The expression of the proteins of equine herpesvirus 1 which share homology with herpes simplex virus 1 glycoproteins H and L

Stokes, A; Alber, Dagmar; Greensill, Julie; Amellal, Bahia; Carvalho, Rogério Falleiros; Taylor, Lesley A.; Doel, T. R.; Killington, R. A.; Halliburton, I. W.; Meredith, David M.

doi:10.1016/0168-1702(95)01256-7

Cited by 26 publications

(15 citation statements)

References 34 publications

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“…In all human and animal herpesviruses studied to date, homologs of glycoprotein H (gH) and glycoprotein L (gL) have been found (9,14,15,17,18,21,22,26,32,34,35,40,41,43,44). These two envelope glycoproteins, which associate to form a gH-gL complex, have been implicated as key participants in fusion events that are critical to herpesvirus infection.…”

mentioning

confidence: 99%

The Human Herpesvirus 6 U100 Gene Product Is the Third Component of the gH-gL Glycoprotein Complex on the Viral Envelope

Mori

Akkapaiboon

Yang

et al. 2003

J Virol

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The human herpesvirus 6 (HHV-6) variant A U100 gene encodes the third component of the glycoprotein H (gH)-glycoprotein L (gL)-containing complex. Glycosidase digestion analysis showed that the U100 gene products are glycoproteins consisting of an 80-kDa protein with complex N-linked oligosaccharides and a 74-kDa protein with immature, high-mannose N-linked oligosaccharides. Based on these characteristics, we designated the U100 gene products glycoprotein Q (gQ). Only the 80-kDa form of gQ was coimmunoprecipitated with an anti-gH antibody, suggesting that the 80-kDa protein associates with the gH-gL complex in HHV-6-infected cells. Furthermore, the complex was detected in purified virions, suggesting that it may play an important role in viral entry.

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mentioning

confidence: 99%

The Human Herpesvirus 6 U100 Gene Product Is the Third Component of the gH-gL Glycoprotein Complex on the Viral Envelope

Mori

Akkapaiboon

Yang

et al. 2003

J Virol

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“…Similar to other alphaherpesviruses, EHV-1 also enters cells through direct fusion at the plasma membrane, a process that is mediated by gB, gC, gD, and possibly the gH-gL complex (6,28,32,40,49) and by a cellular receptor which has not been identified conclusively to date (10). Recently, it was shown by electron microscopy that EHV-1 can enter cells not only via direct fusion at the plasma membrane but also via a nonclassical endocytic/ phagocytic entry pathway (11).…”

mentioning

confidence: 99%

Equine Herpesvirus 1 Entry via Endocytosis Is Facilitated by αV Integrins and an RSD Motif in Glycoprotein D

Walle

Peters

VanderVen

et al. 2008

J Virol

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Equine herpesvirus 1 (EHV-1) is a member of the Alphaherpesvirinae, and its broad tissue tropism suggests that EHV-1 may use multiple receptors to initiate virus entry. EHV-1 entry was thought to occur exclusively through fusion at the plasma membrane, but recently entry via the endocytic/phagocytic pathway was reported for Chinese hamster ovary cells (CHO-K1 cells). Here we show that cellular integrins, and more specifically those recognizing RGD motifs such as ␣V␤5, are important during the early steps of EHV-1 entry via endocytosis in CHO-K1 cells. Moreover, mutational analysis revealed that an RSD motif in the EHV-1 envelope glycoprotein D (gD) is critical for entry via endocytosis. In addition, we show that EHV-1 enters peripheral blood mononuclear cells predominantly via the endocytic pathway, whereas in equine endothelial cells entry occurs mainly via fusion at the plasma membrane. Taken together, the data in this study provide evidence that EHV-1 entry via endocytosis is triggered by the interaction between cellular integrins and the RSD motif present in gD and, moreover, that EHV-1 uses different cellular entry pathways to infect important target cell populations of its natural host.

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“…Glycoprotein gL was shown to promote the correct folding and transport to the cell surface of gH in infected cells. This association has also been described for other herpesviruses (Kaye et al, 1992 ;Liu et al, 1993 ;Forghani et al, 1994 ;Stokes et al, 1996 ;van Drunen Littel-van den Hurk, 1996). In the present study, the biochemical properties of gH (gp110) and gL (gp45-55) of BHV-4 were determined and complex formation between the two glycoproteins was demonstrated both in infected cells and in virions.…”

Section: Discussionmentioning

confidence: 83%

“…However, except for a few observations (Roop et al, 1993 ;Novotny et al, 1996 ;Duus & Grose, 1996) the precise functions of gL are still poorly understood. The two glycoproteins have been shown to be inevitably associated on the surface of infected cells forming a complex of either two (Hutchinson et al, 1992 ;Kaye et al, 1992 ;Liu et al, 1993 ;Forghani et al, 1994 ;Stokes et al, 1996 ;van Drunen Littel-van den Hurk, 1996) or three proteins (Yaswen et al, 1993 ;Li et al, 1995). Indeed, in the γ " herpesvirus Epstein-Barr virus (EBV), a third glycoprotein, gp42\38, which is the translation product of the BZLF2 open reading frame (ORF), is associated with the gH and gL homologues and seems to be directly involved in the penetration of EBV into B lymphocytes (Li et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

Analysis of the biochemical properties of, and complex formation between, glycoproteins H and L of the gamma2 herpesvirus bovine herpesvirus-4.

Lomonte

Filée²,

Lyaku

et al. 1997

Journal of General Virology

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Genes encoding glycoprotein gH and gL homologues were localized in the genome of the gammaherpesvirus bovine herpesvirus-4 (BHV-4). Both genes were sequenced and glutathione S-transferase fusion proteins were produced and used to immunize rabbits against the translation products of the two genes. The anti-gH serum recognized a protein with an apparent molecular mass (MM) of 110 kDa both in infected cells and in virions. This protein was sensitive to endo-β-N-acetylglucosaminase-H (endoH) and endoglycosidase F-N-glycosidase F (endoF-PNGaseF) digestion. A protein with the same relative mobility was immunoprecipitated from infected cells radiolabelled with [ 3 H]glucosamine which confirmed that this product (gp110), now designated BHV-4 gH, was glycosylated. Western blotting with the anti-gL serum detected in infected cells a product with an apparent

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The expression of the proteins of equine herpesvirus 1 which share homology with herpes simplex virus 1 glycoproteins H and L

Cited by 26 publications

References 34 publications

The Human Herpesvirus 6 U100 Gene Product Is the Third Component of the gH-gL Glycoprotein Complex on the Viral Envelope

The Human Herpesvirus 6 U100 Gene Product Is the Third Component of the gH-gL Glycoprotein Complex on the Viral Envelope

Equine Herpesvirus 1 Entry via Endocytosis Is Facilitated by αV Integrins and an RSD Motif in Glycoprotein D

Analysis of the biochemical properties of, and complex formation between, glycoproteins H and L of the gamma2 herpesvirus bovine herpesvirus-4.

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