Spike protein
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In virology, a spike protein or peplomer protein is a protein that forms a large structure known as a spike or peplomer projecting from the surface of an enveloped virus.[2]: 29–33 The proteins are usually glycoproteins that form dimers or trimers.[3]: 29–33 Often the term "spike protein" refers specifically to the coronavirus spike protein, one of the four major structural proteins common to all coronaviruses, which gives rise to the distinctive appearance of these viruses in electron micrographs.[4]
History and etymology
The term "peplomer" refers to an individual spike from the viral surface; collectively the layer of material at the outer surface of the virion has been referred to as the "peplos".[5] The term is derived from the Greek peplos, "a loose outer garment"[3] or "woman['s] mantle".[5] Early systems of viral taxonomy, such as the Lwoff-Horne-Tournier system proposed in the 1960s, used the appearance and morphology of the "peplos" and peplomers as important characteristics for classification.[5][6][7]
Properties
Spikes or peplomers are usually rod- or club-shaped projections from the viral surface. Spike proteins are membrane proteins with typically large external ectodomains, a single transmembrane domain, and a short tail in the interior of the virion. They may also form protein-protein interactions with other viral proteins, such as those forming the nucleocapsid.[3]: 51–2
Examples
Spikes or peplomers can be visible in electron micrograph images of enveloped viruses such as orthomyxoviruses, paramyxoviruses, rhabdoviruses, filoviruses, coronaviruses, bunyaviruses, arenaviruses, and retroviruses.[3]: 33
- Coronaviruses exhibit coronavirus spike protein, also known as the S protein, on their surfaces; S is a class I fusion protein and is responsible for mediating viral entry as the first step in viral infection.[8] It is highly antigenic and accounts for most antibodies produced by the immune system in response to infection. For this reason the spike protein has been the focus of development for Covid-19 vaccines in response to the Covid-19 pandemic caused by the virus SARS-CoV-2.[9][10] A subgenus of the betacoronaviruses, known as embecoviruses (not including SARS-like coronaviruses), have an additional shorter surface protein known as hemagglutinin esterase.[11]
- Most influenza virus subgroups have two surface proteins described as peplomers, neuraminidase (an enzyme) and hemagglutinin (also a class I fusion protein). Some instead have a single hemagglutinin esterase protein with both functions.[3]: 356–9
- Retroviruses such as the human immunodeficiency virus (HIV) have surface peplomers.[3]: 318–25 These are protein complexes formed by two proteins, gp41 and gp120, both expressed from the env gene, collectively forming a spike protein complex that mediates viral entry.[12]
See also
References
- ^ Solodovnikov, Alexey; Arkhipova, Valeria (29 July 2021). "Достоверно красиво: как мы сделали 3D-модель SARS-CoV-2" [Truly beautiful: how we made the SARS-CoV-2 3D model] (in Russian). N+1. Archived from the original on 30 July 2021. Retrieved 30 July 2021.
- ^ Saunders Comprehensive Veterinary Dictionary (3rd ed.). Elsevier, Inc. 2007. as cited in "peplomer". The Free Dictionary. Farlex. 2011. Retrieved 30 March 2011.
- ^ a b c d e f Cite error: The named reference
burrell_2016was invoked but never defined (see the help page). - ^ Deng, X.; Baker, S.C. (2021). "Coronaviruses: Molecular Biology (Coronaviridae)". Encyclopedia of Virology: 198–207. doi:10.1016/B978-0-12-814515-9.02550-9.
- ^ a b c Lwoff, André; Tournier, Paul (October 1966). "The Classification of Viruses". Annual Review of Microbiology. 20 (1): 45–74. doi:10.1146/annurev.mi.20.100166.000401.
- ^ LWOFF, A; HORNE, RW; TOURNIER, P (13 June 1962). "[A virus system]". Comptes rendus hebdomadaires des seances de l'Academie des sciences. 254: 4225–7. PMID 14467544.
- ^ Lwoff, A.; Horne, R.; Tournier, P. (1 January 1962). "A System of Viruses". Cold Spring Harbor Symposia on Quantitative Biology. 27 (0): 51–55. doi:10.1101/sqb.1962.027.001.008.
- ^ Wang, Yuhang; Grunewald, Matthew; Perlman, Stanley (2020). "Coronaviruses: An Updated Overview of Their Replication and Pathogenesis". Coronaviruses. 2203: 1–29. doi:10.1007/978-1-0716-0900-2_1.
- ^ Le, Tung Thanh; Cramer, Jakob P.; Chen, Robert; Mayhew, Stephen (October 2020). "Evolution of the COVID-19 vaccine development landscape". Nature Reviews Drug Discovery. 19 (10): 667–668. doi:10.1038/d41573-020-00151-8.
- ^ Kyriakidis, Nikolaos C.; López-Cortés, Andrés; González, Eduardo Vásconez; Grimaldos, Alejandra Barreto; Prado, Esteban Ortiz (December 2021). "SARS-CoV-2 vaccines strategies: a comprehensive review of phase 3 candidates". npj Vaccines. 6 (1): 28. doi:10.1038/s41541-021-00292-w.
- ^ Woo, Patrick C. Y.; Huang, Yi; Lau, Susanna K. P.; Yuen, Kwok-Yung (24 August 2010). "Coronavirus Genomics and Bioinformatics Analysis". Viruses. 2 (8): 1804–1820. doi:10.3390/v2081803.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ Mao, Youdong; Wang, Liping; Gu, Christopher; Herschhorn, Alon; Xiang, Shi-Hua; Haim, Hillel; Yang, Xinzhen; Sodroski, Joseph (September 2012). "Subunit organization of the membrane-bound HIV-1 envelope glycoprotein trimer". Nature Structural & Molecular Biology. 19 (9): 893–899. doi:10.1038/nsmb.2351.
Further reading
- F. Fenner et al.: The Biology of Animal Viruses, 2. Auflage, New York, London 1968, ISBN 0-12-253040-3, S. 5f
- D. J. Garwes et al.: Identification of epitopes of immunological importance on the peplomer of porcine transmissible gastroenteritis virus. Adv Exp Med Biol. (1987) 218: S. 509–515, PMID 2449047
- H. G. Niesters et al.: The peplomer protein sequence of the M41 strain of coronavirus IBV and its comparison with Beaudette strains. Virus Res. (1986) 5(2-3): S. 253–263, PMID 2429473
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