1932
0
  1. Home
  2. A-Z Publications
  3. Annual Review of Virology
  4. Volume 9, 2022
  5. Article

Annual Review of Virology

Volume 9, 2022

Opportunities, Technology, and the Joy of Discovery

Abstract

My grandparents were immigrants. My paternal grandfather was illiterate. Yet my parents were able to complete college and to become teachers. I had a conventional upbringing in a small town in Florida, graduating from high school in 1960. I was fortunate enough to graduate cum laude from Florida State University and to earn other credentials leading to faculty positions at outstanding institutions of higher education: the University of Chicago and Northwestern University. At a time when women were rarely the leaders of research groups, I was able to establish a well-funded research program and to make contributions to our understanding of viral entry into cells. My best research was done after I became confident enough to seek productive interactions with collaborators. I am grateful for the collaborators and collaborations that moved our field forward and for my trainees who have gone on to successes in many different careers.

Keyword(s): autobiography, entry receptors, herpes simplex viruses, viral entry
Loading

Article metrics loading...

/content/journals/10.1146/annurev-virology-100520-012840
2022-09-29
2024-05-11
Loading full text...

Full text loading...

/deliver/fulltext/virology/9/1/annurev-virology-100520-012840.html?itemId=/content/journals/10.1146/annurev-virology-100520-012840&mimeType=html&fmt=ahah

Literature Cited

  1. 1.
    Spear PG, Roizman B. 1967. Buoyant density of herpes simplex virus in solutions of caesium chloride. Nature 214:713–14
     [Crossref] [Google Scholar]
  2. 2.
    Roizman B, Spear PG. 1968. Preparation of herpes simplex virus of high titer. J. Virol. 2:83–84
     [Crossref] [Google Scholar]
  3. 3.
    Spear PG, Roizman B. 1968. The proteins specified by herpes simplex virus. I. Time of synthesis, transfer into nuclei, and properties of proteins made in productively infected cells. Virology 36:545–55
     [Crossref] [Google Scholar]
  4. 4.
    Spear PG, Roizman B. 1968. An improved procedure for H3 and C14 counting in acrylamide gels with a nonaqueous scintillation system. Anal. Biochem. 26:197–200
     [Crossref] [Google Scholar]
  5. 5.
    Spear PG, Roizman B. 1972. Proteins specified by herpes simplex virus. V. Purification and structural proteins of the herpesvirion. J. Virol. 9:143–59
     [Crossref] [Google Scholar]
  6. 6.
    Spear PG, Keller JM, Roizman B. 1970. Proteins specified by herpes simplex virus. II. Viral glycoproteins associated with cellular membranes. J. Virol. 5:123–31
     [Crossref] [Google Scholar]
  7. 7.
    Spear PG, Roizman B. 1970. Proteins specified by herpes simplex virus, IV. Site of glycosylation and accumulation of viral membrane proteins. PNAS 66:730–37
     [Crossref] [Google Scholar]
  8. 8.
    Roizman B, Spear PG. 1971. Herpesvirus antigens on cell membranes detected by centrifugation of membrane-antibody complexes. Science 171:298–300
     [Crossref] [Google Scholar]
  9. 9.
    Heine JW, Spear PG, Roizman B. 1972. Proteins specified by herpes simplex virus. VI. Viral proteins in the plasma membrane. J. Virol. 9:431–39
     [Crossref] [Google Scholar]
  10. 10.
    Loret S, Guay G, Lippe R. 2008. Comprehensive characterization of extracellular herpes simplex virus type 1 virions. J. Virol. 82:8605–18
     [Crossref] [Google Scholar]
  11. 11.
    Spear PG, Wang AL, Rutishauser U, Edelman GM. 1973. Characterization of splenic lymphoid cells in fetal and newborn mice. J. Exp. Med. 138:557–73
     [Crossref] [Google Scholar]
  12. 12.
    Spear PG, Edelman GM. 1974. Maturation of the humoral immune response in mice. J. Exp. Med. 139:249–63
     [Crossref] [Google Scholar]
  13. 13.
    Spear PG. 1976. Membrane proteins specified by herpes simplex viruses. I. Identification of four glycoprotein precursors and their products in type 1-infected cells. J. Virol. 17:991–1008
     [Crossref] [Google Scholar]
  14. 14.
    Spear PG. 1993. Entry of alphaherpesviruses into cells. Semin. Virol. 4:167–80
     [Crossref] [Google Scholar]
  15. 15.
    Hilterbrand AT, Daly RE, Heldwein EE. 2021. Contributions of the four essential entry glycoproteins to HSV-1 tropism and the selection of entry routes. mBio 12:e00143–21
     [Crossref] [Google Scholar]
  16. 16.
    Hilterbrand AT, Heldwein EE. 2019. Go go gadget glycoprotein!: HSV-1 draws on its sizeable glycoprotein tool kit to customize its diverse entry routes. PLOS Pathog 15:e1007660
     [Crossref] [Google Scholar]
  17. 17.
    Shukla D, Spear PG. 2001. Herpesviruses and heparan sulfate: an intimate relationship in aid of viral entry. J. Clin. Invest. 108:503–10
     [Crossref] [Google Scholar]
  18. 18.
    Parry C, Bell S, Minson T, Browne H. 2005. Herpes simplex virus type 1 glycoprotein H binds to αvβ3 integrins. J. Gen. Virol. 86:7–10
     [Crossref] [Google Scholar]
  19. 19.
    Galdiero M, Whiteley A, Bruun B, Bell S, Minson T, Browne H. 1997. Site-directed and linker insertion mutagenesis of herpes simplex virus type 1 glycoprotein H. J. Virol. 71:2163–70
     [Crossref] [Google Scholar]
  20. 20.
    Satoh T, Arii J, Suenaga T, Wang J, Kogure A et al. 2008. PILRα is a herpes simplex virus-1 entry coreceptor that associates with glycoprotein B. Cell 132:935–44
     [Crossref] [Google Scholar]
  21. 21.
    Spear PG, Eisenberg RJ, Cohen GH. 2000. Three classes of cell surface receptors for alphaherpesvirus entry. Virology 275:1–8
     [Crossref] [Google Scholar]
  22. 22.
    Eisenberg RJ, Atanasiu D, Cairns TM, Gallagher JR, Krummenacher C, Cohen GH. 2012. Herpes virus fusion and entry: a story with many characters. Viruses 4:800–32
     [Crossref] [Google Scholar]
  23. 23.
    Vollmer B, Prazak V, Vasishtan D, Jefferys EE, Hernandez-Duran A et al. 2020. The prefusion structure of herpes simplex virus glycoprotein B. Sci. Adv. 6:eabc1726
     [Crossref] [Google Scholar]
  24. 24.
    Heldwein EE, Lou H, Bender FC, Cohen GH, Eisenberg RJ, Harrison SC. 2006. Crystal structure of glycoprotein B from herpes simplex virus 1. Science 313:217–20
     [Crossref] [Google Scholar]
  25. 25.
    Johnson DC, Spear PG. 1983. O-linked oligosaccharides are acquired by herpes simplex virus glycoproteins in the Golgi apparatus. Cell 32:987–97
     [Crossref] [Google Scholar]
  26. 26.
    Nahmias AJ, Kibrick S. 1964. Inhibitory effect of heparin on herpes simplex virus. J. Bacteriol. 87:1060–66
     [Crossref] [Google Scholar]
  27. 27.
    WuDunn D, Spear PG. 1989. Initial interaction of herpes simplex virus with cells is binding to heparan sulfate. J. Virol. 63:52–58
     [Crossref] [Google Scholar]
  28. 28.
    Shieh MT, WuDunn D, Montgomery RI, Esko JD, Spear PG. 1992. Cell surface receptors for herpes simplex virus are heparan sulfate proteoglycans. J. Cell Biol. 116:1273–81
     [Crossref] [Google Scholar]
  29. 29.
    Herold BC, WuDunn D, Soltys N, Spear PG. 1991. Glycoprotein C of herpes simplex virus type 1 plays a principal role in the adsorption of virus to cells and in infectivity. J. Virol. 65:1090–98
     [Crossref] [Google Scholar]
  30. 30.
    Herold BC, Visalli RJ, Susmarski N, Brandt CR, Spear PG. 1994. Glycoprotein C-independent binding of herpes simplex virus to cells requires cell surface heparan sulphate and glycoprotein B. J. Gen. Virol. 75:Part 61211–22
     [Crossref] [Google Scholar]
  31. 31.
    Manservigi R, Spear PG, Buchan A. 1977. Cell fusion induced by herpes simplex virus is promoted and suppressed by different viral glycoproteins. PNAS 74:3913–17
     [Crossref] [Google Scholar]
  32. 32.
    Gruenheid S, Gatzke L, Meadows H, Tufaro F. 1993. Herpes simplex virus infection and propagation in a mouse L cell mutant lacking heparan sulfate proteoglycans. J. Virol. 67:93–100
     [Crossref] [Google Scholar]
  33. 33.
    Pertel PE, Spear PG. 1996. Modified entry and syncytium formation by herpes simplex virus type 1 mutants selected for resistance to heparin inhibition. Virology 226:22–33
     [Crossref] [Google Scholar]
  34. 34.
    Clausen TM, Sandoval DR, Spliid CB, Pihl J, Perrett HR et al. 2020. SARS-CoV-2 infection depends on cellular heparan sulfate and ACE2. Cell 183:1043–57.e15
     [Crossref] [Google Scholar]
  35. 35.
    Shieh MT, Spear PG. 1994. Herpesvirus-induced cell fusion that is dependent on cell surface heparan sulfate or soluble heparin. J. Virol. 68:1224–28
     [Crossref] [Google Scholar]
  36. 36.
    Haffey ML, Spear PG. 1980. Alterations in glycoprotein gB specified by mutants and their partial revertants in herpes simplex virus type 1 and relationship to other mutant phenotypes. J. Virol. 35:114–28
     [Crossref] [Google Scholar]
  37. 37.
    Sarmiento M, Haffey M, Spear PG. 1979. Membrane proteins specified by herpes simplex viruses. III. Role of glycoprotein VP7(B2) in virion infectivity. J. Virol. 29:1149–58
     [Crossref] [Google Scholar]
  38. 38.
    Cai WH, Gu B, Person S. 1988. Role of glycoprotein B of herpes simplex virus type 1 in viral entry and cell fusion. J. Virol. 62:2596–604
     [Crossref] [Google Scholar]
  39. 39.
    Claesson-Welsh L, Spear PG 1986. Oligomerization of herpes simplex virus glycoprotein B. J. Virol. 60:803–6
     [Crossref] [Google Scholar]
  40. 40.
    Sarmiento M, Spear PG. 1979. Membrane proteins specified by herpes simplex viruses. IV. Conformation of the virion glycoprotein designated VP7(B2). J. Virol. 29:1159–67
     [Crossref] [Google Scholar]
  41. 41.
    Para MF, Parish ML, Noble AG, Spear PG. 1985. Potent neutralizing activity associated with anti-glycoprotein D specificity among monoclonal antibodies selected for binding to herpes simplex virions. J. Virol. 55:483–88
     [Crossref] [Google Scholar]
  42. 42.
    Stannard LM, Fuller AO, Spear PG. 1987. Herpes simplex virus glycoproteins associated with different morphological entities projecting from the virion envelope. J. Gen. Virol. 68:715–25
     [Crossref] [Google Scholar]
  43. 43.
    Campadelli-Fiume G, Arsenakis M, Farabegoli F, Roizman B. 1988. Entry of herpes simplex virus 1 in BJ cells that constitutively express viral glycoprotein D is by endocytosis and results in degradation of the virus. J. Virol. 62:159–67
     [Crossref] [Google Scholar]
  44. 44.
    Johnson RM, Spear PG. 1989. Herpes simplex virus glycoprotein D mediates interference with herpes simplex virus infection. J. Virol. 63:819–27
     [Crossref] [Google Scholar]
  45. 45.
    Vogt PK. 1970. Envelope classification of avian RNA tumor viruses. Bibl. Haematol. 36:153–67
     [Google Scholar]
  46. 46.
    Ligas MW, Johnson DC. 1988. A herpes simplex virus mutant in which glycoprotein D sequences are replaced by β-galactosidase sequences binds to but is unable to penetrate into cells. J. Virol. 62:1486–94
     [Crossref] [Google Scholar]
  47. 47.
    Johnson DC, Ligas MW. 1988. Herpes simplex viruses lacking glycoprotein D are unable to inhibit virus penetration: quantitative evidence for virus-specific cell surface receptors. J. Virol. 62:4605–12
     [Crossref] [Google Scholar]
  48. 48.
    Fuller AO, Spear PG. 1985. Specificities of monoclonal and polyclonal antibodies that inhibit adsorption of herpes simplex virus to cells and lack of inhibition by potent neutralizing antibodies. J. Virol. 55:475–82
     [Crossref] [Google Scholar]
  49. 49.
    Fuller AO, Spear PG. 1987. Anti-glycoprotein D antibodies that permit adsorption but block infection by herpes simplex virus 1 prevent virion-cell fusion at the cell surface. PNAS 84:5454–58
     [Crossref] [Google Scholar]
  50. 50.
    Noble AG, Lee GT, Sprague R, Parish ML, Spear PG. 1983. Anti-gD monoclonal antibodies inhibit cell fusion induced by herpes simplex virus type 1. Virology 129:218–24
     [Crossref] [Google Scholar]
  51. 51.
    Dean HJ, Terhune SS, Shieh MT, Susmarski N, Spear PG. 1994. Single amino acid substitutions in gD of herpes simplex virus 1 confer resistance to gD-mediated interference and cause cell-type-dependent alterations in infectivity. Virology 199:67–80
     [Crossref] [Google Scholar]
  52. 52.
    Fuller AO, Santos RE, Spear PG. 1989. Neutralizing antibodies specific for glycoprotein H of herpes simplex virus permit viral attachment to cells but prevent penetration. J. Virol. 63:3435–43
     [Crossref] [Google Scholar]
  53. 53.
    Desai PJ, Schaffer PA, Minson AC. 1988. Excretion of non-infectious virus particles lacking glycoprotein H by a temperature-sensitive mutant of herpes simplex virus type 1: evidence that gH is essential for virion infectivity. J. Gen. Virol. 69:Part 61147–56
     [Crossref] [Google Scholar]
  54. 54.
    Montgomery RI, Warner MS, Lum BJ, Spear PG. 1996. Herpes simplex virus-1 entry into cells mediated by a novel member of the TNF/NGF receptor family. Cell 87:427–36
     [Crossref] [Google Scholar]
  55. 55.
    Sedy J, Bekiaris V, Ware CF. 2014. Tumor necrosis factor superfamily in innate immunity and inflammation. Cold Spring Harb. Perspect. Biol. 7:a016279
     [Crossref] [Google Scholar]
  56. 56.
    Burn Aschner C, Loh LN, Galen B, Delwel I, Jangra RK et al. 2020. HVEM signaling promotes protective antibody-dependent cellular cytotoxicity (ADCC) vaccine responses to herpes simplex viruses. Sci. Immunol. 5:eaax2454
     [Crossref] [Google Scholar]
  57. 57.
    Warner MS, Geraghty RJ, Martinez WM, Montgomery RI, Whitbeck JC et al. 1998. A cell surface protein with herpesvirus entry activity (HveB) confers susceptibility to infection by mutants of herpes simplex virus type 1, herpes simplex virus type 2, and pseudorabies virus. Virology 246:179–89
     [Crossref] [Google Scholar]
  58. 58.
    Freistadt MS, Kaplan G, Racaniello VR. 1990. Heterogeneous expression of poliovirus receptor-related proteins in human cells and tissues. Mol. Cell. Biol. 10:5700–6
     [Google Scholar]
  59. 59.
    Takahashi K, Nakanishi H, Miyahara M, Mandai K, Satoh K et al. 1999. Nectin/PRR: an immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with Afadin, a PDZ domain-containing protein. J. Cell Biol. 145:539–49
     [Crossref] [Google Scholar]
  60. 60.
    Geraghty RJ, Krummenacher C, Cohen GH, Eisenberg RJ, Spear PG. 1998. Entry of alphaherpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor. Science 280:1618–20
     [Crossref] [Google Scholar]
  61. 61.
    Mizutani K, Miyata M, Shiotani H, Kameyama T, Takai Y. 2021. Nectins and nectin-like molecules in synapse formation and involvement in neurological diseases. Mol. Cell. Neurosci. 115:103653
     [Crossref] [Google Scholar]
  62. 62.
    Yoon M, Spear PG. 2002. Disruption of adherens junctions liberates nectin-1 to serve as receptor for herpes simplex virus and pseudorabies virus entry. J. Virol. 76:7203–8
     [Crossref] [Google Scholar]
  63. 63.
    Whitbeck JC, Peng C, Lou H, Xu R, Willis SH et al. 1997. Glycoprotein D of herpes simplex virus (HSV) binds directly to HVEM, a member of the tumor necrosis factor receptor superfamily and a mediator of HSV entry. J. Virol. 71:6083–93
     [Crossref] [Google Scholar]
  64. 64.
    Krummenacher C, Nicola AV, Whitbeck JC, Lou H, Hou W et al. 1998. Herpes simplex virus glycoprotein D can bind to poliovirus receptor-related protein 1 or herpesvirus entry mediator, two structurally unrelated mediators of virus entry. J. Virol. 72:7064–74
     [Crossref] [Google Scholar]
  65. 65.
    Nicola AV, Ponce de Leon M, Xu R, Hou W, Whitbeck JC et al. 1998. Monoclonal antibodies to distinct sites on herpes simplex virus (HSV) glycoprotein D block HSV binding to HVEM. J. Virol. 72:3595–601
     [Crossref] [Google Scholar]
  66. 66.
    Krummenacher C, Rux AH, Whitbeck JC, Ponce-de-Leon M, Lou H et al. 1999. The first immunoglobulin-like domain of HveC is sufficient to bind herpes simplex virus gD with full affinity, while the third domain is involved in oligomerization of HveC. J. Virol. 73:8127–37
     [Crossref] [Google Scholar]
  67. 67.
    Krummenacher C, Supekar VM, Whitbeck JC, Lazear E, Connolly SA et al. 2005. Structure of unliganded HSV gD reveals a mechanism for receptor-mediated activation of virus entry. EMBO J 24:4144–53
     [Crossref] [Google Scholar]
  68. 68.
    Carfi A, Willis SH, Whitbeck JC, Krummenacher C, Cohen GH et al. 2001. Herpes simplex virus glycoprotein D bound to the human receptor HveA. Mol. Cell 8:169–79
     [Crossref] [Google Scholar]
  69. 69.
    Di Giovine P, Settembre EC, Bhargava AK, Luftig MA, Lou H et al. 2011. Structure of herpes simplex virus glycoprotein D bound to the human receptor nectin-1. PLOS Pathog 7:e1002277
     [Crossref] [Google Scholar]
  70. 70.
    Yoon M, Spear PG. 2004. Random mutagenesis of the gene encoding a viral ligand for multiple cell entry receptors to obtain viral mutants altered for receptor usage. PNAS 101:17252–57
     [Crossref] [Google Scholar]
  71. 71.
    Yoon M, Zago A, Shukla D, Spear PG. 2003. Mutations in the N termini of herpes simplex virus type 1 and 2 gDs alter functional interactions with the entry/fusion receptors HVEM, nectin-2, and 3-O-sulfated heparan sulfate but not with nectin-1. J. Virol. 77:9221–31
     [Crossref] [Google Scholar]
  72. 72.
    Manoj S, Jogger CR, Myscofski D, Yoon M, Spear PG. 2004. Mutations in herpes simplex virus glycoprotein D that prevent cell entry via nectins and alter cell tropism. PNAS 101:12414–21
     [Crossref] [Google Scholar]
  73. 73.
    Jogger CR, Montgomery RI, Spear PG. 2004. Effects of linker-insertion mutations in herpes simplex virus 1 gD on glycoprotein-induced fusion with cells expressing HVEM or nectin-1. Virology 318:318–26
     [Crossref] [Google Scholar]
  74. 74.
    Geraghty RJ, Jogger CR, Spear PG. 2000. Cellular expression of alphaherpesvirus gD interferes with entry of homologous and heterologous alphaherpesviruses by blocking access to a shared gD receptor. Virology 268:147–58
     [Crossref] [Google Scholar]
  75. 75.
    Terry-Allison T, Montgomery RI, Warner MS, Geraghty RJ, Spear PG. 2001. Contributions of gD receptors and glycosaminoglycan sulfation to cell fusion mediated by herpes simplex virus 1. Virus Res 74:39–45
     [Crossref] [Google Scholar]
  76. 76.
    Pertel PE, Fridberg A, Parish ML, Spear PG. 2001. Cell fusion induced by herpes simplex virus glycoproteins gB, gD, and gH-gL requires a gD receptor but not necessarily heparan sulfate. Virology 279:313–24
     [Crossref] [Google Scholar]
  77. 77.
    Fan Q, Lin E, Satoh T, Arase H, Spear PG. 2009. Differential effects on cell fusion activity of mutations in herpes simplex virus 1 glycoprotein B (gB) dependent on whether a gD receptor or a gB receptor is overexpressed. J. Virol. 83:7384–90
     [Crossref] [Google Scholar]
  78. 78.
    Shukla D, Dal Canto MC, Rowe CL, Spear PG. 2000. Striking similarity of murine nectin-1α to human nectin-1α (HveC) in sequence and activity as a glycoprotein D receptor for alphaherpesvirus entry. J. Virol. 74:11773–81
     [Crossref] [Google Scholar]
  79. 79.
    Shukla D, Rowe CL, Dong Y, Racaniello VR, Spear PG. 1999. The murine homolog (Mph) of human herpesvirus entry protein B (HveB) mediates entry of pseudorabies virus but not herpes simplex virus types 1 and 2. J. Virol. 73:4493–97
     [Crossref] [Google Scholar]
  80. 80.
    Shukla D, Liu J, Blaiklock P, Shworak NW, Bai X et al. 1999. A novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1 entry. Cell 99:13–22
     [Crossref] [Google Scholar]
  81. 81.
    Wang Y, Subudhi SK, Anders RA, Lo J, Sun Y et al. 2005. The role of herpesvirus entry mediator as a negative regulator of T cell-mediated responses. J. Clin. Invest. 115:711–17
     [Crossref] [Google Scholar]
  82. 82.
    Inagaki M, Irie K, Ishizaki H, Tanaka-Okamoto M, Morimoto K et al. 2005. Roles of cell-adhesion molecules nectin 1 and nectin 3 in ciliary body development. Development 132:1525–37
     [Crossref] [Google Scholar]
  83. 83.
    Parr MB, Kepple L, McDermott MR, Drew MD, Bozzola JJ, Parr EL. 1994. A mouse model for studies of mucosal immunity to vaginal infection by herpes simplex virus type 2. Lab. Invest. 70:369–80
     [Google Scholar]
  84. 84.
    Taylor JM, Lin E, Susmarski N, Yoon M, Zago A et al. 2007. Alternative entry receptors for herpes simplex virus and their roles in disease. Cell Host Microbe 2:19–28
     [Crossref] [Google Scholar]
  85. 85.
    Kopp SJ, Banisadr G, Glajch K, Maurer UE, Grunewald K et al. 2009. Infection of neurons and encephalitis after intracranial inoculation of herpes simplex virus requires the entry receptor nectin-1. PNAS 106:17916–20
     [Crossref] [Google Scholar]
  86. 86.
    Karaba AH, Kopp SJ, Longnecker R. 2011. Herpesvirus entry mediator and nectin-1 mediate herpes simplex virus 1 infection of the murine cornea. J. Virol. 85:10041–47
     [Crossref] [Google Scholar]
  87. 87.
    Karaba AH, Kopp SJ, Longnecker R. 2012. Herpesvirus entry mediator is a serotype specific determinant of pathogenesis in ocular herpes. PNAS 109:20649–54
     [Crossref] [Google Scholar]
  88. 88.
    Edwards RG, Kopp SJ, Karaba AH, Wilcox DR, Longnecker R. 2015. Herpesvirus entry mediator on radiation-resistant cell lineages promotes ocular herpes simplex virus 1 pathogenesis in an entry-independent manner. mBio 6:e01532–15
     [Google Scholar]
/content/journals/10.1146/annurev-virology-100520-012840
Loading
Opportunities, Technology, and the Joy of Discovery
Annual Review of Virology 9, 1 (2022); https://doi.org/10.1146/annurev-virology-100520-012840
/content/journals/10.1146/annurev-virology-100520-012840
/content/journals/10.1146/annurev-virology-100520-012840
Loading

Data & Media loading...

  • Article Type: Review Article

Most Cited Most Cited RSS feed

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error