Have you ever wished you could create your own virus, either for your own learning or as a prank Virus creation takes time and knowledge, but anyone can do it if they put their mind to it. Creating a virus can teach you a lot about how a programming language works, as well as operating system and network security. While it may seem as if all viruses are malicious, viruses are simply pieces of code whose goal is to spread as many copies of itself as possible. See Step 1 below to get started and have fun creating your own virus.
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It typically takes a few weeks after vaccination for the body to produce T-lymphocytes and B-lymphocytes. Therefore, it is possible that a person could be infected with the virus that causes COVID-19 just before or just after vaccination and then get sick because the vaccine did not have enough time to provide protection.
Currently, there are three main types of COVID-19 vaccines that are approved or authorized for use in the United States: mRNA, viral vector, and protein subunit. Each type of vaccine prompts our bodies to recognize and help protect us from the virus that causes COVID-19.
Protein subunit vaccines contain pieces (proteins) of the virus that causes COVID-19. These virus pieces are the spike protein. The vaccine also contains another ingredient called an adjuvant that helps the immune system respond to that spike protein in the future. Once the immune system knows how to respond to the spike protein, the immune system will be able to respond quickly to the actual virus spike protein and protect you against COVID-19.
New vaccines are first developed in laboratories. Scientists have been working for many years to develop vaccines against coronaviruses, such as those that cause severe acute respiratory syndrome (SARS) and Middle East respiratory syndrome (MERS). SARS-CoV-2, the virus that causes COVID-19, is related to these other coronaviruses. The knowledge that was gained through past research on coronavirus vaccines helped speed up the initial development of the current COVID-19 vaccines.
To view the full-size infographic, click this photo or the link in the text. Several basic strategies are used to make vaccines, as shown in this infographic [PDF, 272KB]. The strengths and limitations of each approach are described here.
Using this strategy, viruses are completely inactivated (or killed) with a chemical. By killing the virus, it cannot possibly reproduce itself or cause disease. The inactivated polio, hepatitis A, influenza (shot), and rabies vaccines are made this way. Because the virus is still \"seen\" by the body, cells of the immune system that protect against disease are generated.
Using this strategy, just one part of the virus is removed and used as a vaccine. The hepatitis B, shingles, human papillomavirus (HPV), and one of the influenza vaccines are made this way. The vaccine is composed of a protein that resides on the surface of the virus. This strategy can be used when an immune response to one part of the virus (or bacteria) is responsible for protection against disease.These vaccines can be given to people with weakened immunity and appear to induce long-lived immunity after two doses.
Some bacteria cause disease by making a harmful protein called a toxin. Several vaccines are made by taking toxins and inactivating them with a chemical (the toxin, once inactivated, is called a toxoid). By inactivating the toxin, it no longer causes disease. The diphtheria, tetanus and pertussis vaccines are made this way.Another strategy to make a bacterial vaccine is to use part of the sugar coating (or polysaccharide) of the bacteria. Protection against infection by certain bacteria is based on immunity to this sugar coating (and not the whole bacteria). However, because young children don't make a very good immune response to the sugar coating alone, the coating is linked to a harmless protein (this is called a \"conjugated polysaccharide\" vaccine). The Haemophilus influenzae type B (or Hib), pneumococcal, and some meningococcal vaccines are made this way.
Experts in the latter camp argue that gain-of-function virus studies can presage what will eventually happen in nature. Speeding things up in the lab gives researchers firsthand evidence about how a virus might evolve. Such insights could drive predictions about future viral behaviors in order to stay a step ahead of these pathogens.
The moratorium was lifted in 2017. A U.S. government review panel later approved a resumption of funding for more lab studies involving gain-of-function modifications of bird flu viruses in ferrets. Conditions of the approvals, according to reports, included enhanced safety measures and reporting requirements.
Researchers can also test the capacity of virus proteins to engage with different kinds of cells. Software can predict how these proteins might interact with various cell types or how their genetic sequences could be associated with specific virus features. Also, if the researchers use cells in a lab dish, the viruses might be designed not to replicate.
This page doesn't provide information on how to create a computer virus. Computer Hope doesn't condone the creation of or use of computer viruses, and therefore doesn't provide training on how to create a virus. This page discusses the reasons for not creating viruses and alternate options that you could pursue.
Instead of creating computer viruses or other malware, consider learning a computer programming language. You will learn more by learning one or more programming languages and become more qualified in getting hired at a company that designs programs or analyzes viruses. No one ever got hired because they wrote a computer virus.
Virus-like particles (VLPs) are virus-derived structures made up of one or more different molecules with the ability to self-assemble, mimicking the form and size of a virus particle but lacking the genetic material so they are not capable of infecting the host cell. Expression and self-assembly of the viral structural proteins can take place in various living or cell-free expression systems after which the viral structures can be assembled and reconstructed. VLPs are gaining in popularity in the field of preventive medicine and to date, a wide range of VLP-based candidate vaccines have been developed for immunization against various infectious agents, the latest of which is the vaccine against SARS-CoV-2, the efficacy of which is being evaluated. VLPs are highly immunogenic and are able to elicit both the antibody- and cell-mediated immune responses by pathways different from those elicited by conventional inactivated viral vaccines. However, there are still many challenges to this surface display system that need to be addressed in the future. VLPs that are classified as subunit vaccines are subdivided into enveloped and non- enveloped subtypes both of which are discussed in this review article. VLPs have also recently received attention for their successful applications in targeted drug delivery and for use in gene therapy. The development of more effective and targeted forms of VLP by modification of the surface of the particles in such a way that they can be introduced into specific cells or tissues or increase their half-life in the host is likely to expand their use in the future. Recent advances in the production and fabrication of VLPs including the exploration of different types of expression systems for their development, as well as their applications as vaccines in the prevention of infectious diseases and cancers resulting from their interaction with, and mechanism of activation of, the humoral and cellular immune systems are discussed in this review.
Viral-like particles (VLPs) are nanoscale structures made up of assembled viral proteins that lack viral genetic material and are therefore non-infectious . VLPs are dispersed nanomaterials that can be produced in a variety of systems, including mammals, plants, insects, and bacteria. VLPs can be exploited as carriers for the delivery of bio- and nanomaterials, such as drugs, vaccines, quantum dots and imaging substances by virtue of the cavity within their structure [2, 3]. VLPs are icosahedral or rod-shaped structures made by the self-assembly of viral structural proteins . These nanoparticle structures were first identified in 1968 in the sera of patients with Down's syndrome, leukemia and hepatitis. However, their biological nature remained unknown, though it was shown that there are antigenic sites on the surface of these particles . Subsequently it was shown that virus capsid, envelope and, sometimes, core viral proteins can form VLP structures. VLPs can be experimentally generated in the laboratory using recombinant viral proteins that are expressed in a range of expression systems including prokaryotic cells , yeast , insect cell lines [8, 9], plants  and mammalian cell lines [11, 12]. While VLPs are commonly produced using proteins(s) from a single virus type, chimeric VLPs can also be created by the assembly of structural proteins from different viruses .
A largely exploited application of VLPs is their potential in vaccinology where they can offer several advantages over conventional vaccine approaches [18,19,20]. Because of their size and shape, which resembles the actual size and shape of native viruses, these structures can efficiently elicit the immune responses and in VLPs lacking viral genomes there is no potential for replication within the target cells, which offers improved safety especially for immunocompromised or elderly vaccinees . While VLPs can stimulate both humoral and cellu