Identification and characterization of a 30K glycoprotein of herpes simplex virus type 2

K. F. Qin, Andy Yu, Q. Gao, M. X. Wang, S. Z. Jiang

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

A herpes simplex virus type 2 (HSV-2) type-specific monoclonal antibody (MAb), CH-A9, precipitated a glycoprotein with an M(r) of approximately 30000 (g30K) from extracts of HSV-2-infected BHK cells labelled with [3H]leucine, [14C]fructose or [3H]glucosamine. The M(r) of this glycoprotein is lower than those of other HSV glycoproteins. Immunoassays of BHK cells infected with HSV-I-HSV-2 intertypic recombinants localized the gene encoding the target antigen of MAb CH-A9 to the unique long (U(L)) region at map units 0.490 to 0.564. Tunicamycin effectively inhibits N-linked glycosylation of g30K, which suggests that g30K may be modified by addition of N-linked oligosaccharides and that the amino acid sequence may contain Asn-X-Ser or Asn-X-Thr. The g30K was also purified on an immunoadsorbent column consisting of MAb CH-A9 linked to Sepharose 4B and was shown to be an HSV-2 type-specific antigen by indirect ELISA. The glycoprotein could induce HSV-2 type-specific neutralizing antibody in BALB/c mice. This evidence suggests that g30K may be a novel glycoprotein of HSV-2.

Original languageEnglish (US)
Pages (from-to)1693-1701
Number of pages9
JournalJournal of General Virology
Volume73
Issue number7
StatePublished - 1992
Externally publishedYes

Fingerprint

Human Herpesvirus 2
Glycoproteins
Monoclonal Antibodies
Antigens
Tunicamycin
Immunosorbents
Glucosamine
Neutralizing Antibodies
Fructose
Oligosaccharides
Glycosylation
Immunoassay
Leucine
Sepharose
Amino Acid Sequence
Enzyme-Linked Immunosorbent Assay
Genes

ASJC Scopus subject areas

  • Immunology
  • Virology

Cite this

Identification and characterization of a 30K glycoprotein of herpes simplex virus type 2. / Qin, K. F.; Yu, Andy; Gao, Q.; Wang, M. X.; Jiang, S. Z.

In: Journal of General Virology, Vol. 73, No. 7, 1992, p. 1693-1701.

Research output: Contribution to journalArticle

Qin, K. F. ; Yu, Andy ; Gao, Q. ; Wang, M. X. ; Jiang, S. Z. / Identification and characterization of a 30K glycoprotein of herpes simplex virus type 2. In: Journal of General Virology. 1992 ; Vol. 73, No. 7. pp. 1693-1701.
@article{4e9f253ccf414394a86ab583563fe5c3,
title = "Identification and characterization of a 30K glycoprotein of herpes simplex virus type 2",
abstract = "A herpes simplex virus type 2 (HSV-2) type-specific monoclonal antibody (MAb), CH-A9, precipitated a glycoprotein with an M(r) of approximately 30000 (g30K) from extracts of HSV-2-infected BHK cells labelled with [3H]leucine, [14C]fructose or [3H]glucosamine. The M(r) of this glycoprotein is lower than those of other HSV glycoproteins. Immunoassays of BHK cells infected with HSV-I-HSV-2 intertypic recombinants localized the gene encoding the target antigen of MAb CH-A9 to the unique long (U(L)) region at map units 0.490 to 0.564. Tunicamycin effectively inhibits N-linked glycosylation of g30K, which suggests that g30K may be modified by addition of N-linked oligosaccharides and that the amino acid sequence may contain Asn-X-Ser or Asn-X-Thr. The g30K was also purified on an immunoadsorbent column consisting of MAb CH-A9 linked to Sepharose 4B and was shown to be an HSV-2 type-specific antigen by indirect ELISA. The glycoprotein could induce HSV-2 type-specific neutralizing antibody in BALB/c mice. This evidence suggests that g30K may be a novel glycoprotein of HSV-2.",
author = "Qin, {K. F.} and Andy Yu and Q. Gao and Wang, {M. X.} and Jiang, {S. Z.}",
year = "1992",
language = "English (US)",
volume = "73",
pages = "1693--1701",
journal = "Journal of General Virology",
issn = "0022-1317",
publisher = "Society for General Microbiology",
number = "7",

}

TY - JOUR

T1 - Identification and characterization of a 30K glycoprotein of herpes simplex virus type 2

AU - Qin, K. F.

AU - Yu, Andy

AU - Gao, Q.

AU - Wang, M. X.

AU - Jiang, S. Z.

PY - 1992

Y1 - 1992

N2 - A herpes simplex virus type 2 (HSV-2) type-specific monoclonal antibody (MAb), CH-A9, precipitated a glycoprotein with an M(r) of approximately 30000 (g30K) from extracts of HSV-2-infected BHK cells labelled with [3H]leucine, [14C]fructose or [3H]glucosamine. The M(r) of this glycoprotein is lower than those of other HSV glycoproteins. Immunoassays of BHK cells infected with HSV-I-HSV-2 intertypic recombinants localized the gene encoding the target antigen of MAb CH-A9 to the unique long (U(L)) region at map units 0.490 to 0.564. Tunicamycin effectively inhibits N-linked glycosylation of g30K, which suggests that g30K may be modified by addition of N-linked oligosaccharides and that the amino acid sequence may contain Asn-X-Ser or Asn-X-Thr. The g30K was also purified on an immunoadsorbent column consisting of MAb CH-A9 linked to Sepharose 4B and was shown to be an HSV-2 type-specific antigen by indirect ELISA. The glycoprotein could induce HSV-2 type-specific neutralizing antibody in BALB/c mice. This evidence suggests that g30K may be a novel glycoprotein of HSV-2.

AB - A herpes simplex virus type 2 (HSV-2) type-specific monoclonal antibody (MAb), CH-A9, precipitated a glycoprotein with an M(r) of approximately 30000 (g30K) from extracts of HSV-2-infected BHK cells labelled with [3H]leucine, [14C]fructose or [3H]glucosamine. The M(r) of this glycoprotein is lower than those of other HSV glycoproteins. Immunoassays of BHK cells infected with HSV-I-HSV-2 intertypic recombinants localized the gene encoding the target antigen of MAb CH-A9 to the unique long (U(L)) region at map units 0.490 to 0.564. Tunicamycin effectively inhibits N-linked glycosylation of g30K, which suggests that g30K may be modified by addition of N-linked oligosaccharides and that the amino acid sequence may contain Asn-X-Ser or Asn-X-Thr. The g30K was also purified on an immunoadsorbent column consisting of MAb CH-A9 linked to Sepharose 4B and was shown to be an HSV-2 type-specific antigen by indirect ELISA. The glycoprotein could induce HSV-2 type-specific neutralizing antibody in BALB/c mice. This evidence suggests that g30K may be a novel glycoprotein of HSV-2.

UR - http://www.scopus.com/inward/record.url?scp=0026781597&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026781597&partnerID=8YFLogxK

M3 - Article

C2 - 1321210

AN - SCOPUS:0026781597

VL - 73

SP - 1693

EP - 1701

JO - Journal of General Virology

JF - Journal of General Virology

SN - 0022-1317

IS - 7

ER -