Equine herpesvirus-4 glycoprotein G is secreted as a disulphide-linked homodimer and is present as two homodimeric species in the virion.

Drummer, Heidi E; Studdert, Michael J.; Crabb, Brendan S.

doi:10.1099/0022-1317-79-5-1205

Cited by 23 publications

(30 citation statements)

References 35 publications

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“…Both EHV-1 and EHV-4 are economically important pathogens of horses, and each encodes gG as membrane-associated and secreted forms, the latter representing moieties of approximately 55 to 60 kDa (17,26,59). The full-length, membraneanchored form of EHV-1 gG has vCKBP properties, since recombinant gG expressed on the surfaces of insect cells was capable of binding human CXCL1 and CXCL8 (14).…”

Section: Ehv-1 and Ehv-4 Ggmentioning

confidence: 99%

“…gG is unusual compared to other herpesvirus glycoproteins, since it also gets secreted into the media of infected cells. gG can therefore exist in three isoforms: a full-length membrane-bound form, a smaller membrane-bound form, and a secreted form (26). The latter two isoforms appear to be the results of a proteolytic cleavage event of the full-length membrane-bound form (26).…”

Section: Vil-8mentioning

confidence: 99%

“…gG can therefore exist in three isoforms: a full-length membrane-bound form, a smaller membrane-bound form, and a secreted form (26). The latter two isoforms appear to be the results of a proteolytic cleavage event of the full-length membrane-bound form (26). Alphaherpesviral gG can interfere at different distinct stages of che- mokine action and therefore constitutes yet another immunoevasion tool used by alphaherpesviruses (Fig.…”

Section: Vil-8mentioning

confidence: 99%

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Alphaherpesviruses and Chemokines: Pas de Deux Not Yet Brought to Perfection

Walle

Jarosinski

Osterrieder

2008

J Virol

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Section: Ehv-1 and Ehv-4 Ggmentioning

confidence: 99%

Section: Vil-8mentioning

confidence: 99%

Section: Vil-8mentioning

confidence: 99%

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Alphaherpesviruses and Chemokines: Pas de Deux Not Yet Brought to Perfection

Walle

Jarosinski

Osterrieder

2008

J Virol

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“…Glycoprotein G is expressed early in the infectious cycle and was shown to be nonessential for virus growth in vitro (11)(12)(13). Moreover, gG is unusual in that it can exist in three isoforms: a 68-kDa full-length membrane-bound form, a 12-kDa membrane-bound form, and a 60-kDa form, which is secreted from infected cells (14). The latter two isoforms appear to be the result of a proteolytic event from the 68-kDa full-length form resulting in the 12-kDa C-and the 60-kDa N-terminal moiety, respectively.…”

mentioning

confidence: 99%

Herpesvirus Chemokine-Binding Glycoprotein G (gG) Efficiently Inhibits Neutrophil Chemotaxis In Vitro and In Vivo

Walle

May

Sukhumavasi

et al. 2007

The Journal of Immunology

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Glycoprotein G (gG) of alphaherpesviruses has been described to function as a viral chemokine-binding protein (vCKBP). More recently, mutant viruses devoid of gG have been shown to result in increased virulence, but it remained unclear whether the potential of gG to serve as a vCKBP is responsible for this observation. In this study, we used equine herpesvirus type 1 (EHV-1) as a model to study the pathophysiological importance of vCKBP activity. First, in vitro chemotaxis assays studying migration of immune cells, an important function of chemokines, were established. In such assays, supernatants of EHV-1-infected cells significantly inhibited IL-8-induced chemotaxis of equine neutrophils. Identification of gG as the responsible vCKBP was achieved by repeating similar experiments with supernatants from cells infected with a gG-negative mutant, which were unable to alter IL-8-induced equine neutrophil migration. Furthermore, rEHV-1 gG was able to significantly reduce neutrophil migration, establishing gG as a bona fide vCKBP. Second, and importantly, in vivo analyses in a murine model of EHV-1 infection showed that neutrophil migration in the target organ lung was significantly reduced in the presence of gG. In summary, we demonstrate for the first time that EHV-1 gG not only binds to chemokines but is also capable of inhibiting their chemotactic function both in vitro and in vivo, thereby contributing to viral pathogenesis and virulence.

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“…Radioimmunoprecipitation (RIP) was conducted as described previously (18), with minor alterations. Radiolabeled cells were collected by centrifugation, washed twice in PBS as described above, and solubilized in RIP lysis buffer (0.05 M Tris-HCl [pH 7.5], 1% Triton X-100, 0.6 M KCl, 1 mM phenylmethylsulfonyl fluoride), sonicated briefly, and centrifuged at 100,000 ϫ g at 4°C for 30 min.…”

Section: Methodsmentioning

confidence: 99%

Homologue of Macrophage-Activating Lipoprotein in Mycoplasma gallisepticum Is Not Essential for Growth and Pathogenicity in Tracheal Organ Cultures

et al. 2003

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While the genomes of a number of Mycoplasma species have been fully determined, there has been limited characterization of which genes are essential. The surface protein (p47) identified by monoclonal antibody B3 is the basis for an enzyme-linked immunosorbent assay for serological detection of Mycoplasma gallisepticum infection and appears to be constitutively expressed. Its gene was cloned, and the DNA sequence was determined. Subsequent analysis of the p47 amino acid sequence and searches of DNA databases found homologous gene sequences in the genomes of M. pneumoniae and M. genitalium and identity with a gene family in Ureaplasma urealyticum and genes in M. agalactiae and M. fermentans. The proteins encoded by these genes were found to belong to a family of basic membrane proteins (BMP) that are found in a wide range of bacteria, including a number of pathogens. Several of the BMP family members, including p47, contain selective lipoprotein-associated motifs that are found in macrophage-activating lipoprotein 404 of M. fermentans and lipoprotein P48 of M. agalactiae. The p47 gene was predicted to encode a 59-kDa peptide, but affinity-purified p47 had a molecular mass of approximately 47 kDa, as determined by polyacrylamide gel analysis. Analysis of native and recombinant p47 by mass peptide fingerprinting revealed the absence of the carboxyl end of the protein encoded by the p47 gene in native p47, which would account for the difference seen in the predicted and measured molecular weights and indicated posttranslational cleavage of the lipoprotein at its carboxyl end. A DNA construct containing the p47 gene interrupted by the gene encoding tetracycline resistance was used to transform M. gallisepticum cells. A tetracycline-resistant mycoplasma clone, P2, contained the construct inserted within the genomic p47 gene, with crossovers occurring between 73 bp upstream and 304 bp downstream of the inserted tetracycline resistance gene. The absence of p47 protein in clone P2 was determined by the lack of reactivity with rabbit anti-p47 sera or monoclonal antibody B3 in Western blots of whole-cell proteins. There was no difference between the p47 ؊ mutant and wild-type M. gallisepticum in pathogenicity in chicken tracheal organ cultures. Thus, p47, although homologous to genes that occur in many prokaryotes, is not essential for growth in vitro or for attachment and the initial stages of pathogenesis in chickens.Mycoplasmas are parasitic species that have evolved through reductive evolution from gram-positive bacteria and have developed complex relationships with their hosts (39,40). In many of their mammalian hosts, they produce chronic infections causing respiratory, arthritic, and urogenital diseases. The absence of a cell wall has been associated with an increase in the number and functionality of lipoproteins in mycoplasmas and the development of strategies to evade or control the immunological environment of the host. A number of lipoproteins have been shown to be subject to antigenic and/or phase variation (4...

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Equine herpesvirus-4 glycoprotein G is secreted as a disulphide-linked homodimer and is present as two homodimeric species in the virion.

Cited by 23 publications

References 35 publications

Alphaherpesviruses and Chemokines: Pas de Deux Not Yet Brought to Perfection

Alphaherpesviruses and Chemokines: Pas de Deux Not Yet Brought to Perfection

Herpesvirus Chemokine-Binding Glycoprotein G (gG) Efficiently Inhibits Neutrophil Chemotaxis In Vitro and In Vivo

Homologue of Macrophage-Activating Lipoprotein in Mycoplasma gallisepticum Is Not Essential for Growth and Pathogenicity in Tracheal Organ Cultures

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