Initial Stages in Infection with Animal Viruses

Dimmock, Nigel J.

doi:10.1099/0022-1317-59-1-1

Cited by 171 publications

(67 citation statements)

References 195 publications

(135 reference statements)

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“…Phagocytosis requires energy and is inhibited by inhibitors of microtubule and microfilament assembly (Allison & Davies, 1974;Dimmock, 1982). The demonstrations that these drugs had no effect on the yield of both forms of the virus suggest that the phagocytic process observed by Knudson & Harrap (1976) is probably not directly involved in the pathway of baculovirus infection and that this 'dead end' may be largely responsible for the high PDV particle/infectivity ratio (2 × 105 :l).…”

Section: Discussionmentioning

confidence: 99%

“…Presumably none of the virus taken up by phagocytosis proceeds to infection. If in addition to fusion, endocytosis is also involved in initiating baculovirus infection, this is likely to be micropinocytosis which does not require energy, does not rely on the integrity of microfilaments and microtubules, and usually involves the small vesicles (Allison & Davies, 1974;Dimmock, 1982) which are about the size of a baculovirus nucleocapsid or nucleocapsid singly enveloped virus particle.…”

Section: Discussionmentioning

confidence: 99%

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Baculovirus Replication: Uptake of Trichoplusia ni Nuclear Polyhedrosis Virus Particles by Insect Cells

Wang

Kelly

1985

Journal of General Virology

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SUMMARYThe uptake of two forms of Trichoplusia ni multiple nucleocapsid nuclear polyhedrosis virus by SpodopleraJrugiperda cells in culture has been evaluated. Subtle differences in the Mg 2+ and Ca 2+ requirements for the uptake of cell-released virus (CRV) and polyhedron-derived virus (PDV) exist; otherwise, both forms of the virus appeared similar in their mode of uptake. Entry occurs by fusion of the plasma membrane of the cell with the envelope surrounding the virus nucleocapsid at neutral pH. The receptor turnover for the virus probably occurs rapidly since saturation of receptor sites for the virus was not achieved. The binding and penetration of the virus, and the uncoating and transport of the viral genome to the nucleus is rapid. Uncoating occurs predominantly in the cytoplasm. The lower infectivity of PDV, compared with CRV, for cells in culture may happen because this form of the virus accumulates in cell vacuoles and is unable to proceed with infection.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Baculovirus Replication: Uptake of Trichoplusia ni Nuclear Polyhedrosis Virus Particles by Insect Cells

Wang

Kelly

1985

Journal of General Virology

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“…Recent evidence from influenza virus neutralization studies (Possee, Schild and Dimmock, 1982) suggests that neutralizing antibody to this virus induces allosteric rearrangements in the haemagglutinin molecule which are transmitted across the virus envelope to the interior of the particle. Dimmock (1982) has proposed that conformational changes in virion protein are important in many reactions with cellular components. It seems likely that crucial conformational changes in the viral antigen which interfere with viral replication may only be triggered by antibody to a few regions in the total amino acid sequence of the protein and, if tiiese segments can be synthesised, then the opportunity to make successful vaccines with oligopeptide conjugates may be greatly improved.…”

Section: The Potential Of Selected Oligopeptides As a Basis For Vaccinesmentioning

confidence: 99%

Vaccines for the Future?

1982

Aust J Exp Biol Med

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“…Dans les mécanismes moléculaires de pathogénèse, la grande majorité des associations connues apparaît basée sur la reconnaissance spécifique d'un ligand protéique par un glycoconjugué à la surface de la cellule hôte (récepteur). Le plus souvent, la partie glycosylée est impliquée dans la spécificité de l'attachement [9,30,34,75]. Dans le cas des toxines bactériennes entériques, les sites d'attachement glycosylés, dont les structures sont les mieux décrites, sont le monosialoganglioside GM1, pour les toxines CT et toxine thermolabile d'E.…”

Section: Nature Et Structure D'un Récepteurunclassified

Les récepteurs des entérotoxines bactériennes

Rousset

2000

Vet. Res.

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-Bacterial enterotoxin receptors. Enteric bacterial toxins display a great diversity in their structure, molecular weight and mechanism of action. The interaction of enterotoxins with the intestinal mucosa either leads to a direct effect on the cell membrane or an effect on signal transduction within eukaryotic cells. However, before a toxin can affect a cell, it must after its secretion by a microorganism, recognise and bind to a specific surface molecule, its receptor. Membrane receptors of bacterial enterotoxins have been identified as protein, glycoprotein or glycolipid in nature. The chemical nature of the molecules acting as receptors is crucial and during evolution they have been carefully selected. Some toxins, after their interaction with a receptor molecule, will transduce a signal across the cell membrane while remaining at the cell surface. Other toxins, after this initial binding step with a receptor, will be internalised. Others can form pores leading to leakage of cellular components and cell lysis. Receptors that have been identified often comprise a saccharidic chain that is directly involved in the recognition and binding of the toxin. Today, models explaining toxin-receptor interactions are more complex, including multistep events. This review summarises the knowledge of the interactions between bacterial toxins and membrane receptors present on intestinal mucosa. receptor / intestine / enterotoxin / binding epitope / glycosphingolipidRésumé -Les toxines bactériennes entériques présentent une grande diversité autant dans leur structure que dans leur poids moléculaire et leur mécanisme d'action. L'interaction des entérotoxines avec la muqueuse intestinale conduit soit à un effet direct sur la paroi cellulaire de la cellule hôte, soit à un dérèglement des voies de signalisation de celle-ci. Toutefois, avant même d'affecter la cellule cible, la toxine sécrétée par le micro-organisme devra reconnaître et s'attacher à une molécule présente à la surface cellulaire, son récepteur. Les récepteurs membranaires des entérotoxines bactériennes peuvent être de nature protéique, glycoprotéique ou glycolipidique. La nature chimique de ces récepteurs, sur laquelle repose la spécificité, est primordiale et au cours de l'évolution ceuxci ont été soigneusement sélectionnés. Certaines toxines, une fois en contact avec leur récepteur, envoient un signal à l'intérieur de la cellule tout en demeurant à la surface alors que d'autres toxines sont internalisées. Enfin, certaines toxines bactériennes peuvent former des pores dans la membrane Vet. Res. 31 (2000)

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Initial Stages in Infection with Animal Viruses

Cited by 171 publications

References 195 publications

Baculovirus Replication: Uptake of Trichoplusia ni Nuclear Polyhedrosis Virus Particles by Insect Cells

Baculovirus Replication: Uptake of Trichoplusia ni Nuclear Polyhedrosis Virus Particles by Insect Cells

Vaccines for the Future?

Les récepteurs des entérotoxines bactériennes

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