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Multicomponent anthrax toxin display and delivery using bacteriophage T4

We describe a multicomponent antigen display and delivery system using bacteriophage T4. Two dispensable outer capsid proteins, Hoc (highly antigenic outer capsid protein, 155 copies) and Soc (small outer capsid protein, 810 copies), decorate phage T4 capsid. These proteins bind to the symmetrically... Full description

Journal Title: Vaccine 2007, Vol.25(7), pp.1225-1235
Main Author: Shivachandra, Sathish B
Other Authors: Li, Qin , Peachman, Kristina K , Matyas, Gary R , Leppla, Stephen H , Alving, Carl R , Rao, Mangala , Rao, Venigalla B
Format: Electronic Article Electronic Article
Language: English
Subjects:
Hoc
ID: ISSN: 0264-410X ; E-ISSN: 1873-2518 ; DOI: 10.1016/j.vaccine.2006.10.010
Link: https://www.sciencedirect.com/science/article/pii/S0264410X06011157
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recordid: elsevier_sdoi_10_1016_j_vaccine_2006_10_010
title: Multicomponent anthrax toxin display and delivery using bacteriophage T4
format: Article
creator:
  • Shivachandra, Sathish B
  • Li, Qin
  • Peachman, Kristina K
  • Matyas, Gary R
  • Leppla, Stephen H
  • Alving, Carl R
  • Rao, Mangala
  • Rao, Venigalla B
subjects:
  • Bacteriophage T4
  • Virus Assembly
  • Phage Display
  • Anthrax Toxin
  • Hoc
  • Multi-Component Vaccine
  • Medicine
  • Biology
  • Veterinary Medicine
  • Pharmacy, Therapeutics, & Pharmacology
ispartof: Vaccine, 2007, Vol.25(7), pp.1225-1235
description: We describe a multicomponent antigen display and delivery system using bacteriophage T4. Two dispensable outer capsid proteins, Hoc (highly antigenic outer capsid protein, 155 copies) and Soc (small outer capsid protein, 810 copies), decorate phage T4 capsid. These proteins bind to the symmetrically localized capsid sites, which appear following prohead assembly and expansion. We hypothesized that multiple antigens fused to Hoc can be displayed on the same capsid and such particles can elicit broad immunological responses. Anthrax toxin proteins, protective antigen (PA), lethal factor (LF), and edema factor (EF), and their functional domains, were fused to Hoc with an N-terminal hexa-histidine tag and the recombinant proteins were over-expressed in and purified. Using a defined assembly system, the anthrax-Hoc fusion proteins were efficiently displayed on T4 capsid, either individually or in combinations. All of the 155 Hoc binding...
language: eng
source:
identifier: ISSN: 0264-410X ; E-ISSN: 1873-2518 ; DOI: 10.1016/j.vaccine.2006.10.010
fulltext: fulltext
issn:
  • 0264-410X
  • 0264410X
  • 1873-2518
  • 18732518
url: Link


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titleMulticomponent anthrax toxin display and delivery using bacteriophage T4
creatorShivachandra, Sathish B ; Li, Qin ; Peachman, Kristina K ; Matyas, Gary R ; Leppla, Stephen H ; Alving, Carl R ; Rao, Mangala ; Rao, Venigalla B
ispartofVaccine, 2007, Vol.25(7), pp.1225-1235
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subjectBacteriophage T4 ; Virus Assembly ; Phage Display ; Anthrax Toxin ; Hoc ; Multi-Component Vaccine ; Medicine ; Biology ; Veterinary Medicine ; Pharmacy, Therapeutics, & Pharmacology
descriptionWe describe a multicomponent antigen display and delivery system using bacteriophage T4. Two dispensable outer capsid proteins, Hoc (highly antigenic outer capsid protein, 155 copies) and Soc (small outer capsid protein, 810 copies), decorate phage T4 capsid. These proteins bind to the symmetrically localized capsid sites, which appear following prohead assembly and expansion. We hypothesized that multiple antigens fused to Hoc can be displayed on the same capsid and such particles can elicit broad immunological responses. Anthrax toxin proteins, protective antigen (PA), lethal factor (LF), and edema factor (EF), and their functional domains, were fused to Hoc with an N-terminal hexa-histidine tag and the recombinant proteins were over-expressed in and purified. Using a defined assembly system, the anthrax-Hoc fusion proteins were efficiently displayed on T4 capsid, either individually or in combinations. All of the 155 Hoc binding...
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titleMulticomponent anthrax toxin display and delivery using bacteriophage T4
description

We describe a multicomponent antigen display and delivery system using bacteriophage T4. Two dispensable outer capsid proteins, Hoc (highly antigenic outer capsid protein, 155 copies) and Soc (small outer capsid protein, 810 copies), decorate phage T4 capsid. These proteins bind to the symmetrically localized capsid sites, which appear following prohead assembly and expansion. We hypothesized that multiple antigens fused to Hoc can be displayed on the same capsid and such particles can elicit broad immunological responses. Anthrax toxin proteins, protective antigen (PA), lethal factor (LF), and edema factor (EF), and their functional domains, were fused to Hoc with an N-terminal hexa-histidine tag and the recombinant proteins were over-expressed in

and purified. Using a defined

assembly system, the anthrax-Hoc fusion proteins were efficiently displayed on T4 capsid, either individually or in combinations. All of the 155 Hoc binding...

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abstract

We describe a multicomponent antigen display and delivery system using bacteriophage T4. Two dispensable outer capsid proteins, Hoc (highly antigenic outer capsid protein, 155 copies) and Soc (small outer capsid protein, 810 copies), decorate phage T4 capsid. These proteins bind to the symmetrically localized capsid sites, which appear following prohead assembly and expansion. We hypothesized that multiple antigens fused to Hoc can be displayed on the same capsid and such particles can elicit broad immunological responses. Anthrax toxin proteins, protective antigen (PA), lethal factor (LF), and edema factor (EF), and their functional domains, were fused to Hoc with an N-terminal hexa-histidine tag and the recombinant proteins were over-expressed in

and purified. Using a defined

assembly system, the anthrax-Hoc fusion proteins were efficiently displayed on T4 capsid, either individually or in combinations. All of the 155 Hoc binding...

pubElsevier Ltd
doi10.1016/j.vaccine.2006.10.010
lad01Vaccine