Synthetic vaccine

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A synthetic vaccine is a vaccine consisting mainly of synthetic peptides, carbohydrates, or antigens. They are usually considered to be safer than vaccines from bacterial cultures. Creating vaccines synthetically has the ability to increase the speed of production. This is especially important in the event of a pandemic.

Contents

History

The world's first synthetic vaccine was created in 1796 from diphtheria toxin by Louis Chedid (scientist) from the Pasteur Institute and Michael Sela from the Weizmann Institute.[ citation needed ]

In 1986, Manuel Elkin Patarroyo created the SPf66, the first version of a synthetic vaccine for Malaria. [1]

During the H1N1 outbreak in 2009, vaccines only became available in large quantities after the peak of human infections. This was a learning experience for vaccination companies. Novartis Vaccine and Diagnostics, among other companies, developed a synthetic approach that very rapidly generates vaccine viruses from sequence data in order to be able to administer vaccinations early in the pandemic outbreak. Philip Dormatizer, the leader of viral vaccine research at Novartis, says they have "developed a way of chemically synthesizing virus genomes and growing them in tissue culture cells". [2]

Phase I data of UB-311, a synthetic peptide vaccine targeting amyloid beta, showed that the drug was able to generate antibodies to specific amyloid beta oligomers and fibrils with no decrease in antibody levels in patients of advanced age. Results from the Phase II trial are expected in the second half of 2018. [3] [4]

Related Research Articles

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<span class="mw-page-title-main">Manuel Elkin Patarroyo</span>

Manuel Elkin Patarroyo Murillo is a Colombian Professor of Pathology and Immunology who made the world's first attempt to create a synthetic vaccine against the protozoal parasite Plasmodium falciparum, the cause of severe malaria, and responsible for the death of ~1.5 million people per year in tropical and subtropical regions, including parts of the Americas, Asia, and Africa.

<span class="mw-page-title-main">Amyloid</span> Insoluble protein aggregate with a fibrillar morphology

Amyloids are aggregates of proteins characterised by a fibrillar morphology of typically 7–13 nm in diameter, a beta sheet (β-sheet) secondary structure and ability to be stained by particular dyes, such as Congo red. In the human body, amyloids have been linked to the development of various diseases. Pathogenic amyloids form when previously healthy proteins lose their normal structure and physiological functions (misfolding) and form fibrous deposits within and around cells. These protein misfolding and deposition processes disrupt the healthy function of tissues and organs.

<span class="mw-page-title-main">Amyloid beta</span> Group of peptides

Amyloid beta denotes peptides of 36–43 amino acids that are the main component of the amyloid plaques found in the brains of people with Alzheimer's disease. The peptides derive from the amyloid precursor protein (APP), which is cleaved by beta secretase and gamma secretase to yield Aβ in a cholesterol-dependent process and substrate presentation. Aβ molecules can aggregate to form flexible soluble oligomers which may exist in several forms. It is now believed that certain misfolded oligomers can induce other Aβ molecules to also take the misfolded oligomeric form, leading to a chain reaction akin to a prion infection. The oligomers are toxic to nerve cells. The other protein implicated in Alzheimer's disease, tau protein, also forms such prion-like misfolded oligomers, and there is some evidence that misfolded Aβ can induce tau to misfold.

<span class="mw-page-title-main">Amyloid-beta precursor protein</span> Mammalian protein found in Homo sapiens

Amyloid-beta precursor protein (APP) is an integral membrane protein expressed in many tissues and concentrated in the synapses of neurons. It functions as a cell surface receptor and has been implicated as a regulator of synapse formation, neural plasticity, antimicrobial activity, and iron export. It is coded for by the gene APP and regulated by substrate presentation. APP is best known as the precursor molecule whose proteolysis generates amyloid beta (Aβ), a polypeptide containing 37 to 49 amino acid residues, whose amyloid fibrillar form is the primary component of amyloid plaques found in the brains of Alzheimer's disease patients.

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The Alzheimer's disease biomarkers are neurochemical indicators used to assess the risk or presence of the disease. The biomarkers can be used to diagnose Alzheimer's disease (AD) in a very early stage, but they also provide objective and reliable measures of disease progress. It is imperative to diagnose AD disease as soon as possible, because neuropathologic changes of AD precede the symptoms by years. It is well known that amyloid beta (Aβ) is a good indicator of AD disease, which has facilitated doctors to accurately pre-diagnose cases of AD. When Aβ peptide is released by proteolytic cleavage of amyloid-beta precursor protein, some Aβ peptides that are solubilized are detected in CSF and blood plasma which makes AB peptides a promising candidate for biological markers. It has been shown that the amyloid beta biomarker shows 80% or above sensitivity and specificity, in distinguishing AD from dementia. It is believed that amyloid beta as a biomarker will provide a future for diagnosis of AD and eventually treatment of AD.

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References

  1. Patarroyo, Manuel E. (May 30, 2007). "Synthetic vaccine update: Applying lessons learned from recent SPf66 malarial vaccine physicochemical, structural and immunological characterization". Vaccine. 25, 22 (22): 4487–4501. doi:10.1016/j.vaccine.2007.03.016. PMID   17403557.
  2. Young Rojahn, Susan (May 14, 2013). "Synthetic Biology Could Speed Flu Vaccine Production". MIT Technology Review.
  3. http://www.bioworld.com/content/alz-players-stand-united-new-beta-bids-also-fall%5B%5D
  4. Wang, Chang Yi; Wang, Pei-Ning; Chiu, Ming-Jang; Finstad, Connie L; Lin, Feng; Lynn, Shugene; Tai, Yuan-Hung; De Fang, Xin; Zhao, Kesheng; Hung, Chung-Ho; Tseng, Yiting; Peng, Wen-Jiun; Wang, Jason; Yu, Chih-Chieh; Kuo, Be-Sheng; Frohna, Paul A (2017). "UB-311, a novel UBITh ® amyloid β peptide vaccine for mild Alzheimer's disease". Alzheimer's & Dementia: Translational Research & Clinical Interventions. 3 (2): 262–272. doi:10.1016/j.trci.2017.03.005. PMC   5651432 . PMID   29067332.