Wikipedia

Viral envelope

(Redirected from Viral coat)

A viral envelope is the outermost layer of many types of viruses.[1] It protects the genetic material in their life cycle when traveling between host cells. Not all viruses have envelopes. A viral envelope protein or E protein is a protein in the envelope, which may be acquired by the capsid from an infected host cell.

Schematic of a Cytomegalovirus, coat = envelope

Numerous human pathogenic viruses in circulation are encased in lipid bilayers, and they infect their target cells by causing the viral envelope and cell membrane to fuse. Although there are effective vaccines against some of these viruses, there is no preventative or curative medicine for the majority of them. In most cases, the known vaccines operate by inducing antibodies that prevent the pathogen from entering cells. This happens in the case of enveloped viruses when the antibodies bind to the viral envelope proteins.

The membrane fusion event that triggers viral entrance is caused by the viral fusion protein. Many enveloped viruses only have one protein visible on the surface of the particle, which is required for both mediating adhesion to the cell surface and for the subsequent membrane fusion process. To create potentially protective vaccines for human pathogenic enveloped viruses for which there is currently no vaccine, it is essential to comprehend how antibodies interact with viral envelope proteins, particularly with the fusion protein, and how antibodies neutralize viruses.

Enveloped viruses enter cells by joining a cellular membrane to their lipid bilayer membrane. Priming by proteolytic processing, either of the fusion protein or of a companion protein, is necessary for the majority of viral fusion proteins. The priming stage then gets the fusion protein ready for triggering by the processes that go along with attachment and uptake, which frequently happens during transport of the fusion protein to the cell surface but may also happen extracellularly. So far, structural studies have revealed two kinds of viral fusion proteins. These proteins are believed to catalyze the same mechanism in both situations, resulting in the fusing of two bilayers. In other words, these proteins operate as enzymes, which while having various structural variations catalyze the same chemical reaction.[2]

The envelopes are typically derived from portions of the host cell membranes (phospholipids and proteins), but include some viral glycoproteins. One of the main parts of human pathogenic viruses is glycoprotein. They have been shown to play significant roles in immunity and infection.[3] Viral glycoproteins, a new class of cellular inhibitory proteins has been discovered. These include the E3 ubiquitin ligases of the membrane-associated RING-CH (MARCH) family, which among other things, inhibits the expression of cell surface proteins implicated in adaptive immunity.[4] Being made up mostly of host membrane, the viral envelope can also have the proteins associated with the host cell within their membrane after budding.[5] Many enveloped viruses mature by budding at the plasma membrane, which allows them to be discharged from infected cells. During this procedure, viral transmembrane proteins, also known as spike proteins, are integrated into membrane vesicles containing components of the viral core (capsid).

For a very long time, it was thought that the spike proteins, which are necessary for infectivity, were directly incorporated into the viral core through their cytoplasmic domains. Recent research suggests that while such direct interactions may be what causes the budding of alphaviruses, this may not be the case for retroviruses and negative strand RNA viruses. These viruses can form bud particles even in the absence of spike proteins by relying only on viral core components. The spike proteins can occasionally be produced as virus-like particles without the viral core. Therefore, optimal budding and release may be dependent on a coordinated "push-and-pull" action between core and spike, where oligomerization of both components is essential.[6]

They may help viruses avoid the host immune system. TAM receptor tyrosine kinases increase phagocytic clearance of apoptotic cells and inhibit immunological responses brought on by Toll-like receptors and type I interferons (IFNs) when they are activated by the ligands Gas6 and Protein S. The phospholipid phosphatidylserine may be seen on the membranes of several enveloped viruses, which they employ to bind Gas6 and Protein S to activate TAM receptors.

Ligand-coated viruses stimulate type I IFN signaling, activate TAM receptors on dendritic cells (DCs), and suppress type II interferon signaling to circumvent host defenses and advance infection.TAM-deficient DCs exhibit type I IFN responses that are more pronounced than those of wild-type cells in response to viral exposure. As a result, flaviviruses and pseudo typed retroviruses have a harder time infecting TAM-deficient DCs, albeit infection can be brought back by type I IFN antibodies. A TAM kinase inhibitor, meanwhile, prevents infection of wild-type DCs. TAM receptors, which are potential targets for therapy, are thereby activated by viruses to reduce type I IFN signaling.[7] Glycoproteins on the surface of the envelope serve to identify and bind to receptor sites on the host's membrane. The particular set of viral proteins are engaged in a series of structural changes. When these changes are set/finished, there is then and only then, fusion with the host membrane.[8] These glycoproteins mediate the interaction between virion and host cell, typically initiating the fusion between the viral envelope and the host's cellular membrane.[9] In some cases, the virus with an envelope will form an endosome within the host cell.[10] There are three main types of viral glycoproteins: Envelope proteins, membrane proteins, and spike proteins (E, M, and S).[11] The viral envelope then fuses with the host's membrane, allowing the capsid and viral genome to enter and infect the host.[citation needed]

All enveloped viruses also have a capsid, another protein layer, between the envelope and the genome.[1] The virus wraps its delicate nucleic acid with a protein shell known as the capsid, from the Latin capsa, meaning "box," in order to shield it from this hostile environment. Similar to how numerous bricks come together to form a wall, the capsid is made up of one or more distinct protein types that repeatedly repeat to form the whole capsid. This repetitive pattern creates a robust but rather flexible capsid. The nucleic acid inside the capsid is appropriately protected by its modest size and physical difficulty in opening it. The nucleocapsid of the virion is made up of the nucleic acid and the capsid. Remember that the genomes of most viruses are very small. Genes code for instructions to make proteins, so small genomes cannot code for many proteins. Therefore, the virion capsid consists of one or only a few proteins that repeat over and over  to form the structure. The viral nucleic acid  would be physically too large to fit inside the capsid if it consisted of more than  a few proteins.[12] The capsid, having a focused role of protecting the genome in addition to immune recognition evasion.[13] The viral capsid is known for its protection of RNA before it is inserted into the host cell, unlike the viral envelope which protects the protein capsid.[14]

The cell from which a virus buds often dies or is weakened, and sheds more viral particles for an extended period. The lipid bilayer envelope of these viruses is relatively sensitive to desiccation, heat, and amphiphiles such as soap and detergents, therefore these viruses are easier to sterilize than non-enveloped viruses, have limited survival outside host environments, and typically must transfer directly from host to host. Viral envelope persistence, whether it be enveloped or naked, are a factor in determining longevity of a virus on inanimate surfaces.[15] Enveloped viruses possess great adaptability and can change in a short time in order to evade the immune system. Enveloped viruses can cause persistent infections.[citation needed]

Vaccination against enveloped viruses can function by neutralizing the glycoprotein activity with antibodies.[16]

Eliminating the virus's ability to form an envelope—by removing or inactivating a structural protein—or to bud has been studied as a method for producing viruses incapable of replication[17][18][19][20][21].

Examples of enveloped viruses

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The following are some examples of enveloped virus species:

Examples of non-enveloped viruses

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The following are some examples of viruses without envelopes:

See also

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References

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  1. ^ a b HURLBERT, RONALD E. Fundamentals of Microbiology 102. Chapter #11: Viruses. Archived from the original on 2008-11-10. Retrieved 2008-11-07.
  2. ^ Rey, Felix A.; Lok, Shee-Mei (2018-03-08). "Common Features of Enveloped Viruses and Implications for Immunogen Design for Next-Generation Vaccines". Cell. 172 (6): 1319–1334. doi:10.1016/j.cell.2018.02.054. ISSN 0092-8674. PMC 7112304. PMID 29522750. S2CID 3775608.
  3. ^ Banerjee, Nilotpal; Mukhopadhyay, Sumi (March 2016). "Viral glycoproteins: biological role and application in diagnosis". Virusdisease. 27 (1): 1–11. doi:10.1007/s13337-015-0293-5. ISSN 2347-3584. PMC 4758313. PMID 26925438.
  4. ^ Lun, Cheng Man; Waheed, Abdul A.; Majadly, Ahlam; Powell, Nicole; Freed, Eric O. (2021-03-16). "Mechanism of Viral Glycoprotein Targeting by Membrane-Associated RING-CH Proteins". mBio. 12 (2): e00219–21. doi:10.1128/mBio.00219-21. ISSN 2150-7511. PMC 8092221. PMID 33727347.
  5. ^ Gelderblom HR. Structure and Classification of Viruses. In: Baron S, editor. Medical Microbiology. 4th edition. Galveston (TX): University of Texas Medical Branch at Galveston; 1996. Chapter 41. Available from: https://www.ncbi.nlm.nih.gov/books/NBK8174/
  6. ^ Cadd, T. L.; Skoging, U.; Liljeström, P. (November 1997). "Budding of enveloped viruses from the plasma membrane". BioEssays: News and Reviews in Molecular, Cellular and Developmental Biology. 19 (11): 993–1000. doi:10.1002/bies.950191109. ISSN 0265-9247. PMC 7161837. PMID 9394621.
  7. ^ Bhattacharyya, Suchita; Zagórska, Anna; Lew, Erin D.; Shrestha, Bimmi; Rothlin, Carla V.; Naughton, John; Diamond, Michael S.; Lemke, Greg; Young, John A.T. (2013-08-14). "Enveloped Viruses Disable Innate Immune Responses in Dendritic Cells by Direct Activation of TAM Receptors". Cell Host & Microbe. 14 (2): 136–147. doi:10.1016/j.chom.2013.07.005. ISSN 1931-3128. PMC 3779433. PMID 23954153.
  8. ^ Benhaim, Mark A.; Lee, Kelly K. (2020-04-08). "New Biophysical Approaches Reveal the Dynamics and Mechanics of Type I Viral Fusion Machinery and Their Interplay with Membranes". Viruses. 12 (4): E413. doi:10.3390/v12040413. ISSN 1999-4915. PMC 7232462. PMID 32276357.
  9. ^ Navaratnarajah, C.K. et al. “Assembly of Viruses: Enveloped Particles.” Encyclopedia of Virology (2008): 193–200. doi:10.1016/B978-012374410-4.00667-1
  10. ^ White, Judith M, and Gary R Whittaker. “Fusion of Enveloped Viruses in Endosomes.” Traffic vol. 17,6 (2016): 593-614. doi:10.1111/tra.12389
  11. ^ Banerjee, Nilotpal, and Sumi Mukhopadhyay. “Viral glycoproteins: biological role and application in diagnosis.” Virusdisease vol. 27,1 (2016): 1-11. doi:10.1007/s13337-015-0293-5
  12. ^ Louten, Jennifer (2016). "Virus Structure and Classification". Essential Human Virology: 19–29. doi:10.1016/B978-0-12-800947-5.00002-8. ISBN 9780128009475. PMC 7150055.
  13. ^ Stuart, David I.; Ren, Jingshan; Wang, Xiangxi; Rao, Zihe; Fry, Elizabeth E. (May 2019). "Hepatitis A Virus Capsid Structure". Cold Spring Harbor Perspectives in Medicine. 9 (5): a031807. doi:10.1101/cshperspect.a031807. ISSN 2157-1422. PMC 6496327. PMID 30037986.
  14. ^ Cliver, Dean O. (2009). "Capsid and Infectivity in Virus Detection". Food and Environmental Virology. 1 (3): 123–128. doi:10.1007/s12560-009-9020-y. ISSN 1867-0334. PMC 2837222. PMID 20234879.
  15. ^ Firquet, Swan; Beaujard, Sophie; Lobert, Pierre-Emmanuel; Sané, Famara; Caloone, Delphine; Izard, Daniel; Hober, Didier (June 2015). "Survival of Enveloped and Non-Enveloped Viruses on Inanimate Surfaces". Microbes and Environments. 30 (2): 140–144. doi:10.1264/jsme2.ME14145. ISSN 1342-6311. PMC 4462923. PMID 25843687.
  16. ^ Rey, Felix A.; Lok, Shee-Mei (8 March 2018). "Common Features of Enveloped Viruses and Implications for Immunogen Design for Next-Generation Vaccines". Cell. 172 (6): 1319–1334. doi:10.1016/j.cell.2018.02.054. PMC 7112304. PMID 29522750.
  17. ^ Zhang, En; Ke, Yong; Ran, Weihong; Zhang, Yu; Li, Ruihang; Fang, Xinkui; Wang, Lei; Zhang, Baohong; Sun, Tao (2024-11-11). "Assessment of Single-Cycle M-Protein Mutated Vesicular Stomatitis Virus as a Safe and Immunogenic Mucosal Vaccine Platform for SARS-CoV-2 Immunogen Delivery". Advanced Science (Weinheim, Baden-Wurttemberg, Germany): e2404197. doi:10.1002/advs.202404197. ISSN 2198-3844. PMID 39526809.
  18. ^ Zheng, Ming Z. M.; Tan, Tiong Kit; Villalon-Letelier, Fernando; Lau, Hilda; Deng, Yi-Mo; Fritzlar, Svenja; Valkenburg, Sophie A.; Gu, Haogao; Poon, Leo L. M.; Reading, Patrick C.; Townsend, Alain R.; Wakim, Linda M. (2023-09-08). "Single-cycle influenza virus vaccine generates lung CD8+ Trm that cross-react against viral variants and subvert virus escape mutants". Science Advances. 9 (36): eadg3469. doi:10.1126/sciadv.adg3469. ISSN 2375-2548. PMC 10491285. PMID 37683004.
  19. ^ Zheng, Ming Z. M.; Tan, Tiong Kit; Villalon-Letelier, Fernando; Lau, Hilda; Deng, Yi-Mo; Fritzlar, Svenja; Valkenburg, Sophie A.; Gu, Haogao; Poon, Leo L. M.; Reading, Patrick C.; Townsend, Alain R.; Wakim, Linda M. (2023-09-08). "Single-cycle influenza virus vaccine generates lung CD8+ Trm that cross-react against viral variants and subvert virus escape mutants". Science Advances. 9 (36): eadg3469. doi:10.1126/sciadv.adg3469. ISSN 2375-2548. PMC 10491285. PMID 37683004.
  20. ^ Kim, Se-Heon; Carew, John F.; Kooby, David A.; Shields, John; Entwisle, Claire; Patel, Snehal; Shah, Jatin P.; Fong, Yuman (September 2000). "Combination gene therapy using multiple immunomodulatory genes transferred by a defective infectious single-cycle herpes virus in squamous cell cancer". Cancer Gene Therapy. 7 (9): 1279–1285. doi:10.1038/sj.cgt.7700231. ISSN 1476-5500. PMID 11023201.
  21. ^ Lett, Martin Joseph; Otte, Fabian; Hauser, David; Schön, Jacob; Kipfer, Enja Tatjana; Hoffmann, Donata; Halwe, Nico J.; Breithaupt, Angele; Ulrich, Lorenz; Britzke, Tobias; Kochmann, Jana; Corleis, Björn; Zhang, Yuepeng; Urda, Lorena; Cmiljanovic, Vladimir (2024-10-30). "High protection and transmission-blocking immunity elicited by single-cycle SARS-CoV-2 vaccine in hamsters". npj Vaccines. 9 (1): 206. doi:10.1038/s41541-024-00992-z. ISSN 2059-0105. PMC 11522273. PMID 39472701.
  22. ^ "The Rabies Virus". CDC. Archived from the original on 2017-01-18. Retrieved 2008-11-07.
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Wikimedia Commons has media related to Viral envelope.
  • "Virus Structure". Molecular Expressions: Images from the Microscope. Retrieved 2007-06-27.
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