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Home / Equine Research Bank / PLoS One / Computational modelling of the equine arteritis virus GP5/M ...
PloS one2026; 21(3); e0344287; doi: 10.1371/journal.pone.0344287

Computational modelling of the equine arteritis virus GP5/M Dimer: Implications for immune evasion and virulence.

Abstract: Equine arteritis virus (EAV) is a positive-stranded RNA virus of the Arteriviridae family. Its GP5/M dimer, the principal component of the viral envelope, mediates virus budding and serves as a key target for neutralizing antibodies. Using AlphaFold3, we predicted the 3D structure of the EAV GP5/M dimer and compared it to its homolog in porcine reproductive and respiratory syndrome virus (PRRSV). Both complexes share a conserved architecture comprising a short ectodomain, three helical transmembrane regions, and a β-sheet-rich endodomain. EAV GP5 features a longer ectodomain with four α-helices and a disulfide-linked β-sheet, which forms the most variable and surface-exposed region containing neutralizing epitopes. Adjacent conserved and variable N-glycosylation sites suggest immune evasion mechanisms involving antigenic drift and glycan shielding. Another epitope, located in a membrane-proximal helix, overlaps with known virulence and persistence determinants. The transmembrane domains are the most structurally conserved regions between EAV and PRRSV, characterized by tilted and kinked helices stabilized by hydrophilic interactions within the lipid bilayer. These findings provide molecular insights into the structural organization, immune targets, and virulence-associated features of the GP5/M dimer, offering a foundation for rational vaccine design against EAV.
Copyright: © 2026 Veit, Matczuk. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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Publication Date: 2026-03-10 PubMed ID: 41805756PubMed Central: PMC12974795DOI: 10.1371/journal.pone.0344287Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

Overview

  • This research focuses on computationally predicting the 3D structure of the equine arteritis virus (EAV) GP5/M dimer using AlphaFold3.
  • The study compares this structure to a similar protein in a related virus, revealing insights into immune evasion, virus structure, and virulence.

Background and Significance

  • Equine arteritis virus (EAV): A positive-stranded RNA virus within the Arteriviridae family that infects horses and causes respiratory and reproductive disease.
  • GP5/M dimer: The main protein complex embedded in the viral envelope, responsible for virus budding from the host cell and serving as a primary target for the host’s neutralizing antibodies.
  • Understanding the structure of GP5/M can reveal how the virus interacts with the host immune system and how it maintains virulence.

Methodology

  • Structural prediction: Utilized AlphaFold3, an advanced machine-learning tool for protein folding, to predict the 3D structure of the EAV GP5/M dimer.
  • Comparative analysis: Compared the EAV GP5/M structure with its homologous complex from porcine reproductive and respiratory syndrome virus (PRRSV), another arterivirus with similar structural features.

Key Structural Features Identified

  • General architecture: Both EAV and PRRSV GP5/M dimers share a conserved overall structure including:
    • A short ectodomain (portion of protein outside the viral membrane)
    • Three helical transmembrane regions (spanning the viral membrane)
    • A β-sheet-rich endodomain (portion inside the viral membrane or cytoplasmic side)
  • Ectodomain of EAV GP5:
    • Longer than that in PRRSV
    • Contains four α-helices and a disulfide-linked β-sheet structure
    • Forms the most variable and surface-exposed region, which harbors neutralizing antibody epitopes
  • N-glycosylation sites:
    • Conserved and variable sites are located adjacent to the neutralizing epitopes
    • These glycans likely contribute to immune evasion via:
      • Antigenic drift – the accumulation of mutations to escape antibody recognition
      • Glycan shielding – sugar molecules physically blocking antibody access
  • Membrane-proximal helix epitope:
    • Located near the viral membrane surface
    • Overlaps with regions known to influence viral virulence and persistence in the host
  • Transmembrane domain conservation:
    • Most structurally conserved part between EAV and PRRSV
    • Consists of tilted and kinked α-helices
    • Stabilized by hydrophilic interactions within the lipid bilayer, maintaining protein integrity

Biological and Clinical Implications

  • Immune evasion: The arrangement of glycosylation sites and variable ectodomain structures suggest mechanisms by which EAV avoids detection by host antibodies.
  • Virulence factors: Specific structural epitopes correspond to viral features that modulate how aggressively EAV infects and persists in its host.
  • Vaccine design potential:
    • Knowing the detailed 3D structure of the GP5/M dimer provides a blueprint for designing vaccines that target conserved and vulnerable viral regions.
    • Insights into glycan shielding and epitope variation can guide strategies to produce broadly neutralizing vaccine candidates.

Conclusion

  • The research delivers a high-resolution structural model of the EAV GP5/M dimer, highlighting its key functional and immunological features.
  • These findings offer foundational knowledge useful for understanding virus-host interactions and steering future efforts in antiviral therapies and vaccine development against EAV.

Cite This Article

APA
Veit M, Matczuk AK. (2026). Computational modelling of the equine arteritis virus GP5/M Dimer: Implications for immune evasion and virulence. PLoS One, 21(3), e0344287. https://doi.org/10.1371/journal.pone.0344287

Publication

PloS one
ISSN: 1932-6203
NlmUniqueID: 101285081
Country: United States
Language: English
Volume: 21
Issue: 3
Pages: e0344287
PII: e0344287

Researcher Affiliations

Veit, Michael
  • Institut für Virologie, Veterinärmedizin, Freie Universität Berlin, Berlin, Germany.
Matczuk, Anna Karolina
  • Division of Microbiology, Department of Pathology, Faculty of Veterinary Medicine, Wrocław University of Environmental and Life Sciences, Wrocław, Poland.

MeSH Terms

  • Equartevirus / pathogenicity
  • Equartevirus / immunology
  • Equartevirus / chemistry
  • Immune Evasion
  • Viral Envelope Proteins / chemistry
  • Viral Envelope Proteins / immunology
  • Protein Multimerization
  • Animals
  • Models, Molecular
  • Virulence
  • Horses
  • Amino Acid Sequence
  • Computer Simulation
  • Porcine respiratory and reproductive syndrome virus / immunology
  • Porcine respiratory and reproductive syndrome virus / chemistry
  • Epitopes / immunology
  • Epitopes / chemistry

Conflict of Interest Statement

The authors have declared that no competing interests exist.

References

This article includes 73 references
  1. Balasuriya UBR. Equine viral arteritis. Vet Clin North Am Equine Pract 2014;30(3):543–60.
    doi: 10.1016/j.cveq.2014.08.011pubmed: 25441113google scholar: lookup
  2. Bailey AL, Lauck M, Sibley SD, Friedrich TC, Kuhn JH, Freimer NB. Zoonotic Potential of Simian Arteriviruses. J Virol 2016;90(2):630–5.
    pmc: PMC4702702pubmed: 26559828
  3. Bailey AL, Lauck M, Weiler A, Sibley SD, Dinis JM, Bergman Z. High genetic diversity and adaptive potential of two simian hemorrhagic fever viruses in a wild primate population. PLoS One 2014;9(3):e90714.
    doi: 10.1371/journal.pone.0090714pmc: PMC3961216pubmed: 24651479google scholar: lookup
  4. Brinton MA, Di H, Vatter HA. Simian hemorrhagic fever virus: Recent advances. Virus Res 2015;202:112–9.
    doi: 10.1016/j.virusres.2014.11.024pmc: PMC4449332pubmed: 25455336google scholar: lookup
  5. Lauck M, Hyeroba D, Tumukunde A, Weny G, Lank SM, Chapman CA. Novel, divergent simian hemorrhagic fever viruses in a wild Ugandan red colobus monkey discovered using direct pyrosequencing. PLoS One 2011;6(4):e19056.
    doi: 10.1371/journal.pone.0019056pmc: PMC3081318pubmed: 21544192google scholar: lookup
  6. Kuhn JH, Lauck M, Bailey AL, Shchetinin AM, Vishnevskaya TV, Bào Y. Reorganization and expansion of the nidoviral family Arteriviridae. Arch Virol 2016;161(3):755–68.
    doi: 10.1007/s00705-015-2672-zpmc: PMC5573231pubmed: 26608064google scholar: lookup
  7. Snijder EJ, Kikkert M, Fang Y. Arterivirus molecular biology and pathogenesis. J Gen Virol 2013;94(Pt 10):2141–63.
    doi: 10.1099/vir.0.056341-0pubmed: 23939974google scholar: lookup
  8. Snijder EJ, Meulenberg JJ. The molecular biology of arteriviruses. J Gen Virol 1998;79 (Pt 5):961–79.
    doi: 10.1099/0022-1317-79-5-961pubmed: 9603311google scholar: lookup
  9. Warren CJ, Yu S, Peters DK, Barbachano-Guerrero A, Yang Q, Burris BL. Primate hemorrhagic fever-causing arteriviruses are poised for spillover to humans. Cell 2022;185(21):3980-3991.e18.
    doi: 10.1016/j.cell.2022.09.022pmc: PMC9588614pubmed: 36182704google scholar: lookup
  10. Balasuriya UBR, Go YY, MacLachlan NJ. Equine arteritis virus. Vet Microbiol 2013;167(1–2):93–122.
    doi: 10.1016/j.vetmic.2013.06.015pmc: PMC7126873pubmed: 23891306google scholar: lookup
  11. MacLachlan NJ, Balasuriya UB. Equine viral arteritis. Adv Exp Med Biol 2006;581:429–33.
    doi: 10.1007/978-0-387-33012-9_77pmc: PMC7123899pubmed: 17037573google scholar: lookup
  12. Bhat S, Karunakaran S, Frossard JP, Choudhury B, Steinbach F. Genetic characterization of equine arteritis virus associated with outbreaks in the UK, 2019. J Gen Virol 2025;106(12).
    pmc: PMC12674535pubmed: 41334982
  13. Franco JJ, Gonzálvez M, Cano-Terriza D, Barbero-Moyano J, Jose-Cunilleras E, Alguacil E. Equine viral arteritis: Seroprevalence patterns and risk factors in equids from western Europe. Res Vet Sci 2025;192:105701.
    doi: 10.1016/j.rvsc.2025.105701pubmed: 40424736google scholar: lookup
  14. Minke JM, Audonnet J-C, Fischer L. Equine viral vaccines: the past, present and future. Vet Res 2004;35(4):425–43.
    doi: 10.1051/vetres:2004019pubmed: 15236675google scholar: lookup
  15. Miszczak F, Legrand L, Balasuriya UBR, Ferry-Abitbol B, Zhang J, Hans A. Emergence of novel equine arteritis virus (EAV) variants during persistent infection in the stallion: origin of the 2007 French EAV outbreak was linked to an EAV strain present in the semen of a persistently infected carrier stallion. Virology 2012;423(2):165–74.
    doi: 10.1016/j.virol.2011.11.028pubmed: 22209234google scholar: lookup
  16. Otzdorff C, Beckmann J, Goehring LS. Equine Arteritis Virus (EAV) Outbreak in a Show Stallion Population. Viruses 2021;13(11):2142.
    doi: 10.3390/v13112142pmc: PMC8621670pubmed: 34834949google scholar: lookup
  17. Dokland T. The structural biology of PRRSV. Virus Res 2010;154(1–2):86–97.
    doi: 10.1016/j.virusres.2010.07.029pmc: PMC7114433pubmed: 20692304google scholar: lookup
  18. Veit M, Matczuk AK, Sinhadri BC, Krause E, Thaa B. Membrane proteins of arterivirus particles: structure, topology, processing and function. Virus Res 2014;194:16–36.
    doi: 10.1016/j.virusres.2014.09.010pmc: PMC7172906pubmed: 25278143google scholar: lookup
  19. Wieringa R, de Vries AAF, van der Meulen J, Godeke G-J, Onderwater JJM, van Tol H. Structural protein requirements in equine arteritis virus assembly. J Virol 2004;78(23):13019–27.
    doi: 10.1128/JVI.78.23.13019-13027.2004pmc: PMC524988pubmed: 15542653google scholar: lookup
  20. Wissink EHJ, Kroese MV, van Wijk HAR, Rijsewijk FAM, Meulenberg JJM, Rottier PJM. Envelope protein requirements for the assembly of infectious virions of porcine reproductive and respiratory syndrome virus. J Virol 2005;79(19):12495–506.
    doi: 10.1128/JVI.79.19.12495-12506.2005pmc: PMC1211556pubmed: 16160177google scholar: lookup
  21. Dobbe JC, van der Meer Y, Spaan WJ, Snijder EJ. Construction of chimeric arteriviruses reveals that the ectodomain of the major glycoprotein is not the main determinant of equine arteritis virus tropism in cell culture. Virology 2001;288(2):283–94.
    doi: 10.1006/viro.2001.1074pubmed: 11601900google scholar: lookup
  22. Tian D, Wei Z, Zevenhoven-Dobbe JC, Liu R, Tong G, Snijder EJ. Arterivirus minor envelope proteins are a major determinant of viral tropism in cell culture. J Virol 2012;86(7):3701–12.
    doi: 10.1128/JVI.06836-11pmc: PMC3302522pubmed: 22258262google scholar: lookup
  23. Verheije MH, Welting TJM, Jansen HT, Rottier PJM, Meulenberg JJM. Chimeric arteriviruses generated by swapping of the M protein ectodomain rule out a role of this domain in viral targeting. Virology 2002;303(2):364–73.
    doi: 10.1006/viro.2002.1711pubmed: 12490397google scholar: lookup
  24. Maloney SM, Shaw TM, Nennig KM, Larsen MS, Shah A, Kumar A. CD81 is a receptor for equine arteritis virus (family: Arteriviridae). mBio 2025;16(7):e0062325.
    pmc: PMC12239600pubmed: 40422661
  25. Shaw TM, Huey D, Mousa-Makky M, Compaleo J, Nennig K, Shah AP. The neonatal Fc receptor (FcRn) is a pan-arterivirus receptor. Nat Commun 2024;15(1):6726.
    doi: 10.1038/s41467-024-51142-xpmc: PMC11306234pubmed: 39112502google scholar: lookup
  26. Yang K, Dong J, Li J, Zhou R, Jia X, Sun Z. The neonatal Fc receptor (FcRn) is required for porcine reproductive and respiratory syndrome virus uncoating. J Virol 2025;99(1):e0121824.
    doi: 10.1128/jvi.01218-24pmc: PMC11784455pubmed: 39651859google scholar: lookup
  27. Das PB, Dinh PX, Ansari IH, de Lima M, Osorio FA, Pattnaik AK. The minor envelope glycoproteins GP2a and GP4 of porcine reproductive and respiratory syndrome virus interact with the receptor CD163. J Virol 2010;84(4):1731–40.
    doi: 10.1128/JVI.01774-09pmc: PMC2812361pubmed: 19939927google scholar: lookup
  28. de Vries AA, Chirnside ED, Horzinek MC, Rottier PJ. Structural proteins of equine arteritis virus. J Virol 1992;66(11):6294–303.
    doi: 10.1128/JVI.66.11.6294-6303.1992pmc: PMC240121pubmed: 1328669google scholar: lookup
  29. de Vries AA, Post SM, Raamsman MJ, Horzinek MC, Rottier PJ. The two major envelope proteins of equine arteritis virus associate into disulfide-linked heterodimers. J Virol 1995;69(8):4668–74.
    doi: 10.1128/JVI.69.8.4668-4674.1995pmc: PMC189270pubmed: 7609031google scholar: lookup
  30. Thaa B, Kaufer S, Neumann SA, Peibst B, Nauwynck H, Krause E. The complex co-translational processing of glycoprotein GP5 of type 1 porcine reproductive and respiratory syndrome virus. Virus Res 2017;240:112–20.
    doi: 10.1016/j.virusres.2017.08.004pubmed: 28807563google scholar: lookup
  31. Thaa B, Sinhadri BC, Tielesch C, Krause E, Veit M. Signal peptide cleavage from GP5 of PRRSV: a minor fraction of molecules retains the decoy epitope, a presumed molecular cause for viral persistence. PLoS One 2013;8(6):e65548.
    doi: 10.1371/journal.pone.0065548pmc: PMC3675037pubmed: 23755249google scholar: lookup
  32. Veit M, Gadalla MR, Zhang M. Using Alphafold2 to Predict the Structure of the Gp5/M Dimer of Porcine Respiratory and Reproductive Syndrome Virus. Int J Mol Sci 2022;23(21).
    pmc: PMC9653971pubmed: 36361998
  33. Snijder EJ, Dobbe JC, Spaan WJM. Heterodimerization of the two major envelope proteins is essential for arterivirus infectivity. J Virol 2003;77(1):97–104.
    doi: 10.1128/jvi.77.1.97-104.2003pmc: PMC140607pubmed: 12477814google scholar: lookup
  34. Zhang M, Han X, Osterrieder K, Veit M. Palmitoylation of the envelope membrane proteins GP5 and M of porcine reproductive and respiratory syndrome virus is essential for virus growth. PLoS Pathog 2021;17(4):e1009554.
    doi: 10.1371/journal.ppat.1009554pmc: PMC8099100pubmed: 33891658google scholar: lookup
  35. Balasuriya UBR, Dobbe JC, Heidner HW, Smalley VL, Navarrette A, Snijder EJ. Characterization of the neutralization determinants of equine arteritis virus using recombinant chimeric viruses and site-specific mutagenesis of an infectious cDNA clone. Virology 2004;321(2):235–46.
    doi: 10.1016/j.virol.2003.12.015pubmed: 15051384google scholar: lookup
  36. Balasuriya UB, Patton JF, Rossitto PV, Timoney PJ, McCollum WH, MacLachlan NJ. Neutralization determinants of laboratory strains and field isolates of equine arteritis virus: identification of four neutralization sites in the amino-terminal ectodomain of the G(L) envelope glycoprotein. Virology 1997;232(1):114–28.
    doi: 10.1006/viro.1997.8551pubmed: 9185595google scholar: lookup
  37. Balasuriya UB, Rossitto PV, DeMaula CD, MacLachlan NJ. A 29K envelope glycoprotein of equine arteritis virus expresses neutralization determinants recognized by murine monoclonal antibodies. J Gen Virol 1993;74 (Pt 11):2525–9.
    doi: 10.1099/0022-1317-74-11-2525pubmed: 7504076google scholar: lookup
  38. Chirnside ED, de Vries AA, Mumford JA, Rottier PJ. Equine arteritis virus-neutralizing antibody in the horse is induced by a determinant on the large envelope glycoprotein GL. J Gen Virol 1995;76 (Pt 8):1989–98.
    doi: 10.1099/0022-1317-76-8-1989pubmed: 7636479google scholar: lookup
  39. Mayers J, Westcott D, Steinbach F. Identification of Equine Arteritis Virus Immunodominant Epitopes Using a Peptide Microarray. Viruses 2022;14(9):1880.
    doi: 10.3390/v14091880pmc: PMC9502512pubmed: 36146687google scholar: lookup
  40. Balasuriya UB, Carossino M. Reproductive effects of arteriviruses: equine arteritis virus and porcine reproductive and respiratory syndrome virus infections. Curr Opin Virol 2017;27:57–70.
    doi: 10.1016/j.coviro.2017.11.005pubmed: 29172072google scholar: lookup
  41. Fiers J, Cay AB, Maes D, Tignon M. A Comprehensive Review on Porcine Reproductive and Respiratory Syndrome Virus with Emphasis on Immunity. Vaccines (Basel) 2024;12(8):942.
    doi: 10.3390/vaccines12080942pmc: PMC11359659pubmed: 39204065google scholar: lookup
  42. Balasuriya UBR, MacLachlan NJ. The immune response to equine arteritis virus: potential lessons for other arteriviruses. Vet Immunol Immunopathol 2004;102(3):107–29.
    doi: 10.1016/j.vetimm.2004.09.003pubmed: 15507299google scholar: lookup
  43. Balasuriya UBR, Zhang J, Go YY, MacLachlan NJ. Experiences with infectious cDNA clones of equine arteritis virus: lessons learned and insights gained. Virology 2014;462–463:388–403.
    doi: 10.1016/j.virol.2014.04.029pmc: PMC7172799pubmed: 24913633google scholar: lookup
  44. Jumper J, Evans R, Pritzel A, Green T, Figurnov M, Ronneberger O. Applying and improving AlphaFold at CASP14. Proteins 2021;89(12):1711–21.
    doi: 10.1002/prot.26257pmc: PMC9299164pubmed: 34599769google scholar: lookup
  45. Jumper J, Evans R, Pritzel A, Green T, Figurnov M, Ronneberger O. Highly accurate protein structure prediction with AlphaFold. Nature 2021;596(7873):583–9.
    doi: 10.1038/s41586-021-03819-2pmc: PMC8371605pubmed: 34265844google scholar: lookup
  46. Abramson J, Adler J, Dunger J, Evans R, Green T, Pritzel A. Accurate structure prediction of biomolecular interactions with AlphaFold 3. Nature 2024;630(8016):493–500.
    doi: 10.1038/s41586-024-07487-wpmc: PMC11168924pubmed: 38718835google scholar: lookup
  47. Grewal S, Hegde N, Yanow SK. Integrating machine learning to advance epitope mapping. Front Immunol 2024;15:1463931.
    doi: 10.3389/fimmu.2024.1463931pmc: PMC11471525pubmed: 39403389google scholar: lookup
  48. Wrapp D, Wang N, Corbett KS, Goldsmith JA, Hsieh C-L, Abiona O. Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. Science 2020;367(6483):1260–3.
    doi: 10.1126/science.abb2507pmc: PMC7164637pubmed: 32075877google scholar: lookup
  49. Lopez OJ, Osorio FA. Role of neutralizing antibodies in PRRSV protective immunity. Vet Immunol Immunopathol 2004;102(3):155–63.
    doi: 10.1016/j.vetimm.2004.09.005pubmed: 15507302google scholar: lookup
  50. Ostrowski M, Galeota JA, Jar AM, Platt KB, Osorio FA, Lopez OJ. Identification of neutralizing and nonneutralizing epitopes in the porcine reproductive and respiratory syndrome virus GP5 ectodomain. J Virol 2002;76(9):4241–50.
    doi: 10.1128/jvi.76.9.4241-4250.2002pmc: PMC155073pubmed: 11932389google scholar: lookup
  51. Liaci AM, Steigenberger B, Telles de Souza PC, Tamara S, Gröllers-Mulderij M, Ogrissek P. Structure of the human signal peptidase complex reveals the determinants for signal peptide cleavage. Mol Cell 2021;81(19):3934-3948.e11.
    doi: 10.1016/j.molcel.2021.07.031pubmed: 34388369google scholar: lookup
  52. Matczuk AK, Kunec D, Veit M. Co-translational processing of glycoprotein 3 from equine arteritis virus: N-glycosylation adjacent to the signal peptide prevents cleavage. J Biol Chem 2013;288(49):35396–405.
    doi: 10.1074/jbc.M113.505420pmc: PMC3853287pubmed: 24142700google scholar: lookup
  53. Matczuk AK, Veit M. Signal peptide cleavage from GP3 enabled by removal of adjacent glycosylation sites does not impair replication of equine arteritis virus in cell culture, but the hydrophobic C-terminus is essential. Virus Res 2014;183:107–11.
    doi: 10.1016/j.virusres.2014.02.005pubmed: 24556360google scholar: lookup
  54. Wlodawer A. Stereochemistry and Validation of Macromolecular Structures. Methods Mol Biol 2017;1607:595–610.
    doi: 10.1007/978-1-4939-7000-1_24pmc: PMC5560084pubmed: 28573590google scholar: lookup
  55. Zhang J, Timoney PJ, Shuck KM, Seoul G, Go YY, Lu Z. Molecular epidemiology and genetic characterization of equine arteritis virus isolates associated with the 2006-2007 multi-state disease occurrence in the USA. J Gen Virol 2010;91(Pt 9):2286–301.
    doi: 10.1099/vir.0.019737-0pubmed: 20444993google scholar: lookup
  56. Zhang J, Timoney PJ, MacLachlan NJ, McCollum WH, Balasuriya UBR. Persistent equine arteritis virus infection in HeLa cells. J Virol 2008;82(17):8456–64.
    doi: 10.1128/JVI.01249-08pmc: PMC2519626pubmed: 18579588google scholar: lookup
  57. Buel GR, Walters KJ. Can AlphaFold2 predict the impact of missense mutations on structure?. Nat Struct Mol Biol 2022;29(1):1–2.
    doi: 10.1038/s41594-021-00714-2pmc: PMC11218004pubmed: 35046575google scholar: lookup
  58. Firth AE, Zevenhoven-Dobbe JC, Wills NM, Go YY, Balasuriya UBR, Atkins JF. Discovery of a small arterivirus gene that overlaps the GP5 coding sequence and is important for virus production. J Gen Virol 2011;92(Pt 5):1097–106.
    doi: 10.1099/vir.0.029264-0pmc: PMC3139419pubmed: 21307223google scholar: lookup
  59. Johnson CR, Griggs TF, Gnanandarajah J, Murtaugh MP. Novel structural protein in porcine reproductive and respiratory syndrome virus encoded by an alternative ORF5 present in all arteriviruses. J Gen Virol 2011;92(Pt 5):1107–16.
    doi: 10.1099/vir.0.030213-0pmc: PMC3139420pubmed: 21307222google scholar: lookup
  60. Go YY, Zhang J, Timoney PJ, Cook RF, Horohov DW, Balasuriya UBR. Complex interactions between the major and minor envelope proteins of equine arteritis virus determine its tropism for equine CD3+ T lymphocytes and CD14+ monocytes. J Virol 2010;84(10):4898–911.
    doi: 10.1128/JVI.02743-09pmc: PMC2863813pubmed: 20219931google scholar: lookup
  61. Li D, Zhu L, Cui C, Wu Z, Qing P, Zhou Q. The role of major and minor structural proteins of porcine reproductive and respiratory syndrome virus in induction of protective immunity. Front Microbiol 2025;16:1563186.
    doi: 10.3389/fmicb.2025.1563186pmc: PMC11961951pubmed: 40177477google scholar: lookup
  62. Zhang Z, Nomura N, Muramoto Y, Ekimoto T, Uemura T, Liu K. Structure of SARS-CoV-2 membrane protein essential for virus assembly. Nat Commun 2022;13(1):4399.
    doi: 10.1038/s41467-022-32019-3pmc: PMC9355944pubmed: 35931673google scholar: lookup
  63. Dutta M, Dolan KA, Amiar S, Bass EJ, Sultana R, Voth GA. Direct lipid interactions control SARS-CoV-2 M protein conformational dynamics and virus assembly. bioRxiv 2024.
  64. Laporte M, Jochmans D, Bardiot D, Desmarets L, Debski-Antoniak OJ, Mizzon G. A coronavirus assembly inhibitor that targets the viral membrane protein. Nature 2025;640(8058):514–23.
    doi: 10.1038/s41586-025-08773-xpmc: PMC11981944pubmed: 40140569google scholar: lookup
  65. Van Damme E, Abeywickrema P, Yin Y, Xie J, Jacobs S, Mann MK. A small-molecule SARS-CoV-2 inhibitor targeting the membrane protein. Nature 2025;640(8058):506–13.
    doi: 10.1038/s41586-025-08651-6pmc: PMC11981937pubmed: 40140563google scholar: lookup
  66. Hartmann S, Radochonski L, Ye C, Martinez-Sobrido L, Chen J. SARS-CoV-2 ORF3a drives dynamic dense body formation for optimal viral infectivity.. Nat Commun 2025;16(1):4393.
    doi: 10.1038/s41467-025-59475-xpmc: PMC12069715pubmed: 40355429google scholar: lookup
  67. Miller AN, Houlihan PR, Matamala E, Cabezas-Bratesco D, Lee GY, Cristofori-Armstrong B. The SARS-CoV-2 accessory protein Orf3a is not an ion channel, but does interact with trafficking proteins.. Elife 2023;12:e84477.
    doi: 10.7554/eLife.84477pmc: PMC9910834pubmed: 36695574google scholar: lookup
  68. Mirdita M, Schütze K, Moriwaki Y, Heo L, Ovchinnikov S, Steinegger M. ColabFold: making protein folding accessible to all.. Nat Methods 2022;19(6):679–82.
    doi: 10.1038/s41592-022-01488-1pmc: PMC9184281pubmed: 35637307google scholar: lookup
  69. Laskowski RA, Jabłońska J, Pravda L, Vařeková RS, Thornton JM. PDBsum: Structural summaries of PDB entries.. Protein Sci 2018;27(1):129–34.
    doi: 10.1002/pro.3289pmc: PMC5734310pubmed: 28875543google scholar: lookup
  70. Lomize MA, Pogozheva ID, Joo H, Mosberg HI, Lomize AL. OPM database and PPM web server: resources for positioning of proteins in membranes.. Nucleic Acids Res 2012;40(Database issue):D370-6.
    doi: 10.1093/nar/gkr703pmc: PMC3245162pubmed: 21890895google scholar: lookup
  71. Almagro Armenteros JJ, Tsirigos KD, Sønderby CK, Petersen TN, Winther O, Brunak S. SignalP 5.0 improves signal peptide predictions using deep neural networks.. Nat Biotechnol 2019;37(4):420–3.
    doi: 10.1038/s41587-019-0036-zpubmed: 30778233google scholar: lookup
  72. Crooks GE, Hon G, Chandonia J-M, Brenner SE. WebLogo: a sequence logo generator.. Genome Res 2004;14(6):1188–90.
    doi: 10.1101/gr.849004pmc: PMC419797pubmed: 15173120google scholar: lookup
  73. Yariv B, Yariv E, Kessel A, Masrati G, Chorin AB, Martz E. Using evolutionary data to make sense of macromolecules with a “face-lifted” ConSurf.. Protein Sci 2023;32(3):e4582.
    doi: 10.1002/pro.4582pmc: PMC9942591pubmed: 36718848google scholar: lookup

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