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. 1984 Jul;51(1):263–265. doi: 10.1128/jvi.51.1.263-265.1984

Localization of a type-specific antigenic site on herpes simplex virus type 2 glycoprotein D.

W E Rawls, N Balachandran, G Sisson, R J Watson
PMCID: PMC254429  PMID: 6202883

Abstract

A herpes simplex virus type 1 strain isolated from a recurrent lesion of the nose reacted with monoclonal antibodies recognizing a type 2-specific site on glycoprotein D but not with monoclonal antibodies recognizing other type 2-specific sites. DNA sequence analysis of the glycoprotein D gene of the isolate revealed a single nucleotide alteration which changed the codon for asparagine to one encoding histidine at amino acid 97 in the protein. Histidine is located at this position in glycoprotein of herpes simplex virus type 2; thus, the monoclonal antibody 17 beta A3 recognizes an epitope located at this region of the protein.

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Selected References

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

  1. Balachandran N., Frame B., Chernesky M., Kraiselburd E., Kouri Y., Garcia D., Lavery C., Rawls W. E. Identification and typing of herpes simplex viruses with monoclonal antibodies. J Clin Microbiol. 1982 Jul;16(1):205–208. doi: 10.1128/jcm.16.1.205-208.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Balachandran N., Harnish D., Rawls W. E., Bacchetti S. Glycoproteins of herpes simplex virus type 2 as defined by monoclonal antibodies. J Virol. 1982 Oct;44(1):344–355. doi: 10.1128/jvi.44.1.344-355.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. 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]
  4. 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]
  5. Eisenberg R. J., Ponce de Leon M., Cohen G. H. Comparative structural analysis of glycoprotein gD of herpes simplex virus types 1 and 2. J Virol. 1980 Aug;35(2):428–435. doi: 10.1128/jvi.35.2.428-435.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Heilman C. J., Jr, Zweig M., Hampar B. Herpes simplex virus type 1 and 2 intracellular p40: type-specific and cross-reactive antigenic determinants on peptides generated by partial proteolysis. J Virol. 1981 Nov;40(2):508–515. doi: 10.1128/jvi.40.2.508-515.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. 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]
  8. Killington R. A., Newhook L., Balachandran N., Rawls W. E., Bacchetti S. Production of hybrid cell lines secreting antibodies to herpes simplex virus type 2. J Virol Methods. 1981 Mar;2(4):223–236. doi: 10.1016/0166-0934(81)90012-4. [DOI] [PubMed] [Google Scholar]
  9. Maxam A. M., Gilbert W. Sequencing end-labeled DNA with base-specific chemical cleavages. Methods Enzymol. 1980;65(1):499–560. doi: 10.1016/s0076-6879(80)65059-9. [DOI] [PubMed] [Google Scholar]
  10. Norrild B. Immunochemistry of herpes simplex virus glycoproteins. Curr Top Microbiol Immunol. 1980;90:67–106. doi: 10.1007/978-3-642-67717-5_4. [DOI] [PubMed] [Google Scholar]
  11. Pereira L., Dondero D. V., Gallo D., Devlin V., Woodie J. D. Serological analysis of herpes simplex virus types 1 and 2 with monoclonal antibodies. Infect Immun. 1982 Jan;35(1):363–367. doi: 10.1128/iai.35.1.363-367.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Pereira L., Klassen T., Baringer J. R. Type-common and type-specific monoclonal antibody to herpes simplex virus type 1. Infect Immun. 1980 Aug;29(2):724–732. doi: 10.1128/iai.29.2.724-732.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Powell K. L., Buchan A., Sim C., Watson D. H. Type-specific protein in herpes simplex virus envelope reacts with neutralising antibody. Nature. 1974 May 24;249(455):360–361. doi: 10.1038/249360a0. [DOI] [PubMed] [Google Scholar]
  14. Sim C., Watson D. H. The role of type specific and cross reacting structural antigens in the neutralization of herpes simplex virus types 1 and 2. J Gen Virol. 1973 May;19(2):217–233. doi: 10.1099/0022-1317-19-2-217. [DOI] [PubMed] [Google Scholar]
  15. 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]
  16. Watson R. J., Vande Woude G. F. DNA sequence of an immediate-early gene (IEmRNA-5) of herpes simplex virus type I. Nucleic Acids Res. 1982 Feb 11;10(3):979–991. doi: 10.1093/nar/10.3.979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. 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]
  18. Zweig M., Heilman C. J., Jr, Rabin H., Hopkins R. F., 3rd, Neubauer R. H., Hampar B. Production of monoclonal antibodies against nucleocapsid proteins of herpes simplex virus types 1 and 2. J Virol. 1979 Nov;32(2):676–678. doi: 10.1128/jvi.32.2.676-678.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]

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