recognizes antigens not with Ig, but with a structurally unrelated receptor called the variable lymphocyte receptor B (VLRB). We exploited the convergent evolution of Ig and VLRB antibodies (Abs) to investigate if intrinsic chemical features of foreign proteins determine their antigenicity and immunogenicity. Surprisingly, we find lamprey VLRB and mouse Ig responses to influenza A virus are extremely similar. Each focuses ∼80% of the response on hemagglutinin (HA), mainly through recognition of the major antigenic sites in the HA globular head domain. Our findings predict basic conservation of Ab responses to protein antigens, strongly supporting the use of animal models for understanding human Ab responses to viruses and protein immunogens.

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