Partial genome analysis of murine gammaherpesvirus 4556

Kúdelová, M; Halásová, Zuzana; Belvončíková, Petra; Pančík, P; Režuchová, Ingeborg; M, Valovičová

doi:10.4149/av_2012_03_177

Cited by 7 publications

(8 citation statements)

References 25 publications

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“…Two murine gammaherpesviruses (MHV-68 and MHV-72) originally isolated from the bank vole, Myodes glareolus (Blaškovič et al, 1980), kindly provided by Prof. Mistríková (Faculty of Natural Sciences, Comenius University, Bratislava, Slovakia) were plaque purifi ed twice to obtain clones f2.6 (MHV-68) and h3.7 (MHV-72) (Kúdelová et al, 2012). Viral DNA was isolated and purifi ed from virions as previously described .…”

Section: Methodsmentioning

confidence: 99%

“…Among these is the Wood mouse herpesvirus isolated from wood mouse in the UK, the full genome sequence of which was recently identifi ed by Hughes et al (2010). Biological properties of some other murine herpesviruses (MHV-60, MHV-78, MHV-76, MHV-Šumava, MHV-4556) isolated from bank vole and wood mice in Slovakia and Bohemia (Blaškovič et al, 1980;Kožuch et al, 1993;Blaškovičová et al, 2007;Halásová et al, 2011;Kúdelová et al, 2012) are also studied (reviewed by Wagnerová et al, 2015).…”

Section: Introductionmentioning

confidence: 99%

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Soluble M3 proteins of murine gammaherpesviruses 68 and 72 expressed in Escherichia coli: analysis of chemokine-binding properties

Matuskova¹,

Pančík²,

Štibrániová³

et al. 2015

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Summary. -M3 protein of murine gammaherpesvirus 68 (MHV-68) was identifi ed as a viral chemokinebinding protein 3 (vCKBP-3) capable to bind a broad spectrum of chemokines and their receptors. During both acute and latent infection MHV-68 M3 protein provides a selective advantage for the virus by inhibiting the antiviral and infl ammatory response. A unique mutation Asp307Gly was identifi ed in the M3 protein of murine gammaherpesvirus 72 (MHV-72), localized near chemokine-binding domain. Study on chemokine-binding properties of MHV-72 M3 protein purifi ed from medium of infected cells implied reduced binding to some chemokines when compared to MHV-68 M3 protein. It was suggested that the mutation in the M3 protein might be involved in the attenuation of immune response to infection with MHV-72. Recently, Escherichia coli cells were used to prepare native recombinant M3 proteins of murine gammaherpesviruses 68 and 72 (Pančík et al., 2013). In this study, we assessed the chemokine-binding properties of three M3 proteins prepared in E. coli Rosetta-gami 2 (DE3) cells, the full length M3 protein of both MHV-68 and MHV-72 and MHV-68 M3 protein truncated in the signal sequence (the fi rst 24 aa). Th ey all displayed binding activity to human chemokines CCL5 (RANTES), CXCL8 (IL-8), and CCL3 (MIP-1α). Th e truncated MHV-68 M3 protein had more than twenty times reduced binding activity to CCL5, but only about fi ve and three times reduced binding to CXCL8 and CCL3 when compared to its full length counterpart. Binding of the full length MHV-72 M3 protein to all chemokines was reduced when compared to MHV-68 M3 protein. Its binding to CCL5 and CCL3 was reduced over ten and seven times. However, its binding to CXCL8 was only slightly reduced (64.8 vs 91.8%). Th ese data implied the signifi cance of the signal sequence and also of a single mutation (at aa 307) for effi cient M3 protein binding to some chemokines.

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Soluble M3 proteins of murine gammaherpesviruses 68 and 72 expressed in Escherichia coli: analysis of chemokine-binding properties

Matuskova¹,

Pančík²,

Štibrániová³

et al. 2015

Self Cite

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“…Although we have an recent update about the type and its role in a large number of physiological processes, such as the function of heart and smooth muscles, glandular secretion, release of neurotransmitters, gene expression and cognitive functions as learning and memory [7] . However, contraction of the guinea-pig isolated gallbladder mediating muscarinic receptor which belongs to the M 3 or M 4 subtype and which was characterized by subtype agonists and antagonists [8] .…”

Section: Muscarinic Receptorsmentioning

confidence: 99%

Basic and modern concepts on cholinergic receptor: A review

Tiwari¹,

Dwivedi²,

Singh³

et al. 2013

Asian Pacific Journal of Tropical Disease

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“…The twice-plaque purified clone f2.6 of MHV-68, obtained from an isolate of the bank vole Myodes glareolus, was used to prepare pure virion DNA as previously described [12,15,42]. The Spodoptera frugiperda 9 (Sf9) insect ovary cell line (ATCC® CRL-1711) was maintained as an adherent culture in Sf-900 TM II SFM media (Gibco) supplemented with 2.5-10% (v/v) fetal bovine serum (FBS, SigmaAldrich) and 50 µg/ml of gentamicin (Sandoz) at 27.5°C.…”

Section: Virus and Cellsmentioning

confidence: 99%

“…captured in Slovakia and Bohemia [13]. From these, the murine herpesviruses MHV-72 and MHV-4556 have been the most deeply studied with regards to their pathogenesis and molecular properties [14,15].…”

Section: Introductionmentioning

confidence: 99%

A Deletion of Signal Peptide in Recombinant Murine Gamma-herpesvirus 68 M3 Protein Enhances its Binding Affinity to CCL5 Chemokine and Increases its Yield from Insect Cells

Šebová¹,

Lenhartová²,

Štibrániová³

et al. 2017

J Infect Dis Ther

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Objective: The M3 protein encoded by murine gamma-herpesvirus 68 (MHV-68) was the first secreted protein identified in herpesvirus. This protein is unique in its ability to bind a broad-spectrum of chemokines from all four subfamilies, thus it has been proposed to be a potential gene therapy candidate for controlling the overactive inflammatory responses of some human inflammatory diseases. Methods:We prepared MHV-68 M3del protein with a deletion of its signal peptide (M3del) and full-length MHV-68 M3 protein (M3) using a baculovirus-mediated insect cell expression system and confirmed their specificity by Western blot using newly prepared mouse monoclonal anti-M3 antibody 1/27. Binding affinity of both proteins to human CCL5 and CXCL8 chemokine was examined by ELISA.Results: M3del and M3 displayed affinity to both chemokines tested. M3 del concentration sufficient to bind 25% of CCL5 was two times smaller than that of M3 (IC25=3.5 nmol/l vs. 6.1 nmol/l). In contrary, the values of IC25 for CXCL8 for M3del and M3 were comparable (IC25=13.8 nmol/l vs. 13.3 nmol/l. We have found that the absence of signal peptide strongly affects the yield of recombinant M3 protein. The yields of M3del and M3 were in an unbalanced ratio of 67 to 1. Conclusions:The results suggest that the absence of signal peptide in recombinant MHV-68 M3 protein allows increased binding activity of the protein to CCL5 but not to CXCL8, and even a very large increase in its yield from insect cells.

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Partial genome analysis of murine gammaherpesvirus 4556

Cited by 7 publications

References 25 publications

Soluble M3 proteins of murine gammaherpesviruses 68 and 72 expressed in Escherichia coli: analysis of chemokine-binding properties

Soluble M3 proteins of murine gammaherpesviruses 68 and 72 expressed in Escherichia coli: analysis of chemokine-binding properties

Basic and modern concepts on cholinergic receptor: A review

A Deletion of Signal Peptide in Recombinant Murine Gamma-herpesvirus 68 M3 Protein Enhances its Binding Affinity to CCL5 Chemokine and Increases its Yield from Insect Cells

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