Binding of human cytomegalovirus to sulfated glucuronyl glycosphingolipids and their inhibitory effects on the infection

K. Ogawa-Goto, Yujiro Arao, Y. Ito, T. Ogawa, T. Abe, T. Kurata, S. Irie, H. Akanuma

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Interactions between human cytomegalovirus (HCMV) and various carbohydrate structures were analysed using sulfated glucuronyl glycosphingolipids (SGGLs) and the structurally related glycosphingolipids (GLs). A thin-layer chromatography-overlay assay and a solid-phase binding assay revealed that HCMV strongly bound to sulfated glucuronyl lactosaminylparagloboside, one of the SGGLs having the repeating lactosamine structure (3Galβ1-4GlcNAc1-)2 in addition to the 3-O-sulfated glucuronyl moiety. The virus bound less strongly to other 3-O-sulfated GLs, which included sulfated glucuronyl paragloboside and cerebroside sulfate ester, and also to (3Galβ1-4GlcNAc1-)2-containing GLs that included nLc6Cer. Thus, a (3Galβ1-4GlcNAc1-)2 and a 3-O-sulfated saccharide seem to be important structures for the binding by HCMV. When virus particles were preincubated with these GLs, inhibitory effects were observed both on expression of the viral immediate-early gene and on plaque formation by HCMV. These effects were very well correlated with the abilities of the GLs to bind to the virus. Pretreatment of host cells with HNK-1 monoclonal antibody, which specifically recognizes SGGLs, resulted in partial inhibition of plaque formation by HCMV. These results clearly show that HCMV recognizes and binds to the sulfated carbohydrate structure in SGGL and also suggest that binding of HCMV to the specific sugar structure may play an important role in HCMV infection.

Original languageEnglish
Pages (from-to)2533-2541
Number of pages9
JournalJournal of General Virology
Volume79
Issue number10
Publication statusPublished - Oct 1998
Externally publishedYes

Fingerprint

Glycosphingolipids
Cytomegalovirus
Infection
Carbohydrates
Viruses
Immediate-Early Genes
Viral Genes
Cytomegalovirus Infections
Thin Layer Chromatography
Virion
Esters
Monoclonal Antibodies

ASJC Scopus subject areas

  • Virology
  • Immunology

Cite this

Binding of human cytomegalovirus to sulfated glucuronyl glycosphingolipids and their inhibitory effects on the infection. / Ogawa-Goto, K.; Arao, Yujiro; Ito, Y.; Ogawa, T.; Abe, T.; Kurata, T.; Irie, S.; Akanuma, H.

In: Journal of General Virology, Vol. 79, No. 10, 10.1998, p. 2533-2541.

Research output: Contribution to journalArticle

Ogawa-Goto, K, Arao, Y, Ito, Y, Ogawa, T, Abe, T, Kurata, T, Irie, S & Akanuma, H 1998, 'Binding of human cytomegalovirus to sulfated glucuronyl glycosphingolipids and their inhibitory effects on the infection', Journal of General Virology, vol. 79, no. 10, pp. 2533-2541.
Ogawa-Goto, K. ; Arao, Yujiro ; Ito, Y. ; Ogawa, T. ; Abe, T. ; Kurata, T. ; Irie, S. ; Akanuma, H. / Binding of human cytomegalovirus to sulfated glucuronyl glycosphingolipids and their inhibitory effects on the infection. In: Journal of General Virology. 1998 ; Vol. 79, No. 10. pp. 2533-2541.
@article{0e91064bbbdf46b1b3df70abee9ce3d1,
title = "Binding of human cytomegalovirus to sulfated glucuronyl glycosphingolipids and their inhibitory effects on the infection",
abstract = "Interactions between human cytomegalovirus (HCMV) and various carbohydrate structures were analysed using sulfated glucuronyl glycosphingolipids (SGGLs) and the structurally related glycosphingolipids (GLs). A thin-layer chromatography-overlay assay and a solid-phase binding assay revealed that HCMV strongly bound to sulfated glucuronyl lactosaminylparagloboside, one of the SGGLs having the repeating lactosamine structure (3Galβ1-4GlcNAc1-)2 in addition to the 3-O-sulfated glucuronyl moiety. The virus bound less strongly to other 3-O-sulfated GLs, which included sulfated glucuronyl paragloboside and cerebroside sulfate ester, and also to (3Galβ1-4GlcNAc1-)2-containing GLs that included nLc6Cer. Thus, a (3Galβ1-4GlcNAc1-)2 and a 3-O-sulfated saccharide seem to be important structures for the binding by HCMV. When virus particles were preincubated with these GLs, inhibitory effects were observed both on expression of the viral immediate-early gene and on plaque formation by HCMV. These effects were very well correlated with the abilities of the GLs to bind to the virus. Pretreatment of host cells with HNK-1 monoclonal antibody, which specifically recognizes SGGLs, resulted in partial inhibition of plaque formation by HCMV. These results clearly show that HCMV recognizes and binds to the sulfated carbohydrate structure in SGGL and also suggest that binding of HCMV to the specific sugar structure may play an important role in HCMV infection.",
author = "K. Ogawa-Goto and Yujiro Arao and Y. Ito and T. Ogawa and T. Abe and T. Kurata and S. Irie and H. Akanuma",
year = "1998",
month = "10",
language = "English",
volume = "79",
pages = "2533--2541",
journal = "Journal of General Virology",
issn = "0022-1317",
publisher = "Society for General Microbiology",
number = "10",

}

TY - JOUR

T1 - Binding of human cytomegalovirus to sulfated glucuronyl glycosphingolipids and their inhibitory effects on the infection

AU - Ogawa-Goto, K.

AU - Arao, Yujiro

AU - Ito, Y.

AU - Ogawa, T.

AU - Abe, T.

AU - Kurata, T.

AU - Irie, S.

AU - Akanuma, H.

PY - 1998/10

Y1 - 1998/10

N2 - Interactions between human cytomegalovirus (HCMV) and various carbohydrate structures were analysed using sulfated glucuronyl glycosphingolipids (SGGLs) and the structurally related glycosphingolipids (GLs). A thin-layer chromatography-overlay assay and a solid-phase binding assay revealed that HCMV strongly bound to sulfated glucuronyl lactosaminylparagloboside, one of the SGGLs having the repeating lactosamine structure (3Galβ1-4GlcNAc1-)2 in addition to the 3-O-sulfated glucuronyl moiety. The virus bound less strongly to other 3-O-sulfated GLs, which included sulfated glucuronyl paragloboside and cerebroside sulfate ester, and also to (3Galβ1-4GlcNAc1-)2-containing GLs that included nLc6Cer. Thus, a (3Galβ1-4GlcNAc1-)2 and a 3-O-sulfated saccharide seem to be important structures for the binding by HCMV. When virus particles were preincubated with these GLs, inhibitory effects were observed both on expression of the viral immediate-early gene and on plaque formation by HCMV. These effects were very well correlated with the abilities of the GLs to bind to the virus. Pretreatment of host cells with HNK-1 monoclonal antibody, which specifically recognizes SGGLs, resulted in partial inhibition of plaque formation by HCMV. These results clearly show that HCMV recognizes and binds to the sulfated carbohydrate structure in SGGL and also suggest that binding of HCMV to the specific sugar structure may play an important role in HCMV infection.

AB - Interactions between human cytomegalovirus (HCMV) and various carbohydrate structures were analysed using sulfated glucuronyl glycosphingolipids (SGGLs) and the structurally related glycosphingolipids (GLs). A thin-layer chromatography-overlay assay and a solid-phase binding assay revealed that HCMV strongly bound to sulfated glucuronyl lactosaminylparagloboside, one of the SGGLs having the repeating lactosamine structure (3Galβ1-4GlcNAc1-)2 in addition to the 3-O-sulfated glucuronyl moiety. The virus bound less strongly to other 3-O-sulfated GLs, which included sulfated glucuronyl paragloboside and cerebroside sulfate ester, and also to (3Galβ1-4GlcNAc1-)2-containing GLs that included nLc6Cer. Thus, a (3Galβ1-4GlcNAc1-)2 and a 3-O-sulfated saccharide seem to be important structures for the binding by HCMV. When virus particles were preincubated with these GLs, inhibitory effects were observed both on expression of the viral immediate-early gene and on plaque formation by HCMV. These effects were very well correlated with the abilities of the GLs to bind to the virus. Pretreatment of host cells with HNK-1 monoclonal antibody, which specifically recognizes SGGLs, resulted in partial inhibition of plaque formation by HCMV. These results clearly show that HCMV recognizes and binds to the sulfated carbohydrate structure in SGGL and also suggest that binding of HCMV to the specific sugar structure may play an important role in HCMV infection.

UR - http://www.scopus.com/inward/record.url?scp=0031693035&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031693035&partnerID=8YFLogxK

M3 - Article

C2 - 9780061

AN - SCOPUS:0031693035

VL - 79

SP - 2533

EP - 2541

JO - Journal of General Virology

JF - Journal of General Virology

SN - 0022-1317

IS - 10

ER -