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Membrane fusion protein

December 02, 2023

Membrane fusion proteins (not to be confused with chimeric or fusion proteins) are proteins that cause fusion of biological membranes. Membrane fusion is critical for many biological processes, especially in eukaryotic development and viral entry. Fusion proteins can originate from genes encoded by infectious enveloped viruses, ancient retroviruses integrated into the host genome,[1] or solely by the host genome.[2] Post-transcriptional modifications made to the fusion proteins by the host, namely addition and modification of glycans and acetyl groups, can drastically affect fusogenicity (the ability to fuse).[3]

Fusion in eukaryotes edit

Eukaryotic genomes contain several gene families, of host and viral origin, which encode products involved in driving membrane fusion. While adult somatic cells do not typically undergo membrane fusion under normal conditions, gametes and embryonic cells follow developmental pathways to non-spontaneously drive membrane fusion, such as in placental formation, syncytiotrophoblast formation, and neurodevelopment. Fusion pathways are also involved in the development of musculoskeletal and nervous system tissues. Vesicle fusion events involved in neurotransmitter trafficking also relies on the catalytic activity of fusion proteins.

SNARE family edit

The SNARE family include bona fide eukaryotic fusion proteins. They are only found in eukaryotes and their closest archaeal relatives like Heimdallarchaeota.[4]

Retroviral edit

These proteins originate from the env gene of endogenous retroviruses. They are domesticated viral class I fusion proteins.

HAP2 family edit

HAP2 is a domesticated viral class II fusion protein found in diverse eukaryotes including Toxoplasma, vascular plants, and fruit flies. This protein is essential for gamete fusion in these organisms.[5]

Pathogenic viral fusion edit

Enveloped viruses readily overcome the thermodynamic barrier of merging two plasma membranes by storing kinetic energy in fusion (F) proteins. F proteins can be independently expressed on host cell surfaces which can either (1) drive the infected cell to fuse with neighboring cells, forming a syncytium, or (2) be incorporated into a budding virion from the infected cell which leads to the full emancipation of plasma membrane from the host cell. Some F components solely drive fusion while a subset of F proteins can interact with host factors. There are four groups of fusion proteins categorized by their structure and mechanism of fusion.[6]

Class I edit

Class I fusion proteins resemble influenzavirus hemagglutinin in their structure. Post-fusion, the active site has a trimer of α-helical coiled-coils. The binding domain is rich in α-helices and hydrophobic fusion peptides located near the N-terminus. Fusion conformation change can often be controlled by pH.[7][8]

Class II edit

Class II proteins are dominant in β-sheets and the catalytic sites are localized in the core region. The peptide regions required to drive fusion are formed from the turns between the β-sheets.[7][8]

Class III edit

Class III fusion proteins are distinct from I and II. They typically consist of 5 structural domains, where domain 1 and 2 localized to the C-terminal end often contain more β-sheets and domains 2-5 closer to the N-terminal side are richer in α-helices. In the pre-fusion state, the later domains nest and protect domain 1 (i.e. domain 1 is protected by domain 2, which is nested in domain 3, which is protected by domain 4). Domain 1 contains the catalytic site for membrane fusion.[7][8]

Class IV edit

Class IV fusion proteins, better known as fusion-associated small transmembrane proteins (FAST), are the smallest type of fusion protein. They are found in reoviruses, which are non-enveloped viruses and are specialized for cell-cell rather than virus-cell fusion, forming syncytia. They are the only known membrane fusion proteins found in non-enveloped viruses.[9][10]

Examples edit

See also edit

References edit

  1. ^ Classification of viral fusion proteins in TCDB database
  2. ^ Klapper R, Stute C, Schomaker O, Strasser T, Janning W, Renkawitz-Pohl R, Holz A (January 2002). "The formation of syncytia within the visceral musculature of the Drosophila midgut is dependent on duf, sns and mbc". Mechanisms of Development. 110 (1–2): 85–96. doi:10.1016/S0925-4773(01)00567-6. PMID 11744371.
  3. ^ Ortega V, Stone JA, Contreras EM, Iorio RM, Aguilar HC (January 2019). "Addicted to sugar: roles of glycans in the order Mononegavirales". Glycobiology. 29 (1): 2–21. doi:10.1093/glycob/cwy053. PMC 6291800. PMID 29878112.
  4. ^ Neveu E, Khalifeh D, Salamin N, Fasshauer D (July 2020). "Prototypic SNARE Proteins Are Encoded in the Genomes of Heimdallarchaeota, Potentially Bridging the Gap between the Prokaryotes and Eukaryotes". Current Biology. 30 (13): 2468–2480.e5. doi:10.1016/j.cub.2020.04.060. PMID 32442459. S2CID 218762979.
  5. ^ Fédry J, Liu Y, Péhau-Arnaudet G, Pei J, Li W, Tortorici MA, et al. (February 2017). "The Ancient Gamete Fusogen HAP2 Is a Eukaryotic Class II Fusion Protein". Cell. 168 (5): 904–915.e10. doi:10.1016/j.cell.2017.01.024. PMC 5332557. PMID 28235200.
  6. ^ a b c d e f g h i Podbilewicz, Benjamin (11 October 2014). "Virus and Cell Fusion Mechanisms". Annual Review of Cell and Developmental Biology. 30 (1): 111–139. doi:10.1146/annurev-cellbio-101512-122422. PMID 25000995.
  7. ^ a b c Backovic M, Jardetzky TS (April 2009). "Class III viral membrane fusion proteins". Current Opinion in Structural Biology. 19 (2): 189–96. doi:10.1016/j.sbi.2009.02.012. PMC 3076093. PMID 19356922.
  8. ^ a b c White JM, Delos SE, Brecher M, Schornberg K (2008). "Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme". Critical Reviews in Biochemistry and Molecular Biology. 43 (3): 189–219. doi:10.1080/10409230802058320. PMC 2649671. PMID 18568847.
  9. ^ Shmulevitz, Maya; Duncan, Roy (1 March 2000). "A new class of fusion-associated small transmembrane (FAST) proteins encoded by the non-enveloped fusogenic reoviruses". The EMBO Journal. 19 (5): 902–912. doi:10.1093/emboj/19.5.902. PMC 305630. PMID 10698932.
  10. ^ a b Ciechonska, Marta; Duncan, Roy (December 2014). "Reovirus FAST proteins: virus-encoded cellular fusogens". Trends in Microbiology. 22 (12): 715–724. doi:10.1016/j.tim.2014.08.005. PMID 25245455.
  11. ^ Li, Fang (29 September 2016). "Structure, Function, and Evolution of Coronavirus Spike Proteins". Annual Review of Virology. 3 (1): 237–261. doi:10.1146/annurev-virology-110615-042301. PMC 5457962. PMID 27578435.
  12. ^ Zhu, Chaogeng; He, Guiyun; Yin, Qinqin; Zeng, Lin; Ye, Xiangli; Shi, Yongzhong; Xu, Wei (October 2021). "Molecular biology of the SARs‐CoV‐2 spike protein: A review of current knowledge". Journal of Medical Virology. 93 (10): 5729–5741. doi:10.1002/jmv.27132. PMC 8427004. PMID 34125455.
  13. ^ a b c d e White, Judith M.; Whittaker, Gary R. (June 2016). "Fusion of Enveloped Viruses in Endosomes". Traffic. 17 (6): 593–614. doi:10.1111/tra.12389. PMC 4866878. PMID 26935856.
  14. ^ a b Baquero, Eduard; Albertini, Aurélie AV; Gaudin, Yves (August 2015). "Recent mechanistic and structural insights on class III viral fusion glycoproteins". Current Opinion in Structural Biology. 33: 52–60. doi:10.1016/j.sbi.2015.07.011. PMID 26277251.

External links edit

December 02, 2023
membrane, fusion, protein, confused, with, chimeric, fusion, proteins, proteins, that, cause, fusion, biological, membranes, membrane, fusion, critical, many, biological, processes, especially, eukaryotic, development, viral, entry, fusion, proteins, originate. Membrane fusion proteins not to be confused with chimeric or fusion proteins are proteins that cause fusion of biological membranes Membrane fusion is critical for many biological processes especially in eukaryotic development and viral entry Fusion proteins can originate from genes encoded by infectious enveloped viruses ancient retroviruses integrated into the host genome 1 or solely by the host genome 2 Post transcriptional modifications made to the fusion proteins by the host namely addition and modification of glycans and acetyl groups can drastically affect fusogenicity the ability to fuse 3 Contents 1 Fusion in eukaryotes 1 1 SNARE family 1 2 Retroviral 1 3 HAP2 family 2 Pathogenic viral fusion 2 1 Class I 2 2 Class II 2 3 Class III 2 4 Class IV 2 5 Examples 3 See also 4 References 5 External linksFusion in eukaryotes editEukaryotic genomes contain several gene families of host and viral origin which encode products involved in driving membrane fusion While adult somatic cells do not typically undergo membrane fusion under normal conditions gametes and embryonic cells follow developmental pathways to non spontaneously drive membrane fusion such as in placental formation syncytiotrophoblast formation and neurodevelopment Fusion pathways are also involved in the development of musculoskeletal and nervous system tissues Vesicle fusion events involved in neurotransmitter trafficking also relies on the catalytic activity of fusion proteins SNARE family edit The SNARE family include bona fide eukaryotic fusion proteins They are only found in eukaryotes and their closest archaeal relatives like Heimdallarchaeota 4 Retroviral edit These proteins originate from the env gene of endogenous retroviruses They are domesticated viral class I fusion proteins Syncytins are responsible for structures of the placenta Syncytin 1 Syncytin 2 ERV3 is not functional in humansHAP2 family edit HAP2 is a domesticated viral class II fusion protein found in diverse eukaryotes including Toxoplasma vascular plants and fruit flies This protein is essential for gamete fusion in these organisms 5 Pathogenic viral fusion editEnveloped viruses readily overcome the thermodynamic barrier of merging two plasma membranes by storing kinetic energy in fusion F proteins F proteins can be independently expressed on host cell surfaces which can either 1 drive the infected cell to fuse with neighboring cells forming a syncytium or 2 be incorporated into a budding virion from the infected cell which leads to the full emancipation of plasma membrane from the host cell Some F components solely drive fusion while a subset of F proteins can interact with host factors There are four groups of fusion proteins categorized by their structure and mechanism of fusion 6 Class I edit Class I fusion proteins resemble influenzavirus hemagglutinin in their structure Post fusion the active site has a trimer of a helical coiled coils The binding domain is rich in a helices and hydrophobic fusion peptides located near the N terminus Fusion conformation change can often be controlled by pH 7 8 Class II edit Class II proteins are dominant in b sheets and the catalytic sites are localized in the core region The peptide regions required to drive fusion are formed from the turns between the b sheets 7 8 Class III edit Class III fusion proteins are distinct from I and II They typically consist of 5 structural domains where domain 1 and 2 localized to the C terminal end often contain more b sheets and domains 2 5 closer to the N terminal side are richer in a helices In the pre fusion state the later domains nest and protect domain 1 i e domain 1 is protected by domain 2 which is nested in domain 3 which is protected by domain 4 Domain 1 contains the catalytic site for membrane fusion 7 8 Class IV edit Class IV fusion proteins better known as fusion associated small transmembrane proteins FAST are the smallest type of fusion protein They are found in reoviruses which are non enveloped viruses and are specialized for cell cell rather than virus cell fusion forming syncytia They are the only known membrane fusion proteins found in non enveloped viruses 9 10 Examples edit Fusion protein Abbreviation Class Virus family Example viruses ReferenceCoronavirus spike protein S I Coronaviridae SARS CoV SARS CoV 2 11 12 Ebolavirus glycoprotein GP I Filoviridae Zaire Sudan ebolaviruses Marburgvirus 6 13 Glycoprotein 41 Gp41 I Retroviridae HIV 6 13 Hemagglutinin H HA HN I Orthomyxoviridae Paramyxoviridae Influenza virus measles virus mumps virus 6 13 Alphavirus envelope protein E1 E1 II Togaviridae Semliki Forest virus 6 13 Flavivirus envelope protein E II Flaviviridae Dengue virus West Nile virus 6 13 Herpesvirus glycoprotein B gB III Herpesviridae HSV 1 6 14 VSV G G III Rhabdoviridae Vesicular stomatitis virus rabies lyssavirus 6 14 Fusion associated small transmembrane protein FAST IV Reoviridae Avian orthoreovirus 6 10 See also editInterbilayer forces in membrane fusion Viral membrane fusion proteinsReferences edit Classification of viral fusion proteins in TCDB database Klapper R Stute C Schomaker O Strasser T Janning W Renkawitz Pohl R Holz A January 2002 The formation of syncytia within the visceral musculature of the Drosophila midgut is dependent on duf sns and mbc Mechanisms of Development 110 1 2 85 96 doi 10 1016 S0925 4773 01 00567 6 PMID 11744371 Ortega V Stone JA Contreras EM Iorio RM Aguilar HC January 2019 Addicted to sugar roles of glycans in the order Mononegavirales Glycobiology 29 1 2 21 doi 10 1093 glycob cwy053 PMC 6291800 PMID 29878112 Neveu E Khalifeh D Salamin N Fasshauer D July 2020 Prototypic SNARE Proteins Are Encoded in the Genomes of Heimdallarchaeota Potentially Bridging the Gap between the Prokaryotes and Eukaryotes Current Biology 30 13 2468 2480 e5 doi 10 1016 j cub 2020 04 060 PMID 32442459 S2CID 218762979 Fedry J Liu Y Pehau Arnaudet G Pei J Li W Tortorici MA et al February 2017 The Ancient Gamete Fusogen HAP2 Is a Eukaryotic Class II Fusion Protein Cell 168 5 904 915 e10 doi 10 1016 j cell 2017 01 024 PMC 5332557 PMID 28235200 a b c d e f g h i Podbilewicz Benjamin 11 October 2014 Virus and Cell Fusion Mechanisms Annual Review of Cell and Developmental Biology 30 1 111 139 doi 10 1146 annurev cellbio 101512 122422 PMID 25000995 a b c Backovic M Jardetzky TS April 2009 Class III viral membrane fusion proteins Current Opinion in Structural Biology 19 2 189 96 doi 10 1016 j sbi 2009 02 012 PMC 3076093 PMID 19356922 a b c White JM Delos SE Brecher M Schornberg K 2008 Structures and mechanisms of viral membrane fusion proteins multiple variations on a common theme Critical Reviews in Biochemistry and Molecular Biology 43 3 189 219 doi 10 1080 10409230802058320 PMC 2649671 PMID 18568847 Shmulevitz Maya Duncan Roy 1 March 2000 A new class of fusion associated small transmembrane FAST proteins encoded by the non enveloped fusogenic reoviruses The EMBO Journal 19 5 902 912 doi 10 1093 emboj 19 5 902 PMC 305630 PMID 10698932 a b Ciechonska Marta Duncan Roy December 2014 Reovirus FAST proteins virus encoded cellular fusogens Trends in Microbiology 22 12 715 724 doi 10 1016 j tim 2014 08 005 PMID 25245455 Li Fang 29 September 2016 Structure Function and Evolution of Coronavirus Spike Proteins Annual Review of Virology 3 1 237 261 doi 10 1146 annurev virology 110615 042301 PMC 5457962 PMID 27578435 Zhu Chaogeng He Guiyun Yin Qinqin Zeng Lin Ye Xiangli Shi Yongzhong Xu Wei October 2021 Molecular biology of the SARs CoV 2 spike protein A review of current knowledge Journal of Medical Virology 93 10 5729 5741 doi 10 1002 jmv 27132 PMC 8427004 PMID 34125455 a b c d e White Judith M Whittaker Gary R June 2016 Fusion of Enveloped Viruses in Endosomes Traffic 17 6 593 614 doi 10 1111 tra 12389 PMC 4866878 PMID 26935856 a b Baquero Eduard Albertini Aurelie AV Gaudin Yves August 2015 Recent mechanistic and structural insights on class III viral fusion glycoproteins Current Opinion in Structural Biology 33 52 60 doi 10 1016 j sbi 2015 07 011 PMID 26277251 External links editMembrane fusion proteins at the U S National Library of Medicine Medical Subject Headings MeSH Retrieved from https en wikipedia org w index php title Membrane fusion protein amp oldid 1152499965, wikipedia, wiki, book, books, library,

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