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Anthrax vaccines

About: Anthrax vaccines is a research topic. Over the lifetime, 685 publications have been published within this topic receiving 21495 citations.


Papers
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Journal ArticleDOI
TL;DR: PA-PEG is expected as an effective anthrax vaccine candidate with durable immunoprotection against anthrax and could elicit a robust anti-PA IgG and neutralization antibody response in the magnitude and quality.

3 citations

Patent
06 Oct 2006
TL;DR: In this article, the authors disclosed methods for preparing an anthrax spore glycoprotein complex vaccine, and disclosed compositions of an Anthrax vaccine including a SPG as the active agent, which is sufficient to protect against infection from Bacillus anthracis and some forms of Bacillus cereus.
Abstract: Disclosed are methods for preparing an anthrax spore glycoprotein complex vaccine. Also, disclosed compositions of an anthrax vaccine including a spore glycoprotein complex as the active agent. In certain embodiments, the vaccines are sufficient to protect against infection from Bacillus anthracis and some forms of Bacillus cereus that cause an infections such as inhalation anthrax and the like.

3 citations

Journal ArticleDOI
TL;DR: An approach to the development of a universal platform for recombinant vaccines produced in the form of virus-like particles is suggested, a technique of designing fused bifunctional derivatives of bacteriophage proteins containing antigens of interest should be involved.
Abstract: The profitability of vaccine production is less than that of other pharmaceutical goods worldwide. Thus, the cost of the vaccine substance determines the range of vaccines available for use. This is of particular importance for veterinary vaccines. In this review, we have surveyed the published data on exploited vaccines and concluded that the immunogenicity of antigen substances based on whole virions is higher than that of soluble antigens. The physiological basis of this phenomenon remains unknown; however, it may explain why most of the described recombinant vaccines have not yet been put into practice. All practically implemented antiviral vaccines (except that for hepatitis B) are based on viral substances produced by conventional cultural technologies. In light of this observation, an approach to the development of a universal platform for recombinant vaccines produced in the form of virus-like particles is suggested. To this end, a technique of designing fused bifunctional derivatives of bacteriophage proteins containing antigens of interest should be involved. The approach is depicted with the use of the protective anthrax antigen, a conventional vaccine antigen.

3 citations

Journal ArticleDOI
TL;DR: Recently the authors read contributions from La Scola et al., Luna et al, and Bell et al. about their experiences with screening and laboratory analysis carried out to identify anthrax in human samples and environmental samples.
Abstract: Recently we read contributions from La Scola et al. ([4][1]), Luna et al. ([5][2]), and Bell et al. ([1][3]) published in this journal about their experiences with screening and laboratory analysis carried out to identify anthrax in human samples (nasal swabs) and environmental samples (mail pieces

3 citations

Journal ArticleDOI
TL;DR: The receptor binding domain of PA, domain 4 (D4), is isolated, and the effect of the addition of CMG2 on thermodynamic stability is studied, which indicates that the mechanism of stabilization of PA byCMG2 is likely to involve a mutual stabilization of these two domains.
Abstract: The major immunogenic component of the current anthrax vaccine, anthrax vaccine adsorbed (AVA) is protective antigen (PA). We have shown recently that the thermodynamic stability of PA can be significantly improved by binding to the Von-Willebrand factor A (VWA) domain of capillary morphogenesis protein 2 (CMG2), and improvements in thermodynamic stability may improve storage and long-term stability of PA for use as a vaccine. In order to understand the origin of this increase in stability, we have isolated the receptor binding domain of PA, domain 4 (D4), and have studied the effect of the addition of CMG2 on thermodynamic stability. We are able to determine a binding affinity between D4 and CMG2 (∼300 nM), which is significantly weaker than that between full-length PA and CMG2 (170-300 pM). Unlike full-length PA, we observe very little change in stability of D4 on binding to CMG2, using either fluorescence or 19 F-NMR experiments. Because in previous experiments we could observe a stabilization of both domain 4 and domain 2, the mechanism of stabilization of PA by CMG2 is likely to involve a mutual stabilization of these two domains.

3 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
20241
202312
202236
202112
202026
201915