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Home / Equine Research Bank / Vet Res / The role of glycoprotein H of equine herpesviruses 1 and 4 (...
Veterinary research2012; 43(1); 61; doi: 10.1186/1297-9716-43-61

The role of glycoprotein H of equine herpesviruses 1 and 4 (EHV-1 and EHV-4) in cellular host range and integrin binding.

Abstract: Equine herpesvirus type 1 and 4 (EHV-1 and EHV-4) glycoprotein H (gH) has been hypothesized to play a role in direct fusion of the virus envelope with cellular membranes. To investigate gH's role in infection, an EHV-1 mutant lacking gH was created and the gH genes were exchanged between EHV-1 and EHV-4 to determine if gH affects cellular entry and/or host range. In addition, a serine-aspartic acid-isoleucine (SDI) integrin-binding motif present in EHV-1 gH was mutated as it was presumed important in cell entry mediated by binding to α4β1 or α4β7 integrins. We here document that gH is essential for EHV-1 replication, plays a role in cell-to-cell spread and significantly affects plaque size and growth kinetics. Moreover, we could show that α4β1 and α4β7 integrins are not essential for viral entry of EHV-1 and EHV-4, and that viral entry is not affected in equine cells when the integrins are inaccessible.
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Publication Date: 2012-08-21 PubMed ID: 22909178PubMed Central: PMC3522555DOI: 10.1186/1297-9716-43-61Google 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.

This study investigates the role of a specific protein, glycoprotein H (gH), in facilitating the infection process of Equine Herpesviruses 1 and 4. Through experimentations, the researchers found that gH is crucial for virus replication and has significant influence on its growth and distribution within cells. The study also demonstrated that two specific integrins, α4β1 and α4β7, do not affect the viruses’ capability to enter cells.

About the Research

The main purpose of the research is to study the role of glycoprotein H (gH) of Equine herpesvirus type 1 and 4 (EHV-1 and EHV-4) in the infection process. The scientists leveraged laboratory experiments to isolate these two types of herpesviruses and analyzed the function of the gH protein in the context of virus replication and cellular entry mechanism.

  • The research was initiated by creating an EHV-1 mutant that lacked gH.
  • The gH genes of EHV-1 and EHV-4 were swapped to observe if the genetic changes could affect the viruses’ host range and cellular entry capabilities.
  • A specific motif in EHV-1 gH, known as a serine-aspartic acid-isoleucine (SDI) integrin-binding motif, was mutated to determine its role in cell entry through binding to α4β1 or α4β7 integrins.

Key Findings

The key findings from this study allow for a better understanding of how EHV-1 and EHV-4 function and interact with host cells. The main findings and conclusions highlighted are listed below:

  • The gH protein was found to be essential for EHV-1 replication.
  • This protein also significantly affected how the virus spread from cell to cell, as well as the overall growth kinetics and plaque size of the virus.
  • The study also outlined the discovery that α4β1 and α4β7 integrins are not essential for the virus’s entry into host cells. This was determined through the observation that the viral entry was not affected in equine cells even when these integrins were inaccessible.
  • Despite the initial hypothesis, the mutated SDI integrin-binding motif didn’t influence the mechanism of cell entry.

This research provides valuable insights into the role and functioning of viral proteins, specifically gH, in the infection processes of herpesviruses, which could potentially pave ways for targeted antiviral therapies in the future.

Cite This Article

APA
Azab W, Zajic L, Osterrieder N. (2012). The role of glycoprotein H of equine herpesviruses 1 and 4 (EHV-1 and EHV-4) in cellular host range and integrin binding. Vet Res, 43(1), 61. https://doi.org/10.1186/1297-9716-43-61

Publication

Veterinary research
ISSN: 1297-9716
NlmUniqueID: 9309551
Country: England
Language: English
Volume: 43
Issue: 1
Pages: 61

Researcher Affiliations

Azab, Walid
  • Institut für Virologie, Freie Universität Berlin, Philippstrasse 13, Haus 18, 10115, Berlin, Germany. wfazab@zedat.fu-berlin.de.
Zajic, Lara
    Osterrieder, Nikolaus

      MeSH Terms

      • Animals
      • Herpesviridae Infections / veterinary
      • Herpesviridae Infections / virology
      • Herpesvirus 1, Equid / genetics
      • Herpesvirus 1, Equid / growth & development
      • Herpesvirus 1, Equid / physiology
      • Herpesvirus 4, Equid / genetics
      • Herpesvirus 4, Equid / growth & development
      • Herpesvirus 4, Equid / physiology
      • Horse Diseases / virology
      • Horses
      • Host Specificity
      • Integrins / metabolism
      • Viral Envelope Proteins / genetics
      • Viral Envelope Proteins / metabolism
      • Viral Plaque Assay / veterinary
      • Virus Replication

      References

      This article includes 52 references
      1. King AMQ, Adams MJ, Carstens EB, Lefkowitz EJ. Virus Taxonomy: Ninth Report of the International Committee on Taxonomy of Viruses. UK: Academic Press, Elsevier; 2012. pp. 114–115.
      2. Patel JR, Heldens J. Equine herpesviruses 1 (EHV-1) and 4 (EHV-4)--epidemiology, disease and immunoprophylaxis: a brief review.. Vet J 2005 Jul;170(1):14-23.
        doi: 10.1016/j.tvjl.2004.04.018pubmed: 15993786google scholar: lookup
      3. Telford EA, Watson MS, Perry J, Cullinane AA, Davison AJ. The DNA sequence of equine herpesvirus-4.. J Gen Virol 1998 May;79 ( Pt 5):1197-203.
        pubmed: 9603335doi: 10.1099/0022-1317-79-5-1197google scholar: lookup
      4. Gryspeerdt AC, Vandekerckhove AP, Garré B, Barbé F, Van de Walle GR, Nauwynck HJ. Differences in replication kinetics and cell tropism between neurovirulent and non-neurovirulent EHV1 strains during the acute phase of infection in horses.. Vet Microbiol 2010 May 19;142(3-4):242-53.
        pubmed: 19926232doi: 10.1016/j.vetmic.2009.10.015google scholar: lookup
      5. Lunn DP, Davis-Poynter N, Flaminio MJ, Horohov DW, Osterrieder K, Pusterla N, Townsend HG. Equine herpesvirus-1 consensus statement.. J Vet Intern Med 2009 May-Jun;23(3):450-61.
        doi: 10.1111/j.1939-1676.2009.0304.xpubmed: 19645832google scholar: lookup
      6. Van de Walle GR, Peters ST, VanderVen BC, O'Callaghan DJ, Osterrieder N. Equine herpesvirus 1 entry via endocytosis is facilitated by alphaV integrins and an RSD motif in glycoprotein D.. J Virol 2008 Dec;82(23):11859-68.
        doi: 10.1128/JVI.00868-08pmc: PMC2583640pubmed: 18815313google scholar: lookup
      7. Osterrieder N, Van de Walle GR. Pathogenic potential of equine alphaherpesviruses: the importance of the mononuclear cell compartment in disease outcome.. Vet Microbiol 2010 Jun 16;143(1):21-8.
        doi: 10.1016/j.vetmic.2010.02.010pubmed: 20202764google scholar: lookup
      8. Whalley JM, Ruitenberg KM, Sullivan K, Seshadri L, Hansen K, Birch D, Gilkerson JR, Wellington JE. Host cell tropism of equine herpesviruses: glycoprotein D of EHV-1 enables EHV-4 to infect a non-permissive cell line.. Arch Virol 2007;152(4):717-25.
        doi: 10.1007/s00705-006-0885-xpubmed: 17171298google scholar: lookup
      9. Azab W, Osterrieder N. Glycoproteins D of equine herpesvirus type 1 (EHV-1) and EHV-4 determine cellular tropism independently of integrins.. J Virol 2012 Feb;86(4):2031-44.
        doi: 10.1128/JVI.06555-11pmc: PMC3302398pubmed: 22171258google scholar: lookup
      10. Campadelli-Fiume G, Menotti L. Entry of alphaherpesviruses into the cell. Human Herpesviruses: Biology, Therapy, and Immunoprophylaxis UK: Cambridge University Press; 2007. pp. 93–111.
      11. Frampton AR Jr, Goins WF, Cohen JB, von Einem J, Osterrieder N, O'Callaghan DJ, Glorioso JC. Equine herpesvirus 1 utilizes a novel herpesvirus entry receptor.. J Virol 2005 Mar;79(5):3169-73.
        doi: 10.1128/JVI.79.5.3169-3173.2005pmc: PMC548480pubmed: 15709036google scholar: lookup
      12. Kurtz BM, Singletary LB, Kelly SD, Frampton AR Jr. Equus caballus major histocompatibility complex class I is an entry receptor for equine herpesvirus type 1.. J Virol 2010 Sep;84(18):9027-34.
        doi: 10.1128/JVI.00287-10pmc: PMC2937649pubmed: 20610718google scholar: lookup
      13. Sasaki M, Hasebe R, Makino Y, Suzuki T, Fukushi H, Okamoto M, Matsuda K, Taniyama H, Sawa H, Kimura T. Equine major histocompatibility complex class I molecules act as entry receptors that bind to equine herpesvirus-1 glycoprotein D.. Genes Cells 2011 Apr;16(4):343-57.
        doi: 10.1111/j.1365-2443.2011.01491.xpmc: PMC3118799pubmed: 21306483google scholar: lookup
      14. Frampton AR Jr, Stolz DB, Uchida H, Goins WF, Cohen JB, Glorioso JC. Equine herpesvirus 1 enters cells by two different pathways, and infection requires the activation of the cellular kinase ROCK1.. J Virol 2007 Oct;81(20):10879-89.
        doi: 10.1128/JVI.00504-07pmc: PMC2045510pubmed: 17670830google scholar: lookup
      15. Hasebe R, Sasaki M, Sawa H, Wada R, Umemura T, Kimura T. Infectious entry of equine herpesvirus-1 into host cells through different endocytic pathways.. Virology 2009 Oct 25;393(2):198-209.
        doi: 10.1016/j.virol.2009.07.032pmc: PMC7111996pubmed: 19720389google scholar: lookup
      16. Galdiero S, Falanga A, Vitiello M, Raiola L, Fattorusso R, Browne H, Pedone C, Isernia C, Galdiero M. Analysis of a membrane interacting region of herpes simplex virus type 1 glycoprotein H.. J Biol Chem 2008 Oct 31;283(44):29993-30009.
        doi: 10.1074/jbc.M803092200pmc: PMC2662066pubmed: 18678872google scholar: lookup
      17. Subramanian RP, Geraghty RJ. Herpes simplex virus type 1 mediates fusion through a hemifusion intermediate by sequential activity of glycoproteins D, H, L, and B.. Proc Natl Acad Sci U S A 2007 Feb 20;104(8):2903-8.
        doi: 10.1073/pnas.0608374104pmc: PMC1815279pubmed: 17299053google scholar: lookup
      18. Atanasiu D, Whitbeck JC, de Leon MP, Lou H, Hannah BP, Cohen GH, Eisenberg RJ. Bimolecular complementation defines functional regions of Herpes simplex virus gB that are involved with gH/gL as a necessary step leading to cell fusion.. J Virol 2010 Apr;84(8):3825-34.
        doi: 10.1128/JVI.02687-09pmc: PMC2849501pubmed: 20130048google scholar: lookup
      19. Backovic M, DuBois RM, Cockburn JJ, Sharff AJ, Vaney MC, Granzow H, Klupp BG, Bricogne G, Mettenleiter TC, Rey FA. Structure of a core fragment of glycoprotein H from pseudorabies virus in complex with antibody.. Proc Natl Acad Sci U S A 2010 Dec 28;107(52):22635-40.
        doi: 10.1073/pnas.1011507107pmc: PMC3012528pubmed: 21149698google scholar: lookup
      20. Chowdary TK, Cairns TM, Atanasiu D, Cohen GH, Eisenberg RJ, Heldwein EE. Crystal structure of the conserved herpesvirus fusion regulator complex gH-gL.. Nat Struct Mol Biol 2010 Jul;17(7):882-8.
        doi: 10.1038/nsmb.1837pmc: PMC2921994pubmed: 20601960google scholar: lookup
      21. Matsuura H, Kirschner AN, Longnecker R, Jardetzky TS. Crystal structure of the Epstein-Barr virus (EBV) glycoprotein H/glycoprotein L (gH/gL) complex.. Proc Natl Acad Sci U S A 2010 Dec 28;107(52):22641-6.
        doi: 10.1073/pnas.1011806108pmc: PMC3012493pubmed: 21149717google scholar: lookup
      22. Fan Q, Lin E, Spear PG. Insertional mutations in herpes simplex virus type 1 gL identify functional domains for association with gH and for membrane fusion.. J Virol 2009 Nov;83(22):11607-15.
        doi: 10.1128/JVI.01369-09pmc: PMC2772692pubmed: 19726507google scholar: lookup
      23. Atanasiu D, Whitbeck JC, Cairns TM, Reilly B, Cohen GH, Eisenberg RJ. Bimolecular complementation reveals that glycoproteins gB and gH/gL of herpes simplex virus interact with each other during cell fusion.. Proc Natl Acad Sci U S A 2007 Nov 20;104(47):18718-23.
        doi: 10.1073/pnas.0707452104pmc: PMC2141843pubmed: 18003913google scholar: lookup
      24. Avitabile E, Forghieri C, Campadelli-Fiume G. Complexes between herpes simplex virus glycoproteins gD, gB, and gH detected in cells by complementation of split enhanced green fluorescent protein.. J Virol 2007 Oct;81(20):11532-7.
        doi: 10.1128/JVI.01343-07pmc: PMC2045520pubmed: 17670828google scholar: lookup
      25. Clark EA, Brugge JS. Integrins and signal transduction pathways: the road taken.. Science 1995 Apr 14;268(5208):233-9.
        doi: 10.1126/science.7716514pubmed: 7716514google scholar: lookup
      26. Stewart PL, Nemerow GR. Cell integrins: commonly used receptors for diverse viral pathogens.. Trends Microbiol 2007 Nov;15(11):500-7.
        doi: 10.1016/j.tim.2007.10.001pubmed: 17988871google scholar: lookup
      27. Graham KL, Fleming FE, Halasz P, Hewish MJ, Nagesha HS, Holmes IH, Takada Y, Coulson BS. Rotaviruses interact with alpha4beta7 and alpha4beta1 integrins by binding the same integrin domains as natural ligands.. J Gen Virol 2005 Dec;86(Pt 12):3397-3408.
        doi: 10.1099/vir.0.81102-0pubmed: 16298987google scholar: lookup
      28. Komoriya A, Green LJ, Mervic M, Yamada SS, Yamada KM, Humphries MJ. The minimal essential sequence for a major cell type-specific adhesion site (CS1) within the alternatively spliced type III connecting segment domain of fibronectin is leucine-aspartic acid-valine.. J Biol Chem 1991 Aug 15;266(23):15075-9.
        pubmed: 1869542
      29. Davis GE, Thomas JS, Madden S. The alpha4beta1 integrin can mediate leukocyte adhesion to casein and denatured protein substrates.. J Leukoc Biol 1997 Sep;62(3):318-28.
        pubmed: 9307070doi: 10.1002/jlb.62.3.318google scholar: lookup
      30. Hynes RO. Integrins: bidirectional, allosteric signaling machines.. Cell 2002 Sep 20;110(6):673-87.
        doi: 10.1016/S0092-8674(02)00971-6pubmed: 12297042google scholar: lookup
      31. Tischer BK, von Einem J, Kaufer B, Osterrieder N. Two-step red-mediated recombination for versatile high-efficiency markerless DNA manipulation in Escherichia coli.. Biotechniques 2006 Feb;40(2):191-7.
        doi: 10.2144/000112096pubmed: 16526409google scholar: lookup
      32. Rudolph J, O'Callaghan DJ, Osterrieder N. Cloning of the genomes of equine herpesvirus type 1 (EHV-1) strains KyA and racL11 as bacterial artificial chromosomes (BAC).. J Vet Med B Infect Dis Vet Public Health 2002 Feb;49(1):31-6.
        doi: 10.1046/j.1439-0450.2002.00534.xpubmed: 11911590google scholar: lookup
      33. Azab W, Kato K, Arii J, Tsujimura K, Yamane D, Tohya Y, Matsumura T, Akashi H. Cloning of the genome of equine herpesvirus 4 strain TH20p as an infectious bacterial artificial chromosome.. Arch Virol 2009;154(5):833-42.
        doi: 10.1007/s00705-009-0382-0pubmed: 19387789google scholar: lookup
      34. Azab W, Tsujimura K, Kato K, Arii J, Morimoto T, Kawaguchi Y, Tohya Y, Matsumura T, Akashi H. Characterization of a thymidine kinase-deficient mutant of equine herpesvirus 4 and in vitro susceptibility of the virus to antiviral agents.. Antiviral Res 2010 Feb;85(2):389-95.
        doi: 10.1016/j.antiviral.2009.11.007pubmed: 19931566google scholar: lookup
      35. von Einem J, Smith PM, Van de Walle GR, O'Callaghan DJ, Osterrieder N. In vitro and in vivo characterization of equine herpesvirus type 1 (EHV-1) mutants devoid of the viral chemokine-binding glycoprotein G (gG).. Virology 2007 May 25;362(1):151-62.
        doi: 10.1016/j.virol.2006.12.008pubmed: 17250864google scholar: lookup
      36. Azab W, Tsujimura K, Maeda K, Kobayashi K, Mohamed YM, Kato K, Matsumura T, Akashi H. Glycoprotein C of equine herpesvirus 4 plays a role in viral binding to cell surface heparan sulfate.. Virus Res 2010 Jul;151(1):1-9.
        doi: 10.1016/j.virusres.2010.03.003pubmed: 20236610google scholar: lookup
      37. . Image Processing and Analysis in Java. .
      38. Maeda K, Yasumoto S, Tsuruda A, Andoh K, Kai K, Otoi T, Matsumura T. Establishment of a novel equine cell line for isolation and propagation of equine herpesviruses.. J Vet Med Sci 2007 Sep;69(9):989-91.
        doi: 10.1292/jvms.69.989pubmed: 17917390google scholar: lookup
      39. Kerur N, Veettil MV, Sharma-Walia N, Sadagopan S, Bottero V, Paul AG, Chandran B. Characterization of entry and infection of monocytic THP-1 cells by Kaposi's sarcoma associated herpesvirus (KSHV): role of heparan sulfate, DC-SIGN, integrins and signaling.. Virology 2010 Oct 10;406(1):103-16.
        doi: 10.1016/j.virol.2010.07.012pmc: PMC2932840pubmed: 20674951google scholar: lookup
      40. Wisner T, Brunetti C, Dingwell K, Johnson DC. The extracellular domain of herpes simplex virus gE is sufficient for accumulation at cell junctions but not for cell-to-cell spread.. J Virol 2000 Mar;74(5):2278-87.
        doi: 10.1128/JVI.74.5.2278-2287.2000pmc: PMC111709pubmed: 10666258google scholar: lookup
      41. Gompels U, Minson A. The properties and sequence of glycoprotein H of herpes simplex virus type 1.. Virology 1986 Sep;153(2):230-47.
        doi: 10.1016/0042-6822(86)90026-7pubmed: 3016991google scholar: lookup
      42. Peeters B, de Wind N, Broer R, Gielkens A, Moormann R. Glycoprotein H of pseudorabies virus is essential for entry and cell-to-cell spread of the virus.. J Virol 1992 Jun;66(6):3888-92.
        pmc: PMC241176pubmed: 1316488doi: 10.1128/jvi.66.6.3888-3892.1992google scholar: lookup
      43. Browne HM. The role of glycoprotein H in herpesvirus membrane fusion.. Protein Pept Lett 2009;16(7):760-5.
        doi: 10.2174/092986609788681850pubmed: 19601905google scholar: lookup
      44. Granzow H, Klupp BG, Fuchs W, Veits J, Osterrieder N, Mettenleiter TC. Egress of alphaherpesviruses: comparative ultrastructural study.. J Virol 2001 Apr;75(8):3675-84.
        doi: 10.1128/JVI.75.8.3675-3684.2001pmc: PMC114859pubmed: 11264357google scholar: lookup
      45. Schr der C, Keil GM. Bovine herpesvirus 1 requires glycoprotein H for infectivity and direct spreading and glycoproteins gH(W450) and gB for glycoprotein D-independent cell-to-cell spread.. J Gen Virol 1999 Jan;80 ( Pt 1):57-61.
        pubmed: 9934684doi: 10.1099/0022-1317-80-1-57google scholar: lookup
      46. Farnsworth A, Wisner TW, Webb M, Roller R, Cohen G, Eisenberg R, Johnson DC. Herpes simplex virus glycoproteins gB and gH function in fusion between the virion envelope and the outer nuclear membrane.. Proc Natl Acad Sci U S A 2007 Jun 12;104(24):10187-92.
        doi: 10.1073/pnas.0703790104pmc: PMC1891206pubmed: 17548810google scholar: lookup
      47. Neubauer A, Osterrieder N. Equine herpesvirus type 1 (EHV-1) glycoprotein K is required for efficient cell-to-cell spread and virus egress.. Virology 2004 Nov 10;329(1):18-32.
        doi: 10.1016/j.virol.2004.07.034pubmed: 15476871google scholar: lookup
      48. Cairns TM, Friedman LS, Lou H, Whitbeck JC, Shaner MS, Cohen GH, Eisenberg RJ. N-terminal mutants of herpes simplex virus type 2 gH are transported without gL but require gL for function.. J Virol 2007 May;81(10):5102-11.
        doi: 10.1128/JVI.00097-07pmc: PMC1900195pubmed: 17344290google scholar: lookup
      49. Dubin G, Jiang H. Expression of herpes simplex virus type 1 glycoprotein L (gL) in transfected mammalian cells: evidence that gL is not independently anchored to cell membranes.. J Virol 1995 Jul;69(7):4564-8.
        pmc: PMC189206pubmed: 7769724doi: 10.1128/jvi.69.7.4564-4568.1995google scholar: lookup
      50. Hutchinson L, Browne H, Wargent V, Davis-Poynter N, Primorac S, Goldsmith K, Minson AC, Johnson DC. A novel herpes simplex virus glycoprotein, gL, forms a complex with glycoprotein H (gH) and affects normal folding and surface expression of gH.. J Virol 1992 Apr;66(4):2240-50.
        pmc: PMC289017pubmed: 1312629doi: 10.1128/jvi.66.4.2240-2250.1992google scholar: lookup
      51. Roop C, Hutchinson L, Johnson DC. A mutant herpes simplex virus type 1 unable to express glycoprotein L cannot enter cells, and its particles lack glycoprotein H.. J Virol 1993 Apr;67(4):2285-97.
        pmc: PMC240370pubmed: 8383241doi: 10.1128/jvi.67.4.2285-2297.1993google scholar: lookup
      52. Gianni T, Cerretani A, Dubois R, Salvioli S, Blystone SS, Rey F, Campadelli-Fiume G. Herpes simplex virus glycoproteins H/L bind to cells independently of {alpha}V{beta}3 integrin and inhibit virus entry, and their constitutive expression restricts infection.. J Virol 2010 Apr;84(8):4013-25.
        doi: 10.1128/JVI.02502-09pmc: PMC2849490pubmed: 20147400google scholar: lookup

      Citations

      This article has been cited 6 times.
      1. Kremling V, Loll B, Pach S, Dahmani I, Weise C, Wolber G, Chiantia S, Wahl MC, Osterrieder N, Azab W. Crystal structures of glycoprotein D of equine alphaherpesviruses reveal potential binding sites to the entry receptor MHC-I.. Front Microbiol 2023;14:1197120.
        doi: 10.3389/fmicb.2023.1197120pubmed: 37250020google scholar: lookup
      2. Kolyvushko O, Kelch MA, Osterrieder N, Azab W. Equine Alphaherpesviruses Require Activation of the Small GTPases Rac1 and Cdc42 for Intracellular Transport.. Microorganisms 2020 Jul 7;8(7).
        doi: 10.3390/microorganisms8071013pubmed: 32645930google scholar: lookup
      3. Azab W, Gramatica A, Herrmann A, Osterrieder N. Binding of alphaherpesvirus glycoprotein H to surface α4β1-integrins activates calcium-signaling pathways and induces phosphatidylserine exposure on the plasma membrane.. mBio 2015 Oct 20;6(5):e01552-15.
        doi: 10.1128/mBio.01552-15pubmed: 26489864google scholar: lookup
      4. Chakraborty S, Hu SY, Wu SH, Karmenyan A, Chiou A. The interaction affinity between vascular cell adhesion molecule-1 (VCAM-1) and very late antigen-4 (VLA-4) analyzed by quantitative FRET.. PLoS One 2015;10(3):e0121399.
        doi: 10.1371/journal.pone.0121399pubmed: 25793408google scholar: lookup
      5. Spiesschaert B, Osterrieder N, Azab W. Comparative analysis of glycoprotein B (gB) of equine herpesvirus type 1 and type 4 (EHV-1 and EHV-4) in cellular tropism and cell-to-cell transmission.. Viruses 2015 Feb 3;7(2):522-42.
        doi: 10.3390/v7020522pubmed: 25654240google scholar: lookup
      6. Azab W, Lehmann MJ, Osterrieder N. Glycoprotein H and α4β1 integrins determine the entry pathway of alphaherpesviruses.. J Virol 2013 May;87(10):5937-48.
        doi: 10.1128/JVI.03522-12pubmed: 23514881google scholar: lookup
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