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. 1992 Nov;66(11):6668–6685. doi: 10.1128/jvi.66.11.6668-6685.1992

Disulfide bond structure of glycoprotein D of herpes simplex virus types 1 and 2.

D Long 1, W C Wilcox 1, W R Abrams 1, G H Cohen 1, R J Eisenberg 1
PMCID: PMC240163  PMID: 1328685

Abstract

Glycoprotein D (gD) is a structural component of the herpes simplex virus envelope which is essential for virus penetration. The function of this protein is highly dependent on its structure, and its structure is dependent on maintenance of three intact disulfide bonds. gD contains six cysteines in its ectodomain whose spacing is conserved among all its homologs in other alphaherpesviruses as well as Marek's disease virus. For other proteins, conservation of cysteine spacing correlates with conservation of disulfide bond structure. We have now solved the disulfide bond structure of gD-1 and gD-2 of herpes simplex virus types 1 and 2, respectively. Two approaches were used. First, we constructed 15 double-Cys mutants of gD-1, representing all possible disulfide pairs. In each case, codons for cysteines were changed to serine. We reasoned that if two cysteines normally form a disulfide bond, double mutations which eliminate one proper bond should be less harmful to gD structure than double mutations which eliminate two disulfide bonds. The mutated genes were cloned into a eucaryotic expression vector, and the proteins were expressed in transiently transfected cells. Three double mutations, Cys-1,5, Cys-2,6, and Cys-3,4 permitted gD-1 folding, processing, transport to the cell surface, and function in virus infection, whereas 12 other double mutations each produced a malfolded and nonfunctional protein. Thus, the three functional double-Cys mutants may represent the actual partners in disulfide bond linkages. The second approach was to define the actual disulfide bond structure of gD by biochemical means. Purified native gD-2 was cleaved by CNBr and proteases, and the peptides were separated by high-performance liquid chromatography. Disulfide-linked peptides were subjected to N-terminal amino acid sequencing. The results show that cysteine 1 (amino acid [aa] 66) is bonded to cysteine 5 (aa 189), cysteine 2 (aa 106) is bonded to cysteine 6 (aa 202), and cysteine 3 (aa 118) is bonded to cysteine 4 (aa 127). Thus, the biochemical analysis of gD-2 agrees with the genetic analysis of gD-1. A similar disulfide bond arrangement is postulated to exist in other gD homologs.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Campadelli-Fiume G., Arsenakis M., Farabegoli F., Roizman B. 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. 1988 Jan;62(1):159–167. doi: 10.1128/jvi.62.1.159-167.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Campadelli-Fiume G., Avitabile E., Fini S., Stirpe D., Arsenakis M., Roizman B. Herpes simplex virus glycoprotein D is sufficient to induce spontaneous pH-independent fusion in a cell line that constitutively expresses the glycoprotein. Virology. 1988 Oct;166(2):598–602. doi: 10.1016/0042-6822(88)90533-8. [DOI] [PubMed] [Google Scholar]
  3. Chan W. L. Protective immunization of mice with specific HSV-1 glycoproteins. Immunology. 1983 Jun;49(2):343–352. [PMC free article] [PubMed] [Google Scholar]
  4. Chen E. Y., Seeburg P. H. Supercoil sequencing: a fast and simple method for sequencing plasmid DNA. DNA. 1985 Apr;4(2):165–170. doi: 10.1089/dna.1985.4.165. [DOI] [PubMed] [Google Scholar]
  5. Chou P. Y., Fasman G. D. Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins. Biochemistry. 1974 Jan 15;13(2):211–222. doi: 10.1021/bi00699a001. [DOI] [PubMed] [Google Scholar]
  6. Chou P. Y., Fasman G. D. Prediction of protein conformation. Biochemistry. 1974 Jan 15;13(2):222–245. doi: 10.1021/bi00699a002. [DOI] [PubMed] [Google Scholar]
  7. Cohen G. H., Dietzschold B., Ponce de Leon M., Long D., Golub E., Varrichio A., Pereira L., Eisenberg R. J. Localization and synthesis of an antigenic determinant of herpes simplex virus glycoprotein D that stimulates the production of neutralizing antibody. J Virol. 1984 Jan;49(1):102–108. doi: 10.1128/jvi.49.1.102-108.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Cohen G. H., Isola V. J., Kuhns J., Berman P. W., Eisenberg R. J. Localization of discontinuous epitopes of herpes simplex virus glycoprotein D: use of a nondenaturing ("native" gel) system of polyacrylamide gel electrophoresis coupled with Western blotting. J Virol. 1986 Oct;60(1):157–166. doi: 10.1128/jvi.60.1.157-166.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Cohen G. H., Katze M., Hydrean-Stern C., Eisenberg R. J. Type-common CP-1 antigen of herpes simplex virus is associated with a 59,000-molecular-weight envelope glycoprotein. J Virol. 1978 Jul;27(1):172–181. doi: 10.1128/jvi.27.1.172-181.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Cohen G. H., Long D., Eisenberg R. J. Synthesis and processing of glycoproteins gD and gC of herpes simplex virus type 1. J Virol. 1980 Nov;36(2):429–439. doi: 10.1128/jvi.36.2.429-439.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Cohen G. H., Long D., Matthews J. T., May M., Eisenberg R. Glycopeptides of the type-common glycoprotein gD of herpes simplex virus types 1 and 2. J Virol. 1983 Jun;46(3):679–689. doi: 10.1128/jvi.46.3.679-689.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Cohen G. H., Ponce de Leon M., Nichols C. Isolation of a herpes simplex virus-specific antigenic fraction which stimulates the production of neutralizing antibody. J Virol. 1972 Nov;10(5):1021–1030. doi: 10.1128/jvi.10.5.1021-1030.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Cohen G. H., Wilcox W. C., Sodora D. L., Long D., Levin J. Z., Eisenberg R. J. Expression of herpes simplex virus type 1 glycoprotein D deletion mutants in mammalian cells. J Virol. 1988 Jun;62(6):1932–1940. doi: 10.1128/jvi.62.6.1932-1940.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Dix R. D., Mills J. Acute and latent herpes simplex virus neurological disease in mice immunized with purified virus-specific glycoproteins gB or gD. J Med Virol. 1985 Sep;17(1):9–18. doi: 10.1002/jmv.1890170103. [DOI] [PubMed] [Google Scholar]
  15. Eisenberg R. J., Cerini C. P., Heilman C. J., Joseph A. D., Dietzschold B., Golub E., Long D., Ponce de Leon M., Cohen G. H. Synthetic glycoprotein D-related peptides protect mice against herpes simplex virus challenge. J Virol. 1985 Dec;56(3):1014–1017. doi: 10.1128/jvi.56.3.1014-1017.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Eisenberg R. J., Hydrean-Stern C., Cohen G. H. Structural analysis of precursor and product forms of type-common envelope glycoprotein D (CP-1 antigen) of herpes simplex virus type 1. J Virol. 1979 Sep;31(3):608–620. doi: 10.1128/jvi.31.3.608-620.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Eisenberg R. J., Long D., Hogue-Angeletti R., Cohen G. H. Amino-terminal sequence of glycoprotein D of herpes simplex virus types 1 and 2. J Virol. 1984 Jan;49(1):265–268. doi: 10.1128/jvi.49.1.265-268.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Eisenberg R. J., Long D., Pereira L., Hampar B., Zweig M., Cohen G. H. Effect of monoclonal antibodies on limited proteolysis of native glycoprotein gD of herpes simplex virus type 1. J Virol. 1982 Feb;41(2):478–488. doi: 10.1128/jvi.41.2.478-488.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Eisenberg R. J., Long D., Ponce de Leon M., Matthews J. T., Spear P. G., Gibson M. G., Lasky L. A., Berman P., Golub E., Cohen G. H. Localization of epitopes of herpes simplex virus type 1 glycoprotein D. J Virol. 1985 Feb;53(2):634–644. doi: 10.1128/jvi.53.2.634-644.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Eisenberg R. J., Ponce de Leon M., Friedman H. M., Fries L. F., Frank M. M., Hastings J. C., Cohen G. H. Complement component C3b binds directly to purified glycoprotein C of herpes simplex virus types 1 and 2. Microb Pathog. 1987 Dec;3(6):423–435. doi: 10.1016/0882-4010(87)90012-x. [DOI] [PubMed] [Google Scholar]
  21. Eisenberg R. J., Ponce de Leon M., Pereira L., Long D., Cohen G. H. Purification of glycoprotein gD of herpes simplex virus types 1 and 2 by use of monoclonal antibody. J Virol. 1982 Mar;41(3):1099–1104. doi: 10.1128/jvi.41.3.1099-1104.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Feenstra V., Hodaie M., Johnson D. C. Deletions in herpes simplex virus glycoprotein D define nonessential and essential domains. J Virol. 1990 May;64(5):2096–2102. doi: 10.1128/jvi.64.5.2096-2102.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Flowers C. C., Eastman E. M., O'Callaghan D. J. Sequence analysis of a glycoprotein D gene homolog within the unique short segment of the EHV-1 genome. Virology. 1991 Jan;180(1):175–184. doi: 10.1016/0042-6822(91)90021-3. [DOI] [PubMed] [Google Scholar]
  24. Forrester A. J., Sullivan V., Simmons A., Blacklaws B. A., Smith G. L., Nash A. A., Minson A. C. Induction of protective immunity with antibody to herpes simplex virus type 1 glycoprotein H (gH) and analysis of the immune response to gH expressed in recombinant vaccinia virus. J Gen Virol. 1991 Feb;72(Pt 2):369–375. doi: 10.1099/0022-1317-72-2-369. [DOI] [PubMed] [Google Scholar]
  25. Fuller A. O., Spear P. G. Anti-glycoprotein D antibodies that permit adsorption but block infection by herpes simplex virus 1 prevent virion-cell fusion at the cell surface. Proc Natl Acad Sci U S A. 1987 Aug;84(15):5454–5458. doi: 10.1073/pnas.84.15.5454. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Fuller A. O., Spear P. G. 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. 1985 Aug;55(2):475–482. doi: 10.1128/jvi.55.2.475-482.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Gorman C. M., Moffat L. F., Howard B. H. Recombinant genomes which express chloramphenicol acetyltransferase in mammalian cells. Mol Cell Biol. 1982 Sep;2(9):1044–1051. doi: 10.1128/mcb.2.9.1044. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Highlander S. L., Sutherland S. L., Gage P. J., Johnson D. C., Levine M., Glorioso J. C. Neutralizing monoclonal antibodies specific for herpes simplex virus glycoprotein D inhibit virus penetration. J Virol. 1987 Nov;61(11):3356–3364. doi: 10.1128/jvi.61.11.3356-3364.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Holland T. C., Marlin S. D., Levine M., Glorioso J. Antigenic variants of herpes simplex virus selected with glycoprotein-specific monoclonal antibodies. J Virol. 1983 Feb;45(2):672–682. doi: 10.1128/jvi.45.2.672-682.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Holland T. C., Sandri-Goldin R. M., Holland L. E., Marlin S. D., Levine M., Glorioso J. C. Physical mapping of the mutation in an antigenic variant of herpes simplex virus type 1 by use of an immunoreactive plaque assay. J Virol. 1983 May;46(2):649–652. doi: 10.1128/jvi.46.2.649-652.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Isola V. J., Eisenberg R. J., Siebert G. R., Heilman C. J., Wilcox W. C., Cohen G. H. Fine mapping of antigenic site II of herpes simplex virus glycoprotein D. J Virol. 1989 May;63(5):2325–2334. doi: 10.1128/jvi.63.5.2325-2334.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Izumi K. M., Stevens J. G. Molecular and biological characterization of a herpes simplex virus type 1 (HSV-1) neuroinvasiveness gene. J Exp Med. 1990 Aug 1;172(2):487–496. doi: 10.1084/jem.172.2.487. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Johnson D. C., Burke R. L., Gregory T. Soluble forms of herpes simplex virus glycoprotein D bind to a limited number of cell surface receptors and inhibit virus entry into cells. J Virol. 1990 Jun;64(6):2569–2576. doi: 10.1128/jvi.64.6.2569-2576.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Johnson D. C., Ligas M. W. Herpes simplex viruses lacking glycoprotein D are unable to inhibit virus penetration: quantitative evidence for virus-specific cell surface receptors. J Virol. 1988 Dec;62(12):4605–4612. doi: 10.1128/jvi.62.12.4605-4612.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Johnson R. M., Spear P. G. Herpes simplex virus glycoprotein D mediates interference with herpes simplex virus infection. J Virol. 1989 Feb;63(2):819–827. doi: 10.1128/jvi.63.2.819-827.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Kousoulas K. G., Pellett P. E., Pereira L., Roizman B. Mutations affecting conformation or sequence of neutralizing epitopes identified by reactivity of viable plaques segregate from syn and ts domains of HSV-1(F) gB gene. Virology. 1984 Jun;135(2):379–394. doi: 10.1016/0042-6822(84)90194-6. [DOI] [PubMed] [Google Scholar]
  37. Kunkel T. A., Roberts J. D., Zakour R. A. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 1987;154:367–382. doi: 10.1016/0076-6879(87)54085-x. [DOI] [PubMed] [Google Scholar]
  38. Langeland N., Oyan A. M., Marsden H. S., Cross A., Glorioso J. C., Moore L. J., Haarr L. Localization on the herpes simplex virus type 1 genome of a region encoding proteins involved in adsorption to the cellular receptor. J Virol. 1990 Mar;64(3):1271–1277. doi: 10.1128/jvi.64.3.1271-1277.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. Lasky L. A., Dowbenko D. J. DNA sequence analysis of the type-common glycoprotein-D genes of herpes simplex virus types 1 and 2. DNA. 1984;3(1):23–29. doi: 10.1089/dna.1.1984.3.23. [DOI] [PubMed] [Google Scholar]
  40. Lekutis C., Olshevsky U., Furman C., Thali M., Sodroski J. Contribution of disulfide bonds in the carboxyl terminus of the human immunodeficiency virus type I gp120 glycoprotein to CD4 binding. J Acquir Immune Defic Syndr. 1992;5(1):78–81. [PubMed] [Google Scholar]
  41. Ligas M. W., Johnson D. C. A herpes simplex virus mutant in which glycoprotein D sequences are replaced by beta-galactosidase sequences binds to but is unable to penetrate into cells. J Virol. 1988 May;62(5):1486–1494. doi: 10.1128/jvi.62.5.1486-1494.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  42. Long D., Cohen G. H., Muggeridge M. I., Eisenberg R. J. Cysteine mutants of herpes simplex virus type 1 glycoprotein D exhibit temperature-sensitive properties in structure and function. J Virol. 1990 Nov;64(11):5542–5552. doi: 10.1128/jvi.64.11.5542-5552.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  43. Long D., Madara T. J., Ponce de Leon M., Cohen G. H., Montgomery P. C., Eisenberg R. J. Glycoprotein D protects mice against lethal challenge with herpes simplex virus types 1 and 2. Infect Immun. 1984 Feb;43(2):761–764. doi: 10.1128/iai.43.2.761-764.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  44. Machamer C. E., Rose J. K. Vesicular stomatitis virus G proteins with altered glycosylation sites display temperature-sensitive intracellular transport and are subject to aberrant intermolecular disulfide bonding. J Biol Chem. 1988 Apr 25;263(12):5955–5960. [PubMed] [Google Scholar]
  45. McGeoch D. J. Evolutionary relationships of virion glycoprotein genes in the S regions of alphaherpesvirus genomes. J Gen Virol. 1990 Oct;71(Pt 10):2361–2367. doi: 10.1099/0022-1317-71-10-2361. [DOI] [PubMed] [Google Scholar]
  46. Minson A. C., Hodgman T. C., Digard P., Hancock D. C., Bell S. E., Buckmaster E. A. An analysis of the biological properties of monoclonal antibodies against glycoprotein D of herpes simplex virus and identification of amino acid substitutions that confer resistance to neutralization. J Gen Virol. 1986 Jun;67(Pt 6):1001–1013. doi: 10.1099/0022-1317-67-6-1001. [DOI] [PubMed] [Google Scholar]
  47. Mishkin E. M., Fahey J. R., Kino Y., Klein R. J., Abramovitz A. S., Mento S. J. Native herpes simplex virus glycoprotein D vaccine: immunogenicity and protection in animal models. Vaccine. 1991 Mar;9(3):147–153. doi: 10.1016/0264-410x(91)90146-w. [DOI] [PubMed] [Google Scholar]
  48. Muggeridge M. I., Isola V. J., Byrn R. A., Tucker T. J., Minson A. C., Glorioso J. C., Cohen G. H., Eisenberg R. J. Antigenic analysis of a major neutralization site of herpes simplex virus glycoprotein D, using deletion mutants and monoclonal antibody-resistant mutants. J Virol. 1988 Sep;62(9):3274–3280. doi: 10.1128/jvi.62.9.3274-3280.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  49. Muggeridge M. I., Wilcox W. C., Cohen G. H., Eisenberg R. J. Identification of a site on herpes simplex virus type 1 glycoprotein D that is essential for infectivity. J Virol. 1990 Aug;64(8):3617–3626. doi: 10.1128/jvi.64.8.3617-3626.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  50. Muggeridge M. I., Wu T. T., Johnson D. C., Glorioso J. C., Eisenberg R. J., Cohen G. H. Antigenic and functional analysis of a neutralization site of HSV-1 glycoprotein D. Virology. 1990 Feb;174(2):375–387. doi: 10.1016/0042-6822(90)90091-5. [DOI] [PubMed] [Google Scholar]
  51. Noble A. G., Lee G. T., Sprague R., Parish M. L., Spear P. G. Anti-gD monoclonal antibodies inhibit cell fusion induced by herpes simplex virus type 1. Virology. 1983 Aug;129(1):218–224. doi: 10.1016/0042-6822(83)90409-9. [DOI] [PubMed] [Google Scholar]
  52. Nowak T., Wengler G. Analysis of disulfides present in the membrane proteins of the West Nile flavivirus. Virology. 1987 Jan;156(1):127–137. doi: 10.1016/0042-6822(87)90443-0. [DOI] [PubMed] [Google Scholar]
  53. Paoletti E., Lipinskas B. R., Samsonoff C., Mercer S., Panicali D. Construction of live vaccines using genetically engineered poxviruses: biological activity of vaccinia virus recombinants expressing the hepatitis B virus surface antigen and the herpes simplex virus glycoprotein D. Proc Natl Acad Sci U S A. 1984 Jan;81(1):193–197. doi: 10.1073/pnas.81.1.193. [DOI] [PMC free article] [PubMed] [Google Scholar]
  54. Para M. F., Parish M. L., Noble A. G., Spear P. G. Potent neutralizing activity associated with anti-glycoprotein D specificity among monoclonal antibodies selected for binding to herpes simplex virions. J Virol. 1985 Aug;55(2):483–488. doi: 10.1128/jvi.55.2.483-488.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  55. Petrovskis E. A., Timmins J. G., Armentrout M. A., Marchioli C. C., Yancey R. J., Jr, Post L. E. DNA sequence of the gene for pseudorabies virus gp50, a glycoprotein without N-linked glycosylation. J Virol. 1986 Aug;59(2):216–223. doi: 10.1128/jvi.59.2.216-223.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  56. Rehemtulla A., Ruf W., Edgington T. S. The integrity of the cysteine 186-cysteine 209 bond of the second disulfide loop of tissue factor is required for binding of factor VII. J Biol Chem. 1991 Jun 5;266(16):10294–10299. [PubMed] [Google Scholar]
  57. Rittenhouse J., Marcus F. Peptide mapping by polyacrylamide gel electrophoresis after cleavage at aspartyl-prolyl peptide bonds in sodium dodecyl sulfate-containing buffers. Anal Biochem. 1984 May 1;138(2):442–448. doi: 10.1016/0003-2697(84)90836-4. [DOI] [PubMed] [Google Scholar]
  58. Ross L. J., Binns M. M., Pastorek J. DNA sequence and organization of genes in a 5.5 kbp EcoRI fragment mapping in the short unique segment of Marek's disease virus (strain RB1B). J Gen Virol. 1991 Apr;72(Pt 4):949–954. doi: 10.1099/0022-1317-72-4-949. [DOI] [PubMed] [Google Scholar]
  59. Ross L. J., Binns M. M. Properties and evolutionary relationships of the Marek's disease virus homologues of protein kinase, glycoprotein D and glycoprotein I of herpes simplex virus. J Gen Virol. 1991 Apr;72(Pt 4):939–947. doi: 10.1099/0022-1317-72-4-939. [DOI] [PubMed] [Google Scholar]
  60. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  61. Scheele G., Jacoby R. Conformational changes associated with proteolytic processing of presecretory proteins allow glutathione-catalyzed formation of native disulfide bonds. J Biol Chem. 1982 Oct 25;257(20):12277–12282. [PubMed] [Google Scholar]
  62. Serafini-Cessi F., Dall'Olio F., Malagolini N., Pereira L., Campadelli-Fiume G. Comparative study on O-linked oligosaccharides of glycoprotein D of herpes simplex virus types 1 and 2. J Gen Virol. 1988 Apr;69(Pt 4):869–877. doi: 10.1099/0022-1317-69-4-869. [DOI] [PubMed] [Google Scholar]
  63. Showalter S. D., Zweig M., Hampar B. Monoclonal antibodies to herpes simplex virus type 1 proteins, including the immediate-early protein ICP 4. Infect Immun. 1981 Dec;34(3):684–692. doi: 10.1128/iai.34.3.684-692.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  64. Sodora D. L., Cohen G. H., Eisenberg R. J. Influence of asparagine-linked oligosaccharides on antigenicity, processing, and cell surface expression of herpes simplex virus type 1 glycoprotein D. J Virol. 1989 Dec;63(12):5184–5193. doi: 10.1128/jvi.63.12.5184-5193.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  65. Sodora D. L., Cohen G. H., Muggeridge M. I., Eisenberg R. J. Absence of asparagine-linked oligosaccharides from glycoprotein D of herpes simplex virus type 1 results in a structurally altered but biologically active protein. J Virol. 1991 Aug;65(8):4424–4431. doi: 10.1128/jvi.65.8.4424-4431.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  66. Sodora D. L., Eisenberg R. J., Cohen G. H. Characterization of a recombinant herpes simplex virus which expresses a glycoprotein D lacking asparagine-linked oligosaccharides. J Virol. 1991 Aug;65(8):4432–4441. doi: 10.1128/jvi.65.8.4432-4441.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  67. Suganuma N., Matzuk M. M., Boime I. Elimination of disulfide bonds affects assembly and secretion of the human chorionic gonadotropin beta subunit. J Biol Chem. 1989 Nov 15;264(32):19302–19307. [PubMed] [Google Scholar]
  68. Thornton J. M. Disulphide bridges in globular proteins. J Mol Biol. 1981 Sep 15;151(2):261–287. doi: 10.1016/0022-2836(81)90515-5. [DOI] [PubMed] [Google Scholar]
  69. Tikoo S. K., Fitzpatrick D. R., Babiuk L. A., Zamb T. J. Molecular cloning, sequencing, and expression of functional bovine herpesvirus 1 glycoprotein gIV in transfected bovine cells. J Virol. 1990 Oct;64(10):5132–5142. doi: 10.1128/jvi.64.10.5132-5142.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  70. Watson R. J. DNA sequence of the Herpes simplex virus type 2 glycoprotein D gene. Gene. 1983 Dec;26(2-3):307–312. doi: 10.1016/0378-1119(83)90203-2. [DOI] [PubMed] [Google Scholar]
  71. Watson R. J., Weis J. H., Salstrom J. S., Enquist L. W. Herpes simplex virus type-1 glycoprotein D gene: nucleotide sequence and expression in Escherichia coli. Science. 1982 Oct 22;218(4570):381–384. doi: 10.1126/science.6289440. [DOI] [PubMed] [Google Scholar]
  72. Wendland M., von Figura K., Pohlmann R. Mutational analysis of disulfide bridges in the Mr 46,000 mannose 6-phosphate receptor. Localization and role for ligand binding. J Biol Chem. 1991 Apr 15;266(11):7132–7136. [PubMed] [Google Scholar]
  73. Wilcox W. C., Long D., Sodora D. L., Eisenberg R. J., Cohen G. H. The contribution of cysteine residues to antigenicity and extent of processing of herpes simplex virus type 1 glycoprotein D. J Virol. 1988 Jun;62(6):1941–1947. doi: 10.1128/jvi.62.6.1941-1947.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  74. Williamson R. A., Marston F. A., Angal S., Koklitis P., Panico M., Morris H. R., Carne A. F., Smith B. J., Harris T. J., Freedman R. B. Disulphide bond assignment in human tissue inhibitor of metalloproteinases (TIMP). Biochem J. 1990 Jun 1;268(2):267–274. doi: 10.1042/bj2680267. [DOI] [PMC free article] [PubMed] [Google Scholar]

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