scholarly journals CYTOPATHOGENICITY OF INFLUENZA VIRUS (H4 N3)

2021 ◽  
Vol 25 (1) ◽  
pp. 181-193
Author(s):  
H. M. I. AL-HYALI
Keyword(s):  
Influenza Virus ◽  
Virus Isolate ◽  
Chicken Embryo Fibroblast ◽  
Post Inoculation ◽  
Tissue Cultures ◽  
Cytoplasmic Change ◽  
Infected Cells ◽  
Indirect Immunoperoxidase ◽  
Eosinophilic Inclusions ◽  
Cytopathogenic Effect

Monolayer tissue cultures of chicken embryo fibroblast ( CEF ) cells infected with avian influenza virus isolate were examined by the hematoxylie and eosin (H&E) staining and indirect immunoperoxidase test for studying the cytopathogenic effect of the virus. Cytopathological changes which occurred in the uncleus of infected cells included nuclear and nucleolar hypertropy, chromatin margination and intranuclear inclusions. The most striking cytoplasmic change were the presence of perinuclear. eosinophilic inclusions at 22-36 hours post inoculation ( p. i.). Vacuolization, and granulation were also observed. Indirect immunoperoxidase ( IP ) test demonstrated the localization of influenza virus antigens in infected cells. A positive peroxidase reaction observed in the nucleus and cytoplasm were similar to those shown hematoxyline and eosin staining.

scholarly journals Cytopathogenicity studied of fowl pox virus by using indirect immunoperoxidase and acridine orange tests .

2005 ◽  
Vol 29 (2) ◽  
pp. 12-20
Author(s):  
Harith M. AL-Hyali
Keyword(s):  
Acridine Orange ◽  
Brilliant Green ◽  
Post Inoculation ◽  
Acridine Orange Staining ◽  
Virus Assay ◽  
Intracytoplasmic Inclusions ◽  
Infected Cells ◽  
Indirect Immunoperoxidase ◽  
Chicken Eggs ◽  
Embryonated Chicken

Locally isolated fowl pox virus was inoculated on chorioallantoic membraneof chick embryos, leads to the appearances of odema and pocks lesion on themembrane , 120 hours post inoculation .Virus assay showed that the infectivitytiter were 106.8 to 107.5 EID50/0.1 ml in embryonated chicken eggs. Monolayertissue cultures of chick embryo fibroblast cells infected with fowl pox virus wereexamined by acridine orange staining and indirect immunoperoxidase test to studythe cytopathogenic effects of the virus . The most striking cytoplasmic changesobserved was the presence of the intracytoplasmic inclusions at 24-48 hours postinoculation, numerous inclusions were clearly seen at 72 hr. P.I.in addition tocytoplasmic vaculation and granulation were clearly seen at 96 hr. P.I. Thesechanges stained brilliant green with acridine orange and dark brown staining withimmunoperoxidase . Both tests demonstrated the localization of pox virus antigensin infected cells at same intervals.

Electron Microscopy of a Herpesvirus Isolated from Marek's Disease in Duck and Chicken Embryo Fibroblast Cultures

1968 ◽  
Vol 26 ◽  
pp. 222-223 ◽  
Author(s):  
Keyvan Nazerian
Keyword(s):  
Inclusion Bodies ◽  
Chicken Embryo Fibroblast ◽  
Marek's Disease ◽  
Marek’S Disease ◽  
Duck Embryo Fibroblast ◽  
Multinucleated Cells ◽  
Viral Particles ◽  
Infected Cells ◽  
And Control ◽  
Do So

A herpes-like virus has been isolated from duck embryo fibroblast (DEF) cultures inoculated with blood from Marek's disease (MD) infected birds. Cultures which contained this virus produced MD in susceptible chickens while virus negative cultures and control cultures failed to do so. This and other circumstantial evidence including similarities in properties of the virus and the MD agent implicate this virus in the etiology of MD.Histochemical studies demonstrated the presence of DNA-staining intranuclear inclusion bodies in polykarocytes in infected cultures. Distinct nucleo-plasmic aggregates were also seen in sections of similar multinucleated cells examined with the electron microscope. These aggregates are probably the same as the inclusion bodies seen with the light microscope. Naked viral particles were observed in the nucleus of infected cells within or on the edges of the nucleoplasmic aggregates. These particles measured 95-100mμ, in diameter and rarely escaped into the cytoplasm or nuclear vesicles by budding through the nuclear membrane (Fig. 1). The enveloped particles (Fig. 2) formed in this manner measured 150-170mμ in diameter and always had a densely stained nucleoid. The virus in supernatant fluids consisted of naked capsids with 162 hollow, cylindrical capsomeres (Fig. 3). Enveloped particles were not seen in such preparations.

Studies of a Defective Measles Virus

1968 ◽  
Vol 26 ◽  
pp. 208-209
Author(s):  
R. M. McCombs ◽  
M. Benyesh-Melnick ◽  
J. P. Brunschwig
Keyword(s):  
Inclusion Bodies ◽  
Measles Virus ◽  
Giant Cells ◽  
Helical Structures ◽  
Thin Sections ◽  
Virus Particles ◽  
Extracellular Virus ◽  
Culture Cells ◽  
Infected Cells ◽  
Eosinophilic Inclusions

Measles virus is an agent that is capable of replicating in a number of different culture cells and generally causes the formation of multinucleated giant cells. As a result of infection, virus is released from the cells into the culture fluids and reinfection can be initiated by this cell-free virus. The extracellular virus has been examined by negative staining with phosphotungstic acid and has been shown to be a rather pleomorphic particle with a diameter of about 140 mμ. However, no such virus particles have been detected in thin sections of the infected cells. Rather, the only virus-induced structures present in the giant cells are eosinophilic inclusions (intracytoplasmic or intranuclear). These inclusion bodies have been shown to contain helical structures, resembling the nucleocapsid observed in negatively stained preparations.

scholarly journals Neutrophils do not bind to or phagocytize human immune complexes formed with influenza virus

Blood ◽  
1993 ◽  
Vol 82 (5) ◽  
pp. 1639-1646 ◽  
Author(s):  
DR Ratcliffe ◽  
J Michl ◽  
EB Cramer
Keyword(s):  
Influenza Virus ◽  
Sialic Acid ◽  
Epithelial Cells ◽  
Binding Site ◽  
Immune Complexes ◽  
Human Neutrophils ◽  
Sialic Acid Binding ◽  
Infected Cells ◽  
Neutrophil Adherence ◽  
Human Immune

Abstract Neutrophils appear to form the first line of defense against influenza virus, yet it is unclear how these leukocytes recognize influenza- infected cells. While demonstrating that neutrophils adhere specifically to the sialic acid-binding site on the hemagglutinin molecule (HA) on the surface of influenza-infected (WSN[H1N1]) epithelial cells and not to other viral or epithelial cell antigens, it was observed that human neutrophils do not recognize immune complexes formed with influenza virus. Intact antibodies (mouse monoclonal antibodies [MoAbs] IgG1 and IgG2b, human immune heat-inactivated serum [predominantly IgG1], and IgG purified from human immune serum) that block the sialic acid-binding site on HA significantly reduced (> 80%) neutrophil adherence to influenza-infected epithelial cells. Binding and phagocytosis of free influenza virions and neutrophil agglutination by influenza virus were completely prevented by these antibodies. Intact and F(ab')2 fragments of mouse MoAbs to other viral epitopes caused increased neutrophil adherence to infected cells. This binding was eliminated by F(ab'2) fragments of MoAbs against the sialic acid- binding site on HA, but not by saturating amounts of MoAbs, which block the neutrophil Fc receptors. Thus, it appears that human neutrophils show little ability to bind via their Fc receptors to the immune complexes formed with antibody and either influenza-infected epithelial cells or the free virion. These findings are in contrast to the general dogma, and are the first example of antibody opsonization reducing, rather than enhancing, neutrophil binding and phagocytosis of a pathogen.

scholarly journals Infection of HLA-DR1 Transgenic Mice with a Human Isolate of Influenza A Virus (H1N1) Primes a Diverse CD4 T-Cell Repertoire That Includes CD4 T Cells with Heterosubtypic Cross-Reactivity to Avian (H5N1) Influenza Virus

2009 ◽  
Vol 83 (13) ◽  
pp. 6566-6577 ◽  
Author(s):  
Katherine A. Richards ◽  
Francisco A. Chaves ◽  
Andrea J. Sant
Keyword(s):  
T Cells ◽  
Influenza Virus ◽  
T Cell ◽  
Avian Influenza ◽  
Avian Influenza Virus ◽  
Cd4 T Cells ◽  
Cross Reactivity ◽  
Cd4 T Cell ◽  
Ns1 Protein ◽  
Infected Cells

ABSTRACT The specificity of the CD4 T-cell immune response to influenza virus is influenced by the genetic complexity of the virus and periodic encounters with variant subtypes and strains. In order to understand what controls CD4 T-cell reactivity to influenza virus proteins and how the influenza virus-specific memory compartment is shaped over time, it is first necessary to understand the diversity of the primary CD4 T-cell response. In the study reported here, we have used an unbiased approach to evaluate the peptide specificity of CD4 T cells elicited after live influenza virus infection. We have focused on four viral proteins that have distinct intracellular distributions in infected cells, hemagglutinin (HA), neuraminidase (NA), nucleoprotein, and the NS1 protein, which is expressed in infected cells but excluded from virion particles. Our studies revealed an extensive diversity of influenza virus-specific CD4 T cells that includes T cells for each viral protein and for the unexpected immunogenicity of the NS1 protein. Due to the recent concern about pandemic avian influenza virus and because CD4 T cells specific for HA and NA may be particularly useful for promoting the production of neutralizing antibody to influenza virus, we have also evaluated the ability of HA- and NA-specific CD4 T cells elicited by a circulating H1N1 strain to cross-react with related sequences found in an avian H5N1 virus and find substantial cross-reactivity, suggesting that seasonal vaccines may help promote protection against avian influenza virus.

scholarly journals Effect of the preparation Ingavirin® (imidazolyl ethanamide pentandioic acid) on the interferon status of cells under conditions of viral infection

2016 ◽  
Vol 21 (4) ◽  
pp. 196-205
Author(s):  
Thomas Aschacher ◽  
Artem Krokhin ◽  
Irina Kuznetsova ◽  
Johannes Langle ◽  
Vladimir Nebolsin ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Viral Infection ◽  
Viral Infections ◽  
Antiviral Drug ◽  
Effector Proteins ◽  
Theoretical Ground ◽  
Ns1 Protein ◽  
Interferon Inducer ◽  
Infected Cells ◽  
Interferon System

Ingavirin® (imidazolyl ethanamide pentandioic acid) is an original antiviral drug, which is used in Russia for treatment and profilaxis of influenza and other acute viral infections. We confirmed that imidazolyl ethanamide pentandioic acid (IEPA), not being interferon inducer itself, enhances synthesis of both interferon-a/fi receptors (IFNAR) to interferone and cell sensitivity to interferone signalling, which was suppressed by NS1 protein - pathogen factor of influenza virus. IEPA is able to promote antiviral effector proteins PKR and MxA in infected cells, in opposition to interferon system suppression by influenza virus. Theoretical ground of clinical efficacy of Ingavirine® could be confirmed by obtained data of influence to innate immune system during viral infection.

scholarly journals Modulation of Nuclear Localization of the Influenza Virus Nucleoprotein through Interaction with Actin Filaments

1999 ◽  
Vol 73 (3) ◽  
pp. 2222-2231 ◽  
Author(s):  
Paul Digard ◽  
Debra Elton ◽  
Konrad Bishop ◽  
Elizabeth Medcalf ◽  
Alan Weeds ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Nuclear Localization ◽  
Virus Genome ◽  
Actin Binding ◽  
Filamentous Actin ◽  
Nuclear Localization Signals ◽  
Infected Cells ◽  
Cytoplasmic Accumulation ◽  
High Level

ABSTRACT The influenza virus genome is transcribed in the nuclei of infected cells but assembled into progeny virions in the cytoplasm. This is reflected in the cellular distribution of the virus nucleoprotein (NP), a protein which encapsidates genomic RNA to form ribonucleoprotein structures. At early times postinfection NP is found in the nucleus, but at later times it is found predominantly in the cytoplasm. NP contains several sequences proposed to act as nuclear localization signals (NLSs), and it is not clear how these are overridden to allow cytoplasmic accumulation of the protein. We find that NP binds tightly to filamentous actin in vitro and have identified a cluster of residues in NP essential for the interaction. Complexes containing RNA, NP, and actin could be formed, suggesting that viral ribonucleoproteins also bind actin. In cells, exogenously expressed NP when expressed at a high level partitioned to the cytoplasm, where it associated with F-actin stress fibers. In contrast, mutants unable to bind F-actin efficiently were imported into the nucleus even under conditions of high-level expression. Similarly, nuclear import of NLS-deficient NP molecules was restored by concomitant disruption of F-actin binding. We propose that the interaction of NP with F-actin causes the cytoplasmic retention of influenza virus ribonucleoproteins.

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