Glycoprotein C-dependent attachment of herpes simplex virus to susceptible cells leading to productive infection

Campadelli-Fiume, Gabriella; Stirpe, Daniela; Boscaro, Ambra; Avitabile, Elisa; Foà-Tomasi, Laura; Barker, David E.; Roizman, Bernard

doi:10.1016/0042-6822(90)90396-9

Cited by 67 publications

(61 citation statements)

References 37 publications

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“…First, in this article, we show that the lifespan of this complex on entry of virions into cells is relatively short (Ϸ15 min). Second, there is considerable evidence that expression of gD causes a reduced availability of receptor in transfected cells (39), a ref lection of a key function of gD that prevents reentry of newly released progeny viruses into the cells from which they have emerged (40,41). Consonant with these observations, Krummenacher et al (37) reported downmodulation of nectin1 from the surface of infected cells.…”

Section: Discussionmentioning

confidence: 79%

RETRACTED: The herpesvirus glycoproteins B and H·L are sequentially recruited to the receptor-bound gD to effect membrane fusion at virus entry

Gianni

Forghieri²,

Campadelli-Fiume³

2006

Proc. Natl. Acad. Sci. U.S.A.

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Four glycoproteins (gD, gB, gH, and gL) are required for herpes simplex virus entry into the cell or for cell–cell fusion in transfected cells. gD serves as the receptor-binding glycoprotein and as the trigger of fusion; the other three execute fusion between the viral envelope and the plasma and endocytic membranes or the membranes of adjacent cells and are highly conserved among members of the herpesvirus family. Details of the interaction of gD with gB, gH, and gL were not known. Here, we report that the four glycoproteins assemble into a complex initiated by the interaction of gD with its cellular receptor. gB is recruited to the gD–receptor complex next, even in the absence of gH·gL. gH·gL is recruited next, but only to the receptor–gD–gB ensemble. A complex with the composition receptor–gD–gB–gH·gL is assembled transiently with a life span of 15–30 min in cells exposed to virus but can also be found in infected cells and in cells committed to form polykaryocytes after transfection of the glycoprotein quartet. The results indicate that the complex assembly is a critical step in the process of virus entry and fusion, and that no viral protein other than those that participate in the complex itself is required for complex assembly. These findings imply critical protein–protein interactions among the quartet as herpes simplex virions enter the cells and at cell–cell fusion, define a specific order of recruitment, and place gH·gL as the last link in the process of glycoprotein recruitment to the complex.

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Section: Discussionmentioning

confidence: 79%

RETRACTED: The herpesvirus glycoproteins B and H·L are sequentially recruited to the receptor-bound gD to effect membrane fusion at virus entry

Gianni

Forghieri²,

Campadelli-Fiume³

2006

Proc. Natl. Acad. Sci. U.S.A.

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“…The low-affinity FGF receptor is a transmembrane protein with an extracellular heparan sulphate moiety whereas the high-affinity FGF receptor belongs to the tyrosine kinase family (Blanquet et al, 1989). Apparently, there is more than one pathway for HSV attachment and penetration, as has been suggested by Campadelli-Fiume et al (1990). WuDunn & Spear (1989) have reported that heparinase-and heparitinase-treated cells can be infected only at the highest concentrations of virus used, indicating a role for heparan sulphate in the adsorption of HSV to the cell surface.…”

Section: Discussionmentioning

confidence: 96%

“…Binding to the cell, and fusion of the viral envelope and the plasma membrane of the cell by which penetration is accomplished (Fuller & Spear, 1987;Lycke et al, 1988;Morgan et al, 1968), includes activities of glycoproteins B, C, D and H (Cai et al, 1988;Campadelli-Fiume et al, 1990;Desai et al, 1988;Kfihn et al, 1990;Ligas & Johnsson, 1988;Muggeridge et al, 1990), but it has not been established whether and how the glycoproteins interact and whether nonglycosylated envelope proteins are involved also in the attachment of the virion to the plasma membrane (Langeland et al, 1990;Spear, 1985).…”

Section: Discussionmentioning

confidence: 99%

Binding of herpes simplex virus to cellular heparan sulphate, an initial step in the adsorption process

Lycke

Johansson²,

Svennerholm³

et al. 1991

Journal of General Virology

135

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It has been suggested that heparan sulphate has a receptor function in the initial phase of the attachment of herpes simplex virus (HSV) to cells. We have studied the influence of glycosaminoglycans on cell adsorption of, and plaque formation by, HSV-1 and HSV-2, with regard to the role of saccharide structure, chain length and charge density. Heparin and highly-sulphated heparan sulphate (1-5 sulphate groups/disaccharide unit), but neither chondroitin sulphate nor dermatan sulphate, were found to compete with the cellular receptor for attachment of HSV. Heparan sulphate preparations of low sulphate content (0.5 and 0.7 sulphate groups/disaccharide unit) failed to show any significant interaction with HSV. Oligosaccharides generated by partial deaminative cleavage of heparin were used to determine the minimum molecular size required for the binding of virus; the smallest oligosaccharide which reacted with HSV was composed of l0 monosaccharide units. The importance of charge density was demonstrated more directly by subfractionation of the heparin dodecasaccharide fraction by anion-exchange HPLC. The virus-binding capacities of the four resulting dodecasaccharide subfractions increased from the least sulphated to the most heavily sulphated fraction. The results reported are discussed in relation to virus-receptor interactions involved in the attachment of HSV, including the reported binding of HSV to the fibroblast growth factor receptor.

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“…The hypothesis which best fit the data was that gD made in these cells sequestered a receptor and prevented the infecting virus from penetrating the cells (15). Subsequent studies of viral mutants selected for their ability to overcome the block to infection imposed by gD and shown to carry a mutation in their own gD gene (17) led to the conclusion that cells may contain more than one molecule capable of interacting with gD (18). The existence of a receptor for gD was also deduced from the observations that UVinactivated virions carrying gD, but not those devoid of gD, can prevent infection with wild-type virus (19) and that a recombinant anchorless gD bound in a saturable fashion to cells (16).…”

mentioning

confidence: 99%

“…The initial interaction of HSV with susceptible cells involves a low-affinity binding to cell surface heparan sulfate glycosaminoglycans mediated by glycoproteins C (gC) and probably B (gB) (5)(6)(7). Likely, this enables a subsequent more stable attachment, which culminates in penetration, possibly by fusion of the virion envelope with plasma membranes (see ref.…”

mentioning

confidence: 99%

Anti-idiotypic antibodies mimicking glycoprotein D of herpes simplex virus identify a cellular protein required for virus spread from cell to cell and virus-induced polykaryocytosis.

Huang¹,

Campadelli-Fiume²

1996

Proc. Natl. Acad. Sci. U.S.A.

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Glycoprotein D (gD) of herpes simplex virus 1 (HSV-1) is required for stable attachment and penetration of the virus into susceptible cells after initial binding. We derived anti-idiotypic antibodies to the neutralizing monoclonal antibody HD1 to gD of HSV-1. These antibodies have the properties expected of antibodies against a gD receptor. Specifically, they bind to the surface ofHEp-2, Vero, and HeLa cells susceptible to HSV infection and specifically react with a Mr 62,000 protein in these and other (143TK-and BHK) cell lines. They neutralize virion infectivity, drastically decrease plaque formation by impairing cell-to-cell spread of virions, and reduce polykaryocytosis induced by strain HFEM, which carries a syncytial (syn-) mutation. They do not affect HSV growth in a single-step cycle and plaque formation by an unrelated virus, indicating that they specifically affect the interaction of HSV gD with a cell surface receptor. We conclude that the Mr 62,000 cell surface protein interacts with gD to enable spread of HSV-1 from cell to cell and virusinduced polykaryocytosis.

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Glycoprotein C-dependent attachment of herpes simplex virus to susceptible cells leading to productive infection

Cited by 67 publications

References 37 publications

RETRACTED: The herpesvirus glycoproteins B and H·L are sequentially recruited to the receptor-bound gD to effect membrane fusion at virus entry

RETRACTED: The herpesvirus glycoproteins B and H·L are sequentially recruited to the receptor-bound gD to effect membrane fusion at virus entry

Binding of herpes simplex virus to cellular heparan sulphate, an initial step in the adsorption process

Anti-idiotypic antibodies mimicking glycoprotein D of herpes simplex virus identify a cellular protein required for virus spread from cell to cell and virus-induced polykaryocytosis.

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