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{{Short description|Glycoprotein spike on a viral capsid or viral envelope}}
{{Short description|Glycoprotein spike on a viral capsid or viral envelope}}
{{For|the spike protein in coronaviruses|coronavirus spike protein}}
{{for|the spike protein in coronaviruses|Coronavirus spike protein}}


[[file:Coronavirus. SARS-CoV-2.png|thumb|[[Coronavirus spike protein]]s (turqoise) projecting from the surface of [[SARS-CoV-2]], the virus that causes [[COVID-19]]. The protein is [[glycosylated]] and its [[glycan]]s are shown in orange.<ref>{{cite web |surname1=Solodovnikov | given1=Alexey |surname2=Arkhipova| given2=Valeria |title = Достоверно красиво: как мы сделали 3D-модель SARS-CoV-2 |trans-title=Truly beautiful: how we made the SARS-CoV-2 3D model |url = https://nplus1.ru/blog/2021/07/29/sars-cov-2-model |archive-url = https://web.archive.org/web/20210730143142/https://nplus1.ru/blog/2021/07/29/sars-cov-2-model |publisher= [[w:ru:N+1|N+1]] |archive-date=2021-07-30 |date =2021-07-29 |access-date=30 July 2021 |language =ru}}</ref>]]
[[File:Coronavirus. SARS-CoV-2.png|thumb|[[Coronavirus spike protein]]s (turquoise) projecting from the surface of [[SARS-CoV-2]], the virus that causes [[COVID-19]]. The protein is [[glycosylated]] and its [[glycan]]s are shown in orange.<ref>{{cite web |surname1=Solodovnikov | given1=Alexey |surname2=Arkhipova| given2=Valeria |title = Достоверно красиво: как мы сделали 3D-модель SARS-CoV-2 |trans-title=Truly beautiful: how we made the SARS-CoV-2 3D model |url = https://nplus1.ru/blog/2021/07/29/sars-cov-2-model |archive-url = https://web.archive.org/web/20210730143142/https://nplus1.ru/blog/2021/07/29/sars-cov-2-model |publisher= [[w:ru:N+1|N+1]] |archive-date=2021-07-30 |date =2021-07-29 |access-date=30 July 2021 |language =ru}}</ref>]]
[[File:Novel Coronavirus SARS-CoV-2 Spike Protein (49583626473).jpg|thumb|[[3D print]] of one of the trimeric spikes of [[SARS-CoV-2]]]]
[[File:Novel Coronavirus SARS-CoV-2 Spike Protein (49583626473).jpg|thumb|[[3D print]] of one of the trimeric spikes of [[SARS-CoV-2]]]]


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 [[viral envelope|enveloped]] [[virus]].<ref>{{cite book|title=Saunders Comprehensive Veterinary Dictionary|url=https://archive.org/details/saunderscomprehe00doug|url-access=registration|edition=3rd|year=2007|publisher=[[Elsevier|Elsevier, Inc]]}} as cited in {{cite web|title=peplomer| work=[[TheFreeDictionary.com|The Free Dictionary]]|publisher=Farlex|access-date=30 March 2011|url=http://medical-dictionary.thefreedictionary.com/peplomer|year=2011}}</ref><ref name="burrell_2016">{{cite book |last1=Burrell |first1=Christopher J. |title=Fenner and White's medical virology |date=2016 |location=London, United Kingdom |isbn=978-0123751560 |edition=Fifth}}</ref>{{rp|29-33}} The proteins are usually [[glycoprotein]]s that form [[dimer]]s or [[trimer]]s.<ref name=burrell_2016 />{{rp|29-33}} Often the term "spike protein" refers specifically to the [[coronavirus spike protein]], one of the four major [[viral structural protein|structural protein]]s common to all [[coronavirus]]es, which gives rise to the distinctive appearance of these viruses in [[electron micrograph]]s.<ref name="deng_2021">{{cite journal |last1=Deng |first1=X. |last2=Baker |first2=S.C. |title=Coronaviruses: Molecular Biology (Coronaviridae) |journal=Encyclopedia of Virology |date=2021 |pages=198–207 |doi=10.1016/B978-0-12-814515-9.02550-9}}</ref>
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 [[viral envelope|enveloped]] [[virus]].<ref>{{cite book|title=Saunders Comprehensive Veterinary Dictionary|url=https://archive.org/details/saunderscomprehe00doug|url-access=registration|edition=3rd|year=2007|publisher=[[Elsevier|Elsevier, Inc]]}} as cited in {{cite web|title=peplomer| work=[[TheFreeDictionary.com|The Free Dictionary]]|publisher=Farlex|access-date=30 March 2011|url=http://medical-dictionary.thefreedictionary.com/peplomer|year=2011}}</ref><ref name="burrell_2016">{{cite book |last1=Burrell |first1=Christopher J. |title=Fenner and White's medical virology |date=2016 |location=London, United Kingdom |isbn=978-0123751560 |edition=Fifth}}</ref>{{rp|29–33}} The proteins are usually [[glycoprotein]]s that form [[Protein dimer|dimer]]s or [[Protein trimer|trimer]]s.<ref name=burrell_2016 />{{rp|29–33}} <ref name="deng_2021">{{cite journal |last1=Deng |first1=X. |last2=Baker |first2=S.C. |title=Coronaviruses: Molecular Biology (Coronaviridae) |journal=Encyclopedia of Virology |date=2021 |pages=198–207 |doi=10.1016/B978-0-12-814515-9.02550-9|isbn=9780128145166 |doi-access=free }}</ref>


==History and etymology==
==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".<ref name="lwoff_1966">{{cite journal |last1=Lwoff |first1=André |last2=Tournier |first2=Paul |title=The Classification of Viruses |journal=Annual Review of Microbiology |date=October 1966 |volume=20 |issue=1 |pages=45–74 |doi=10.1146/annurev.mi.20.100166.000401}}</ref> The term is derived from the Greek [[peplos]], "a loose outer garment"<ref name=burrell_2016 /> or "woman['s] mantle".<ref name=lwoff_1966 /> Early systems of [[viral taxonomy]], such as the [[André Michel Lwoff|Lwoff]]-[[Robert Horne|Horne]]-[[Paul Tournier|Tournier]] system proposed in the 1960s, used the appearance and morphology of the "peplos" and peplomers as important characteristics for classification.<ref name=lwoff_1966 /><ref name="lwoff_1962">{{cite journal |last1=LWOFF |first1=A |last2=HORNE |first2=RW |last3=TOURNIER |first3=P |title=[A virus system]. |journal=Comptes rendus hebdomadaires des seances de l'Academie des sciences |date=13 June 1962 |volume=254 |pages=4225-7 |pmid=14467544}}</ref><ref name="lwoff_cshl_1962">{{cite journal |last1=Lwoff |first1=A. |last2=Horne |first2=R. |last3=Tournier |first3=P. |title=A System of Viruses |journal=Cold Spring Harbor Symposia on Quantitative Biology |date=1 January 1962 |volume=27 |issue=0 |pages=51–55 |doi=10.1101/sqb.1962.027.001.008}}</ref>
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".<ref name="lwoff_1966">{{cite journal |last1=Lwoff |first1=André |last2=Tournier |first2=Paul |title=The Classification of Viruses |journal=Annual Review of Microbiology |date=October 1966 |volume=20 |issue=1 |pages=45–74 |doi=10.1146/annurev.mi.20.100166.000401|pmid=5330240 }}</ref> The term is derived from the Greek [[peplos]], "a loose outer garment",<ref name=burrell_2016 /> "robe or cloak",<ref name="mahy_2009">{{cite book |last1=Mahy |first1=B. W. J. |title=The dictionary of virology |date=2009 |publisher=Elsevier/Academic Press |location=Amsterdam |isbn=9780080920368 |edition=4th}}</ref> or "woman['s] mantle".<ref name=lwoff_1966 /> Early systems of [[viral taxonomy]], such as the [[André Michel Lwoff|Lwoff]]–[[Robert Horne (virologist)|Horne]]–[[Paul Tournier (virologist)|Tournier]] system proposed in the 1960s, used the appearance and morphology of the "peplos" and peplomers as important characteristics for classification.<ref name=lwoff_1966 /><ref name="lwoff_1962">{{cite journal |last1=Lwoff |first1=A |last2=Horne |first2=RW |last3=Tournier |first3=P |title=[A virus system]. |journal=Comptes rendus hebdomadaires des séances de l'Académie des sciences |date=13 June 1962 |volume=254 |pages=4225–7 |pmid=14467544}}</ref><ref name="lwoff_cshl_1962">{{cite journal |last1=Lwoff |first1=A. |last2=Horne |first2=R. |last3=Tournier |first3=P. |title=A System of Viruses |journal=Cold Spring Harbor Symposia on Quantitative Biology |date=1 January 1962 |volume=27 |pages=51–55 |doi=10.1101/sqb.1962.027.001.008|pmid=13931895 }}</ref> More recently, the term "peplos" is considered a synonym for [[viral envelope]].<ref name=mahy_2009 />{{rp|362}}


==Properties==
==Properties==
Spikes or peplomers are usually rod- or club-shaped projections from the viral surface. Spike proteins are [[membrane protein]]s with typically large external [[ectodomain]]s, a single [[transmembrane domain]], and a short tail in the interior of the [[virion]]. They may also form [[protein-protein interaction]]s with other viral proteins, such as those forming the [[nucleocapsid]].<ref name=burrell_2016 />{{rp|51-2}}
Spikes or peplomers are usually rod- or club-shaped projections from the viral surface. Spike proteins are [[membrane protein]]s with typically large external [[ectodomain]]s, a single [[transmembrane domain]] that anchors the protein in the [[viral envelope]], and a short tail in the interior of the [[virion]]. They may also form [[protein–protein interaction]]s with other viral proteins, such as those forming the [[nucleocapsid]].<ref name=burrell_2016 />{{rp|51–2}} They are usually [[glycoprotein]]s, more commonly via [[N-linked glycosylation|''N''-linked]] than [[O-linked glycosylation|''O''-linked]] [[glycosylation]].<ref name=burrell_2016 />{{rp|33}}

==Functions==
Spikes typically have a role in [[viral entry]]. They may interact with [[cell-surface receptor]]s located on the [[host cell]] and may have [[Hemagglutination|hemagglutinizing]] activity as a result, or in other cases they may be [[enzyme]]s.<ref name=mahy_2009 />{{rp|362}} For example, [[influenza virus]] has two surface proteins with these two functions, [[hemagglutinin (influenza)|hemagglutinin]] and [[neuraminidase]].<ref name=mahy_2009 />{{rp|329}} The [[binding site]] for the cell-surface receptor is usually located at the tip of the spike.<ref name=burrell_2016 />{{rp|33}} Many spike proteins are [[membrane fusion protein]]s.<ref name="harrison_2015">{{cite journal |last1=Harrison |first1=Stephen C. |title=Viral membrane fusion |journal=Virology |date=May 2015 |volume=479-480 |pages=498–507 |doi=10.1016/j.virol.2015.03.043|pmid=25866377 |pmc=4424100 }}</ref> Being exposed on the surface of the virion, spike proteins can be [[antigen]]s.<ref name=mahy_2009 />{{rp|362}}


==Examples==
==Examples==
Spikes or peplomers can be visible in [[electron micrograph]] images of [[enveloped virus]]es such as [[Orthomyxoviridae|orthomyxoviruses]], [[paramyxoviruses]], [[rhabdoviruses]], [[filoviruses]], [[coronaviruses]], [[Bunyavirales|bunyaviruses]], [[Arenavirus|arenaviruses]], and [[retroviruses]].<ref name=burrell_2016 />{{rp|33}}
Spikes or peplomers can be visible in [[electron micrograph]] images of [[enveloped virus]]es such as [[Orthomyxoviridae|orthomyxoviruses]], [[paramyxoviruses]], [[rhabdoviruses]], [[filoviruses]], [[coronaviruses]], [[Bunyavirales|bunyaviruses]], [[arenavirus]]es, and [[retroviruses]].<ref name=burrell_2016 />{{rp|33}}

===Coronaviruses===
⚫
[[Coronavirus]]es 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.<ref name="wang_2020">{{cite book |last1=Wang |first1=Yuhang |last2=Grunewald |first2=Matthew |last3=Perlman |first3=Stanley |title=Coronaviruses |chapter=Coronaviruses: An Updated Overview of Their Replication and Pathogenesis |series=Methods in Molecular Biology |date=2020 |volume=2203 |pages=1–29 |doi=10.1007/978-1-0716-0900-2_1|pmid=32833200 |pmc=7682345 |isbn=978-1-0716-0899-9 }}</ref> 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]].<ref name="le_2020">{{cite journal |last1=Le |first1=Tung Thanh |last2=Cramer |first2=Jakob P. |last3=Chen |first3=Robert |last4=Mayhew |first4=Stephen |title=Evolution of the COVID-19 vaccine development landscape |journal=Nature Reviews Drug Discovery |date=October 2020 |volume=19 |issue=10 |pages=667–668 |doi=10.1038/d41573-020-00151-8|pmid=32887942 |s2cid=221503034 |doi-access=free }}</ref><ref name="kyriakidis_2021">{{cite journal |last1=Kyriakidis |first1=Nikolaos C. |last2=López-Cortés |first2=Andrés |last3=González |first3=Eduardo Vásconez |last4=Grimaldos |first4=Alejandra Barreto |last5=Prado |first5=Esteban Ortiz |title=SARS-CoV-2 vaccines strategies: a comprehensive review of phase 3 candidates |journal=npj Vaccines |date=December 2021 |volume=6 |issue=1 |pages=28 |doi=10.1038/s41541-021-00292-w|pmid=33619260 |pmc=7900244 }}</ref> A [[subgenus]] of the [[betacoronavirus]]es, known as [[embecovirus]]es (not including [[SARSr-CoV|SARS-like]] coronaviruses), have an additional shorter surface protein known as [[hemagglutinin esterase]].<ref name="woo_2010">{{cite journal |last1=Woo |first1=Patrick C. Y. |last2=Huang |first2=Yi |last3=Lau |first3=Susanna K. P. |last4=Yuen |first4=Kwok-Yung |title=Coronavirus Genomics and Bioinformatics Analysis |journal=Viruses |date=24 August 2010 |volume=2 |issue=8 |pages=1804–1820 |doi=10.3390/v2081803|pmid=21994708 |pmc=3185738 |doi-access=free }}</ref>

The COVID-19 pandemic necessitated identification of viral particles in electron micrographs of patient tissue samples. A number of reports misidentified normal subcellular structures as coronaviruses due to their superficial resemblance to coronavirus morphology, and because the distinctive spikes of coronaviruses are apparent by [[negative stain]] but much less visible in [[Ultramicrotomy|thin section]].<ref name="bullock_2021">{{cite journal |last1=Bullock |first1=Hannah A. |last2=Goldsmith |first2=Cynthia S. |last3=Zaki |first3=Sherif R. |last4=Martines |first4=Roosecelis B. |last5=Miller |first5=Sara E. |title=Difficulties in Differentiating Coronaviruses from Subcellular Structures in Human Tissues by Electron Microscopy |journal=Emerging Infectious Diseases |date=April 2021 |volume=27 |issue=4 |pages=1023–1031 |doi=10.3201/eid2704.204337|pmid=33600302 |pmc=8007326 }}</ref>

===Influenza viruses===
⚫
Most [[influenza virus]] subgroups have two surface proteins described as peplomers, [[neuraminidase]] (an [[enzyme]]) and [[hemagglutinin (influenza)|hemagglutinin]] (also a class I fusion protein). Some instead have a single [[hemagglutinin esterase]] protein with both functions.<ref name=burrell_2016 />{{rp|356–9}}


===Retroviruses===
⚫
* [[Coronavirus]]es 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.<ref name="wang_2020">{{cite journal |last1=Wang |first1=Yuhang |last2=Grunewald |first2=Matthew |last3=Perlman |first3=Stanley |title=Coronaviruses: An Updated Overview of Their Replication and Pathogenesis |journal=Coronaviruses |date=2020 |volume=2203 |pages=1–29 |doi=10.1007/978-1-0716-0900-2_1}}</ref> 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 vaccine]]s in response to the [[Covid-19 pandemic]] caused by the virus [[SARS-CoV-2]].<ref name="le_2020">{{cite journal |last1=Le |first1=Tung Thanh |last2=Cramer |first2=Jakob P. |last3=Chen |first3=Robert |last4=Mayhew |first4=Stephen |title=Evolution of the COVID-19 vaccine development landscape |journal=Nature Reviews Drug Discovery |date=October 2020 |volume=19 |issue=10 |pages=667–668 |doi=10.1038/d41573-020-00151-8}}</ref><ref name="kyriakidis_2021">{{cite journal |last1=Kyriakidis |first1=Nikolaos C. |last2=López-Cortés |first2=Andrés |last3=González |first3=Eduardo Vásconez |last4=Grimaldos |first4=Alejandra Barreto |last5=Prado |first5=Esteban Ortiz |title=SARS-CoV-2 vaccines strategies: a comprehensive review of phase 3 candidates |journal=npj Vaccines |date=December 2021 |volume=6 |issue=1 |pages=28 |doi=10.1038/s41541-021-00292-w}}</ref> A [[subgenus]] of the [[betacoronavirus]]es, known as [[embecovirus]]es (not including [[SARSr-CoV|SARS-like]] coronaviruses), have an additional shorter surface protein known as [[hemagglutinin esterase]].<ref name="woo_2010">{{cite journal |last1=Woo |first1=Patrick C. Y. |last2=Huang |first2=Yi |last3=Lau |first3=Susanna K. P. |last4=Yuen |first4=Kwok-Yung |title=Coronavirus Genomics and Bioinformatics Analysis |journal=Viruses |date=24 August 2010 |volume=2 |issue=8 |pages=1804–1820 |doi=10.3390/v2081803}}</ref>
⚫
[[Retrovirus]]es such as the [[human immunodeficiency virus]] (HIV) have surface peplomers.<ref name=burrell_2016 />{{rp|318–25}} These are [[protein complex]]es formed by two proteins, [[gp41]] and [[gp120]], both expressed from the ''[[env (gene)|env]]'' gene, collectively forming a spike protein complex that mediates viral entry.<ref name="mao_2012">{{cite journal |last1=Mao |first1=Youdong |last2=Wang |first2=Liping |last3=Gu |first3=Christopher |last4=Herschhorn |first4=Alon |last5=Xiang |first5=Shi-Hua |last6=Haim |first6=Hillel |last7=Yang |first7=Xinzhen |last8=Sodroski |first8=Joseph |title=Subunit organization of the membrane-bound HIV-1 envelope glycoprotein trimer |journal=Nature Structural & Molecular Biology |date=September 2012 |volume=19 |issue=9 |pages=893–899 |doi=10.1038/nsmb.2351|pmid=22864288 |pmc=3443289 }}</ref>
⚫
* Most [[influenza virus]] subgroups have two surface proteins described as peplomers, [[neuraminidase]] (an [[enzyme]]) and [[hemagglutinin (influenza)|hemagglutinin]] (also a class I fusion protein). Some instead have a single hemagglutinin esterase protein with both functions.<ref name=burrell_2016 />{{rp|356-9}}
⚫
* [[Retrovirus]]es such as the [[human immunodeficiency virus]] (HIV) have surface peplomers.<ref name=burrell_2016 />{{rp|318-25}} These are [[protein complex]]es formed by two proteins, [[gp41]] and [[gp120]], both expressed from the ''[[env (gene)|env]]'' gene, collectively forming a spike protein complex that mediates viral entry.<ref name="mao_2012">{{cite journal |last1=Mao |first1=Youdong |last2=Wang |first2=Liping |last3=Gu |first3=Christopher |last4=Herschhorn |first4=Alon |last5=Xiang |first5=Shi-Hua |last6=Haim |first6=Hillel |last7=Yang |first7=Xinzhen |last8=Sodroski |first8=Joseph |title=Subunit organization of the membrane-bound HIV-1 envelope glycoprotein trimer |journal=Nature Structural & Molecular Biology |date=September 2012 |volume=19 |issue=9 |pages=893–899 |doi=10.1038/nsmb.2351}}</ref>


===Gallery===
{{Gallery
{{Gallery
| title = Examples of [[electron micrograph]]s of viruses with surface spikes
| title = [[Electron micrograph]]s of viruses with surface spikes
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==References==
==References==
{{reflist}}
{{reflist}}

{{Use dmy dates|date=December 2020}}


[[Category:Virology]]
[[Category:Virology]]

Revision as of 01:27, 23 December 2023

For the spike protein in coronaviruses, see Coronavirus spike protein.
Coronavirus spike proteins (turquoise) projecting from the surface of SARS-CoV-2, the virus that causes COVID-19. The protein is glycosylated and its glycans are shown in orange.[1]
3D print of one of the trimeric spikes of SARS-CoV-2

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][3]: 29–33  The proteins are usually glycoproteins that form dimers or trimers.[3]: 29–33  [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] "robe or cloak",[6] 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][7][8] More recently, the term "peplos" is considered a synonym for viral envelope.[6]: 362 

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 that anchors the protein in the viral envelope, 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  They are usually glycoproteins, more commonly via N-linked than O-linked glycosylation.[3]: 33 

Functions

Spikes typically have a role in viral entry. They may interact with cell-surface receptors located on the host cell and may have hemagglutinizing activity as a result, or in other cases they may be enzymes.[6]: 362  For example, influenza virus has two surface proteins with these two functions, hemagglutinin and neuraminidase.[6]: 329  The binding site for the cell-surface receptor is usually located at the tip of the spike.[3]: 33  Many spike proteins are membrane fusion proteins.[9] Being exposed on the surface of the virion, spike proteins can be antigens.[6]: 362 

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

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.[10] 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.[11][12] A subgenus of the betacoronaviruses, known as embecoviruses (not including SARS-like coronaviruses), have an additional shorter surface protein known as hemagglutinin esterase.[13]

The COVID-19 pandemic necessitated identification of viral particles in electron micrographs of patient tissue samples. A number of reports misidentified normal subcellular structures as coronaviruses due to their superficial resemblance to coronavirus morphology, and because the distinctive spikes of coronaviruses are apparent by negative stain but much less visible in thin section.[14]

Influenza viruses

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

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.[15]

Electron micrographs of viruses with surface spikes

See also

References

  1. ^ 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.
  2. ^ Saunders Comprehensive Veterinary Dictionary (3rd ed.). Elsevier, Inc. 2007. as cited in "peplomer". The Free Dictionary. Farlex. 2011. Retrieved 30 March 2011.
  3. ^ a b c d e f g h i Burrell, Christopher J. (2016). Fenner and White's medical virology (Fifth ed.). London, United Kingdom. ISBN 978-0123751560.{{cite book}}: CS1 maint: location missing publisher (link)
  4. ^ 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. ISBN 9780128145166.
  5. ^ 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. PMID 5330240.
  6. ^ a b c d e Mahy, B. W. J. (2009). The dictionary of virology (4th ed.). Amsterdam: Elsevier/Academic Press. ISBN 9780080920368.
  7. ^ Lwoff, A; Horne, RW; Tournier, P (13 June 1962). "[A virus system]". Comptes rendus hebdomadaires des séances de l'Académie des sciences. 254: 4225–7. PMID 14467544.
  8. ^ Lwoff, A.; Horne, R.; Tournier, P. (1 January 1962). "A System of Viruses". Cold Spring Harbor Symposia on Quantitative Biology. 27: 51–55. doi:10.1101/sqb.1962.027.001.008. PMID 13931895.
  9. ^ Harrison, Stephen C. (May 2015). "Viral membrane fusion". Virology. 479–480: 498–507. doi:10.1016/j.virol.2015.03.043. PMC 4424100. PMID 25866377.
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