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At least 775 records · Page 43Linked to original sources
PubMed1984

The involvement of a helper component in nonpersistent transmission of plant viruses by aphids.

Certain plant viruses require a 'helper component' in order to be transmitted by aphids. The helper component for potyviruses is a virus-encoded protein with a subunit molecular weight of between 50,000 and 60,000. Aphid transmission of caulimoviruses is associated with the presence of an 18,000 molecular weight polypeptide. The mode of action of the helper component is the subject of speculation.

Animals↗
PubMed1996

Intracellular transport and processing of the Marburg virus surface protein in vertebrate and insect cells.

The surface protein (GP) of Marburg virus (MBG) is synthesized as a 90-kDa precursor protein which is cotranslationally modified by the addition of high-mannose sugars (140 kDa). This step is followed by the conversion of the N-linked sugars to endoglycosidase H (endo H)-resistant species and the addition of O-linked oliosaccharides leading to a mature protein of 170-200 kDa approximately 30 min after pulse labelling. The mature form of GP is efficiently transported to the plasma membrane. GP synthesized using the T7 polymerase-driven vaccinia virus expression system was transported with essentially the same kinetics as the authentic GP. However, the protein that is shown to appear 30 min after pulse labeling at the plasma membrane was slighly smaller (160 kDa) than GP incorporated into the virions (170 kDa). Using a recombinant baculovirus, GP was expressed at high levels in insect cells. Three different species could be identified: a 90-kDa unglycosylated GP localized in the cytoplasm and two 140-kDa glycosylated proteins. Characterization of the glycosylated GPs revealed that processing of the oligosaccharides of GP was less efficient in insect cells than in mammalian cells. The majority of GP remained endo H sensitive containing high-mannose type N-linked glycans, whereas only a small fraction became endo H resistant carrying processed N-glycans and O-glycans. Tunicamycin treatment of the GP-expressing cells demonstrated that N-glycosylation is essential for the transport of the MBG surface protein.

Animals↗
PubMed1992

Infectivity and pathogenesis of iridescent virus type 22 in various insect hosts.

This paper reports the results of a series of laboratory experiments to determine the infectivity and pathogenesis of iridescent virus type 22 (IV 22) for six species of mosquitoes, phlebotomine sand flies and triatomid bugs. Following inoculation, IV 22 replicated in all of the species tested, without producing noticeable mortality within a 14 day observation period. Examination of the infected insects by immunofluorescence demonstrated large amounts of viral antigen in many different organs. Electron microscopy done on infected mosquitoes (Aedes aegypti) showed large numbers of virus particles within cells of the fat body, muscle tracheal and midgut epithelium. Virus replication in the mosquitoes was confirmed to host cell cytoplasm and was similar to that described in the natural blackfly (Simulium) host. Transovarial transmission of IV 22 could not be demonstrated in A. aegypti, and only a small percentage of mosquito larvae could be infected orally. Results of these experiments are compatible with observations of other iridescent viruses; IV 22 is highly infectious for a wide range of insects when introduced into their hemolymph, but it is not very infectious per os. These characteristics would appear to limit its value as a potential biocontrol agent for Diptera.

Animals↗
PubMed1997

The loss of outer capsid protein P2 results in nontransmissibility by the insect vector of rice dwarf phytoreovirus.

A transmission-defective (TD) isolate of rice dwarf phytoreovirus lacked the ability to infect cells when derived from the virus-free insect vector Nephotettix cincticeps. Analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified virus showed that among six structural proteins, the P2 outer capsid protein (encoded by genome segment S2) was absent from the TD isolate, whereas all six proteins were present in the transmission-competent (TC) isolate. P2 was not detected on immunoblots of rice plants infected with the TD isolate. Genome segment S2 and its transcript were detected in both TD and TC isolates. Sequence analysis of the S2 segment of the TD isolate revealed the presence of a termination codon due to a point mutation in the open reading frame, which might explain the absence of P2 in the TD isolate. These results demonstrate that the P2 protein is one of the factors essential for infection by the virus of vector cells and, thus, influences transmissibility by vector insects.

Amino Acid Sequence↗
PubMed1990

Enzymatic activities of overexpressed herpes simplex virus DNA polymerase purified from recombinant baculovirus-infected insect cells.

Biochemical characterization of the herpes simplex virus (HSV) DNA polymerase, a model DNA polymerase and an important target for antiviral drugs, has been limited by a lack of pure enzyme in sufficient quantity. To overcome this limitation, the HSV DNA polymerase gene was introduced into the baculovirus, Autographa californica nuclear polyhedrosis virus, under the control of the polyhedrin promoter to give rise to a recombinant baculovirus, BP58. BP58-infected Spodoptera frugiperda insect cells expressed a polypeptide that was indistinguishable from authentic polymerase by several immunological and biochemical properties, at levels approximately ten-fold higher per infected cell than found in HSV-infected Vero cells. The DNA polymerase was purified to apparent homogeneity from BP58-infected insect cells. Using activated DNA as primer-template, the purified enzyme exhibited specific activity similar to that of enzyme isolated from HSV-infected Vero cells, indicating that additional polymerase-associated proteins from HSV-infected cells are not critical for activity with this primer-template. 3'-5' exonuclease activity co-purified with the BP58-expressed HSV DNA polymerase, demonstrating that this activity is intrinsic to the polymerase polypeptide. The purified enzyme also exhibited RNAse H activity. The recombinant baculovirus should permit detailed biochemical and biophysical studies of this enzyme.

Animals↗