scholarly journals Junctional Adhesion Molecule 1 Is a Functional Receptor for Feline Calicivirus

2006 ◽  
Vol 80 (9) ◽  
pp. 4482-4490 ◽  
Author(s):  
Akiko Makino ◽  
Masayuki Shimojima ◽  
Takayuki Miyazawa ◽  
Kentaro Kato ◽  
Yukinobu Tohya ◽  
...  
Keyword(s):  
Adhesion Molecule ◽  
Vero Cells ◽  
Prototype Strain ◽  
Feline Calicivirus ◽  
Progeny Production ◽  
Culture Cells ◽  
Tissue Culture Cells ◽  
The Family ◽  
Infected Cells ◽  
Functional Receptor

ABSTRACT The life cycle of calicivirus is not fully understood because most of the viruses cannot be propagated in tissue culture cells. We studied the mechanism of calicivirus entry into cells using feline calicivirus (FCV), a cultivable calicivirus. From the cDNA library of Crandell-Rees feline kidney (CRFK) cells, feline junctional adhesion molecule 1 (JAM-1), an immunoglobulin-like protein present in tight junctions, was identified as a cellular-binding molecule of the FCV F4 strain, a prototype strain in Japan. Feline JAM-1 expression in nonpermissive hamster lung cells led to binding and infection by F4 and all other strains tested. An anti-feline JAM-1 antibody reduced the binding of FCV to permissive CRFK cells and strongly suppressed the cytopathic effect (CPE) and FCV progeny production in infected cells. Some strains of FCV, such as F4 and F25, have the ability to replicate in Vero cells. We found that regardless of replication ability, FCV bound to Vero and 293T cells via simian and human JAM-1, respectively. In Vero cells, an anti-human JAM-1 antibody inhibited binding, CPE, and progeny production by F4 and F25. In addition, feline JAM-1 expression permitted FCV infection in 293T cells. Taken together, our results demonstrate that feline JAM-1 is a functional receptor for FCV, simian JAM-1 also functions as a receptor for some strains of FCV, and the interaction between FCV and JAM-1 molecules may be a determinant of viral tropism. This is the first report concerning a functional receptor for the viruses in the family Caliciviridae.

scholarly journals α2,6-Linked sialic acid acts as a receptor for Feline calicivirus

2007 ◽  
Vol 88 (1) ◽  
pp. 177-186 ◽  
Author(s):  
Amanda D. Stuart ◽  
T. David K. Brown
Keyword(s):  
Sialic Acid ◽  
Adhesion Molecule ◽  
Sodium Periodate ◽  
Metabolic Inhibitors ◽  
Feline Calicivirus ◽  
Sambucus Nigra ◽  
Virus Binding ◽  
Maackia Amurensis ◽  
The Family

Feline calicivirus (FCV) is a major causative agent of respiratory disease in cats. It is also one of the few cultivatable members of the family Caliciviridae. It has recently been reported that FCV binding is in part due to interaction with junction adhesion molecule-A. This report describes the characterization of additional receptor components for FCV. Chemical treatment of cells with sodium periodate showed that FCV recognized carbohydrate moieties on the surface of permissive cells. Enzymic treatment with Vibrio cholerae neuraminidase demonstrated that sialic acid was a major determinant of virus binding. Further characterization using linkage-specific lectins from Maackia amurensis and Sambucus nigra revealed that FCV recognized sialic acid with an α2,6 linkage. Using various proteases and metabolic inhibitors, it was shown that α2,6-linked sialic acid recognized by FCV is present on an N-linked glycoprotein.

scholarly journals The L Gene of J Paramyxovirus Plays a Critical Role in Viral Pathogenesis

2013 ◽  
Vol 87 (23) ◽  
pp. 12990-12998 ◽  
Author(s):  
Zhuo Li ◽  
Jie Xu ◽  
Zhenhai Chen ◽  
Xiudan Gao ◽  
Lin-Fa Wang ◽  
...  
Keyword(s):  
Nucleotide Sequence ◽  
Severe Disease ◽  
Critical Role ◽  
Vero Cells ◽  
Leader Sequence ◽  
Whole Genome Sequence ◽  
High Sequence Identity ◽  
Culture Cells ◽  
Tissue Culture Cells ◽  
Recent Sequencing

J paramyxovirus (JPV) was first isolated from moribund mice with hemorrhagic lung lesions in Australia in the 1970s. Recent sequencing of JPV (JPV-LW) confirms that JPV is a paramyxovirus with several unique features. However, neither JPV-LW nor a recombinant JPV based on its sequence (rJPV-LW) caused obvious illness in mice. In this work, we analyzed a different JPV isolate (JPV-BH), which behaved differently from JPV-LW; JPV-BH grew more slowly in Vero cells and had less of a cytopathic effect on tissue culture cells but caused severe disease in mice. We have determined the whole genome sequence of JPV-BH. There were several nucleotide sequence differences between JPV-BH and JPV-LW, one in the leader sequence, one in the GX gene, and three in the L gene. The high sequence identity between JPV-BH and JPV-LW suggests that JPV-BH and JPV-LW are the same virus strain but were obtained at different passages from different laboratories. To understand the roles of these nucleotide sequence differences in pathogenicity in mice, we generated a recombinant JPV-BH strain (rJPV-BH) and hybrid rJPV-BH strains with sequences from the leader sequence (rJPV-BH-Le-LW), the GX gene (rJPV-BH-GX-LW), and the L gene (rJPV-BH-L-LW) of JPV-LW and compared their pathogenicities in mice. We have found that rJPV-BH-L-LW was attenuated in mice, indicating that nucleotide sequence differences in the L gene play a critical role in pathogenesis.

scholarly journals The mitochondrial pathway of apoptosis is triggered during feline calicivirus infection

2006 ◽  
Vol 87 (2) ◽  
pp. 357-361 ◽  
Author(s):  
Alessandro Natoni ◽  
George E. N. Kass ◽  
Michael J. Carter ◽  
Lisa O. Roberts
Keyword(s):  
Caspase 3 ◽  
Chromatin Condensation ◽  
Mitochondrial Pathway ◽  
Feline Calicivirus ◽  
Upper Respiratory Tract ◽  
Caspase 9 ◽  
The Family ◽  
Infected Cells ◽  
Upper Respiratory ◽  
Subsequent Activation

Feline calicivirus (FCV) belongs to the family Caliciviridae and is an important pathogen of the upper respiratory tract of cats. Recent studies have shown that cells infected with FCV undergo apoptosis, as evidenced by caspase activation, chromatin condensation and cleavage of poly(ADP-ribose) polymerase. Here, the upstream events were investigated in order to define the molecular mechanism of apoptosis in FCV-infected cells. It was shown that FCV induced translocation of phosphatidylserine to the cell outer membrane and release of cytochrome c from mitochondria at about 6–8 h post-infection. These events were preceded by the loss of mitochondrial membrane potential and Bax translocation from the cytosol to mitochondria between 4 and 6 h after infection. Release of cytochrome c from mitochondria triggered the activation of caspase-9 and the subsequent activation of the executioner caspase, caspase-3. These results suggest that the mitochondrial pathway of apoptosis is triggered during FCV infection.

scholarly journals A New Model of SARS-CoV-2 Infection Based on (Hydroxy)Chloroquine Activity

2020 ◽  
Author(s):  
Robert J. Sheaff
Keyword(s):  
Oxidative Phosphorylation ◽  
Host Cell ◽  
Disease Progression ◽  
Therapeutic Benefit ◽  
Beta Oxidation ◽  
New Model ◽  
Culture Cells ◽  
Tissue Culture Cells ◽  
Obesity And Diabetes ◽  
Infected Cells

Chloroquine and hydroxychloroquine [(H)CQ] are well known anti-malarial drugs, while their use against COVID-19 is more controversial. (H)CQ activity was examined in tissue culture cells to determine if their anti-viral benefits or adverse effects might be due to altering host cell pathways. Metabolic analysis revealed (H)CQ inhibit oxidative phosphorylation in mitochondria, likely by sequestering protons needed to drive ATP synthase. This activity could cause cardiotoxicity because heart muscle relies on beta oxidation of fatty acids. However, it might also explain their therapeutic benefit against COVID-19. A new model of SARS-CoV-2 infection postulates virus enters host cell mitochondria and uses its protons for genome release. Oxidative phosphorylation is eventually compromised, so glycolysis is upregulated to maintain ATP levels. (H)CQ could prevent viral infection and/or slow its replication by sequestering these protons. In support of this model other potential COVID-19 therapeutics also targeted mitochondria, as did tobacco smoke, which may underlie smokers protection. The mitochondria of young people are naturally more adaptable and resilient, providing a rationale for their resistance to disease progression. Conversely, obesity and diabetes could exacerbate disease severity by providing extra glucose to infected cells dependent on glycolysis. The description of (H)CQ function presented here, together with its implications for understanding SARS-CO-V2 infection, makes testable predictions about disease progression and identifies new approaches for treating COVID-19.

scholarly journals IMMUNOFLUORESCENT STUDIES OF HUMAN CELL CULTURES AND CHICK EMBRYOS INOCULATED WITH THE AMEBOID CELL-"LIPOVIRUS" COMPLEX

1966 ◽  
Vol 124 (6) ◽  
pp. 1167-1180 ◽  
Author(s):  
Chien Liu ◽  
Patricia Rodina
Keyword(s):  
Phase Contrast ◽  
Early Stage ◽  
Immunofluorescent Staining ◽  
Chick Embryos ◽  
Culture Cells ◽  
Tissue Culture Cells ◽  
Human Cell Cultures ◽  
Contrast Microscopy ◽  
Infected Cells ◽  
Ameboid Cell

Tissue culture cells of human origin (HeLa, Lich, and AV3) were inoculated with the AL complex. By immunofluorescent staining, AL complex antigen was detectable in the cytoplasm of infected cells as punctate fluorescent granules during the early stage and as homogeneous fluorescence during the late stage of infection. By combining fluorescence and phase-contrast microscopy, many infected cells with cytoplasmic AL complex antigen were shown to have a normal nuclear morphology indistinguishable from uninfected cells. Initiation of AL complex infection was interpreted as occurring by transfer of transmissible factor(s) from cell to cell by contact and mutiplication of such factor(s) therein. Chick embryos were susceptible to AL complex infection following allantoic or amniotic inoculations. Antigen and infectious AL complex were demonstrable in the liver, brain, intestines, lungs, and embryonic membranes. Further investigations on AL complex and its relation to human disease are suggested.

scholarly journals Overexpression of the Rabies Virus Glycoprotein Results in Enhancement of Apoptosis and Antiviral Immune Response

2002 ◽  
Vol 76 (7) ◽  
pp. 3374-3381 ◽  
Author(s):  
Milosz Faber ◽  
Rojjanaporn Pulmanausahakul ◽  
Suchita S. Hodawadekar ◽  
Sergei Spitsin ◽  
James P. McGettigan ◽  
...  
Keyword(s):  
Rabies Virus ◽  
Caspase 3 ◽  
Marked Decrease ◽  
Fluorescence Staining ◽  
Antiviral Immune Response ◽  
Culture Cells ◽  
Tissue Culture Cells ◽  
Glycoprotein G ◽  
Antibody Titers ◽  
Infected Cells

ABSTRACT A recombinant rabies virus (RV) carrying two identical glycoprotein (G) genes (SPBNGA-GA) was constructed and used to determine the effect of RV G overexpression on cell viability and immunity. Immunoprecipitation analysis and flow cytometry showed that tissue culture cells infected with SPBNGA-GA produced, on average, twice as much RV G as cells infected with RV carrying only a single RV G gene (SPBNGA). The overexpression of RV G in SPBNGA-GA-infected NA cells was paralleled by a significant increase in caspase 3 activity followed by a marked decrease in mitochondrial respiration, neither of which was observed in SPBNGA-infected cells. Furthermore, fluorescence staining and confocal microscopy revealed an increased extent of apoptosis and markedly reduced neurofilament and F actin in SPBNGA-GA-infected primary neuron cultures compared with neuronal cells infected with SPBNGA, supporting the concept that RV G or motifs of the RV G gene trigger the apoptosis cascade. Mice immunized with SPBNGA-GA showed substantially higher antibody titers against the RV G and against the nucleoprotein than SPBNGA-immunized mice, suggesting that the speed or extent of apoptosis directly determines the magnitude of the antibody response.

scholarly journals Array Analysis of Simian Varicella Virus Gene Transcription in Productively Infected Cells in Tissue Culture

2005 ◽  
Vol 79 (9) ◽  
pp. 5315-5325 ◽  
Author(s):  
Steven B. Deitch ◽  
Donald H. Gilden ◽  
Mary Wellish ◽  
John Smith ◽  
Randall J. Cohrs ◽  
...  
Keyword(s):  
Tissue Culture ◽  
Cdna Probe ◽  
Vero Cells ◽  
Open Reading Frames ◽  
Simian Varicella Virus ◽  
Varicella Zoster ◽  
Varicella Virus ◽  
Culture Cells ◽  
Infected Cells ◽  
Reading Frames

ABSTRACT Simian varicella virus (SVV) is a neurotropic alphaherpesvirus of monkeys that is a model for varicella pathogenesis and latency. Like human varicella-zoster virus (VZV), SVV causes chicken pox (varicella), becomes latent in ganglia along the entire neuraxis, and reactivates to produce shingles (zoster). We developed macroarrays to determine the extent of viral transcription from all 70 predicted SVV open reading frames (ORFs) in infected cells in tissue culture. Cloned fragments (200 to 400 bp) from the 5′ and 3′ ends of each ORF were PCR amplified, quantitated, spotted onto nylon membranes, and fixed by UV cross-linking. Using a cDNA probe prepared from poly(A)+ RNA extracted from SVV-infected Vero cells at the height of the cytopathic effect (3 days after infection) and chemiluminescence for detection, transcripts corresponding to all SVV ORFs were identified. The abundance of each SVV transcript was compared with that previously demonstrated for VZV in infected tissue culture cells.

Freeze-Etching of Intranuclear Adenovirus

1971 ◽  
Vol 29 ◽  
pp. 384-385
Author(s):  
Dennis T. Brown ◽  
Byron T. Burlingham
Keyword(s):  
Osmium Tetroxide ◽  
Adenovirus Type ◽  
Etching Time ◽  
Human Carcinoma ◽  
Thin Sections ◽  
Culture Cells ◽  
Tissue Culture Cells ◽  
Infected Cells ◽  
Freeze Etching

Adenoviruses are revealed by negative staining to be icosahedral in structure and composed of 252 subunits (insert Fig. 1). The vertices have a fiber-like projection which has been implicated in the adsorbtion of the virus to the host cell. Ultra thin sections of adenovirus-infected cells has revealed that virus morphogenesis occurs in the nucleus.Human carcinoma (KB) tissue culture cells were productively infected with adenovirus type 2 at a multiplicity of 10 and incubated for 40 hours at 37°C. The infected monolayers were fixed in place with 1%, gluteraldehyde buffered in Millonigs phosphate buffer. The fixed cells were suspended in 30%, glycerol and processed according to the procedure of Moor in a Balzers 360 M freeze etch unit with an etching time of 70 seconds at -100°C. A second portion of the fixed cells in glycerol was post-fixed with 1% osmium tetroxide and embeded in epon 812 for ultrathin sectioning.

scholarly journals Providence virus (family: Carmotetraviridae) replicates vRNA in association with the Golgi apparatus and secretory vesicles

2013 ◽  
Vol 94 (5) ◽  
pp. 1073-1078 ◽  
Author(s):  
James R. Short ◽  
Ritah Nakayinga ◽  
Gareth E. Hughes ◽  
Cheryl T. Walter ◽  
Rosemary A. Dorrington
Keyword(s):  
Golgi Apparatus ◽  
Helicoverpa Zea ◽  
Regulation Of Gene Expression ◽  
Secretory Vesicles ◽  
Replication Proteins ◽  
Structural Protein ◽  
Virus Family ◽  
Culture Cells ◽  
The Family ◽  
Infected Cells

Providence virus (PrV) is the sole member of the family Carmotetraviridae (formerly Tetraviridae) sharing the characteristic T = 4 capsid architecture with other tetravirus families. Despite significant structural similarities, PrV differs from other tetraviruses in terms of genome organization, non-structural protein sequence and regulation of gene expression. In addition, it is the only tetravirus that infects tissue culture cells. Previous studies showed that in persistently infected Helicoverpa zea MG8 cells, the PrV replicase associates with detergent-resistant membranes in punctate cytosolic structures, which is similar to the distribution of an alpha-like tetravirus replicase (Helicoverpa armigera stunt virus). Here, we demonstrate that the site of PrV vRNA replication coincides with the presence of PrV p40/p104 proteins in infected cells and that these replication proteins associate with the Golgi apparatus and secretory vesicles in transfected cells.

scholarly journals Identification of Regions and Residues in Feline Junctional Adhesion Molecule Required for Feline Calicivirus Binding and Infection

2007 ◽  
Vol 81 (24) ◽  
pp. 13608-13621 ◽  
Author(s):  
Robert J. Ossiboff ◽  
John S. L. Parker
Keyword(s):  
Flow Cytometry ◽  
Cell Line ◽  
Adhesion Molecule ◽  
Cytoplasmic Tail ◽  
Surface Expression ◽  
Immunoglobulin Superfamily ◽  
Feline Calicivirus ◽  
Cellular Factors ◽  
Membrane Spanning ◽  
Functional Receptor

ABSTRACT The feline junctional adhesion molecule A (fJAM-A) is a functional receptor for feline calicivirus (FCV). fJAM-A is a member of the immunoglobulin superfamily (IgSF) and consists of two Ig-like extracellular domains (D1 and D2), a membrane-spanning domain, and a short cytoplasmic tail. To identify regions of fJAM-A that interact with FCV, we purified recombinant fJAM-A ectodomain and D1 and D2 domains. We found that preincubation of FCV with the ectodomain or D1 was sufficient to inhibit FCV infection in plaque reduction assays. In enzyme-linked immunosorbent assays, FCV binding to fJAM-A ectodomain was concentration dependent and saturable; however, FCV bound D1 alone weakly and was unable to bind D2. To characterize FCV binding to surface-expressed fJAM-A, we transfected truncated and chimeric forms of fJAM-A into a nonpermissive cell line and assayed binding by flow cytometry. Only D1 was necessary for FCV binding to cells; all other domains could be replaced. Using a structure-guided mutational approach, we identified three mutants of fJAM-A within D1 (D42N, K43N, and S97A) that exhibited significantly decreased capacities to bind FCV. In contrast to our finding that D1 mediated FCV binding, we found that all domains of fJAM-A were necessary to confer susceptibility to FCV infection. Furthermore, surface expression of fJAM-A was not sufficient to permit FCV infection by all of the isolates we investigated. This indicates that (i) other cellular factors are required to permit productive FCV infection and (ii) individual FCV isolates differ in the factors they require.

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