scholarly journals The sialate-4-O-acetylesterases of coronaviruses related to mouse hepatitis virus: a proposal to reorganize group 2 Coronaviridae

2002 ◽  
Vol 83 (2) ◽  
pp. 395-402 ◽  
Author(s):  
Walter Juergen Wurzer ◽  
Karola Obojes ◽  
Reinhard Vlasak
Keyword(s):  
Hepatitis Virus ◽  
Horse Serum ◽  
Specific Interaction ◽  
Mouse Hepatitis Virus ◽  
Alkaline Treatment ◽  
Structural Protein ◽  
Gene Encoding ◽  
Acetylneuraminic Acid ◽  
Group 2 ◽  
Phylogenetic Lineages

Group 2 coronaviruses are characterized within the order Nidovirales by a unique genome organization. A characteristic feature of group 2 coronaviruses is the presence of a gene encoding the haemagglutinin–esterase (HE) protein, which is absent in coronaviruses of groups 1 and 3. At least three coronavirus strains within group 2 expressed a structural protein with sialate-4-O-acetylesterase activity, distinguishing them from other members of group 2, which encode an enzyme specific for 5-N-acetyl-9-O-acetylneuraminic acid. The esterases of mouse hepatitis virus (MHV) strains S and JHM and puffinosis virus (PV) specifically hydrolysed 5-N-acetyl-4-O-acetylneuraminic acid (Neu4,5Ac2) as well as the synthetic substrates p-nitrophenyl acetate, 4-methylumbelliferyl acetate and fluorescein diacetate. The K m values of the MHV-like esterases for the latter substrates were two- to tenfold lower than those of the sialate-9-O-acetylesterases of influenza C viruses. Another unspecific esterase substrate, α-naphthyl acetate, was used for the in situ detection of the dimeric HE proteins in SDS–polyacrylamide gels. MHV-S, MHV-JHM and PV bound to horse serum glycoproteins containing Neu4,5Ac2. De-O-acetylation of the glycoproteins by alkaline treatment or incubation with the viral esterases resulted in a complete loss of recognition, indicating a specific interaction of MHV-like coronaviruses with Neu4,5Ac2. Combined with evidence for distinct phylogenetic lineages of group 2 coronaviruses, subdivision into subgroups 2a (MHV-like viruses) and 2b (bovine coronavirus-like viruses) is suggested.

scholarly journals In vitro macrophage manifestation of cortisone-induced decrease in resistance to mouse hepatitis virus.

1981 ◽  
Vol 153 (3) ◽  
pp. 732-737 ◽  
Author(s):  
C E Taylor ◽  
W Y Weiser ◽  
F B Bang
Keyword(s):  
Concanavalin A ◽  
Hepatitis Virus ◽  
Horse Serum ◽  
Mouse Hepatitis Virus ◽  
Treated Animal ◽  
Supernatant Fluid ◽  
Spleen Cells ◽  
In Vitro Susceptibility

Genetically resistant G3H mice routinely yielded macrophages that were resistant when grown in 90% horse serum. These mice also routinely yielded macrophages that were susceptible to the same virus, MHV (PRI), in vitro after the mice had been treated with three intraperitoneal doses, of hydrocortisone. Dexamethasone and prednisolone when similarly administered also increased the susceptibility of C3H macrophages taken from the treated animal, but progesterone and testosterone did not. In addition, spleen cells from mice treated with cortisone made the resistant C3H macrophages 100 times more susceptible in vitro. Increased in vitro susceptibility induced in this way by hydrocortisone was reversed by exposure to supernatant fluid removed from cultures of concanavalin A-treated spleen cells.

scholarly journals Genetic Evidence for a Structural Interaction between the Carboxy Termini of the Membrane and Nucleocapsid Proteins of Mouse Hepatitis Virus

2002 ◽  
Vol 76 (10) ◽  
pp. 4987-4999 ◽  
Author(s):  
Lili Kuo ◽  
Paul S. Masters
Keyword(s):  
Hepatitis Virus ◽  
Expression System ◽  
Mouse Hepatitis Virus ◽  
Viral Envelope ◽  
Genetic Evidence ◽  
M Protein ◽  
Structural Protein ◽  
Virion Protein ◽  
Structural Interaction ◽  
Intact Virion

ABSTRACT The coronavirus membrane (M) protein is the most abundant virion protein and the key component in viral assembly and morphogenesis. The M protein of mouse hepatitis virus (MHV) is an integral membrane protein with a short ectodomain, three transmembrane segments, and a large carboxy-terminal endodomain facing the interior of the viral envelope. The carboxy terminus of MHV M has previously been shown to be extremely sensitive to mutation, both in a virus-like particle expression system and in the intact virion. We have constructed a mutant, MΔ2, containing a two-amino-acid truncation of the M protein that was previously thought to be lethal. This mutant was isolated by means of targeted RNA recombination with a powerful host range-based selection allowed by the interspecies chimeric virus fMHV (MHV containing the ectodomain of the feline infectious peritonitis virus S protein). Analysis of multiple second-site revertants of the MΔ2 mutant has revealed changes in regions of both the M protein and the nucleocapsid (N) protein that can compensate for the loss of the last two residues of the M protein. Our data thus provide the first genetic evidence for a structural interaction between the carboxy termini of the M and N proteins of MHV. In addition, this work demonstrates the efficacy of targeted recombination with fMHV for the systematic genetic analysis of coronavirus structural protein interactions.

scholarly journals The 3′ cis-Acting Genomic Replication Element of the Severe Acute Respiratory Syndrome Coronavirus Can Function in the Murine Coronavirus Genome

2004 ◽  
Vol 78 (14) ◽  
pp. 7846-7851 ◽  
Author(s):  
Scott J. Goebel ◽  
Jill Taylor ◽  
Paul S. Masters
Keyword(s):  
Severe Acute Respiratory Syndrome ◽  
Untranslated Region ◽  
Hepatitis Virus ◽  
Mouse Hepatitis Virus ◽  
Cis Acting ◽  
Group 3 ◽  
Group 2 ◽  
Group 1 ◽  
Murine Coronavirus

ABSTRACT The 3′ untranslated region (3′ UTR) of the genome of the severe acute respiratory syndrome coronavirus can functionally replace its counterpart in the prototype group 2 coronavirus mouse hepatitis virus (MHV). By contrast, the 3′ UTRs of representative group 1 or group 3 coronaviruses cannot operate as substitutes for the MHV 3′ UTR.

scholarly journals The Hemagglutinin-Esterase of Mouse Hepatitis Virus Strain S Is a Sialate-4-O-Acetylesterase

1999 ◽  
Vol 73 (6) ◽  
pp. 4721-4727 ◽  
Author(s):  
Gerhard Regl ◽  
Alexandra Kaser ◽  
Matthias Iwersen ◽  
Hiltrud Schmid ◽  
Guido Kohla ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Guinea Pig ◽  
Virus Strain ◽  
Hepatitis Virus ◽  
Horse Serum ◽  
Mouse Hepatitis Virus ◽  
High Specificity ◽  
Recombinant Vaccinia Virus ◽  
Influenza C Virus ◽  
Pig Serum

By comparative analysis of the hemagglutinin-esterase (HE) protein of mouse hepatitis virus strain S (MHV-S) and the HE protein of influenza C virus, we found major differences in substrate specificities. In striking contrast to the influenza C virus enzyme, the MHV-S esterase was unable to release acetate from bovine submandibulary gland mucin. Furthermore, MHV-S could not remove influenza C virus receptors from erythrocytes. Analysis with free sialic acid derivatives revealed that the MHV-S HE protein specifically de-O-acetylates 5-N-acetyl-4-O-acetyl sialic acid (Neu4,5Ac2) but not 5-N-acetyl-9-O-acetyl sialic acid (Neu5,9Ac2), which is the major substrate for esterases of influenza C virus and bovine coronaviruses. In addition, the MHV-S esterase converted glycosidically bound Neu4,5Ac2 of guinea pig serum glycoproteins to Neu5Ac. By expression of the MHV esterase with recombinant vaccinia virus and incubation with guinea pig serum, we demonstrated that the viral HE possesses sialate-4-O-acetylesterase activity. In addition to observed enzymatic activity, MHV-S exhibited affinity to guinea pig and horse serum glycoproteins. Binding required sialate-4-O-acetyl groups and was abolished by chemical de-O-acetylation. Since Neu4,5Ac2 has not been identified in mice, the nature of potential substrates and/or secondary receptors for MHV-S in the natural host remains to be determined. The esterase of MHV-S is the first example of a viral enzyme with high specificity and affinity toward 4-O-acetylated sialic acids.

scholarly journals The non-structural protein Nsp10 of mouse hepatitis virus binds zinc ions and nucleic acids

FEBS Letters ◽  
2006 ◽  
Vol 580 (17) ◽  
pp. 4143-4149 ◽  
Author(s):  
Nele Matthes ◽  
Jeroen R. Mesters ◽  
Bruno Coutard ◽  
Bruno Canard ◽  
Eric J. Snijder ◽  
...  
Keyword(s):  
Nucleic Acids ◽  
Hepatitis Virus ◽  
Mouse Hepatitis Virus ◽  
Zinc Ions ◽  
Structural Protein

scholarly journals Crystal Structure of the C-Terminal Cytoplasmic Domain of Non-Structural Protein 4 from Mouse Hepatitis Virus A59

PLoS ONE ◽  
2009 ◽  
Vol 4 (7) ◽  
pp. e6217 ◽  
Author(s):  
Xiaoling Xu ◽  
Zhiyong Lou ◽  
Yanlin Ma ◽  
Xuehui Chen ◽  
Zhangsheng Yang ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Hepatitis Virus ◽  
Mouse Hepatitis Virus ◽  
Cytoplasmic Domain ◽  
Structural Protein

scholarly journals One proline deletion in the fusion peptide of neurotropic mouse hepatitis virus (MHV) restricts retrograde axonal transport and neurodegeneration

2020 ◽  
Vol 295 (20) ◽  
pp. 6926-6935 ◽  
Author(s):  
Saurav Saswat Rout ◽  
Manmeet Singh ◽  
Kenneth S. Shindler ◽  
Jayasri Das Sarma
Keyword(s):  
Optic Nerve ◽  
Optic Neuritis ◽  
Axonal Transport ◽  
Hepatitis Virus ◽  
Mouse Hepatitis Virus ◽  
Retrograde Axonal Transport ◽  
Spike Protein ◽  
Fusion Peptides ◽  
Gene Encoding ◽  
The Central Nervous System

Mouse hepatitis virus (MHV; murine coronavirus) causes meningoencephalitis, myelitis, and optic neuritis followed by axonal loss and demyelination. This murine virus is used as a common model to study acute and chronic virus-induced demyelination in the central nervous system. Studies with recombinant MHV strains that differ in the gene encoding the spike protein have demonstrated that the spike has a role in MHV pathogenesis and retrograde axonal transport. Fusion peptides (FPs) in the spike protein play a key role in MHV pathogenesis. In a previous study of the effect of deleting a single proline residue in the FP of a demyelinating MHV strain, we found that two central, consecutive prolines are important for cell–cell fusion and pathogenesis. The dihedral fluctuation of the FP was shown to be repressed whenever two consecutive prolines were present, in contrast to the presence of a single proline in the chain. Using this proline-deleted MHV strain, here we investigated whether intracranial injection of this strain can induce optic neuritis by retrograde axonal transport from the brain to the retina through the optic nerve. We observed that the proline-deleted recombinant MHV strain is restricted to the optic nerve, is unable to translocate to the retina, and causes only minimal demyelination and no neuronal death. We conclude that an intact proline dyad in the FP of the recombinant demyelinating MHV strain plays a crucial role in translocation of the virus through axons and subsequent neurodegeneration.

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