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Biomedical subjects

A K Banerjee

Publications and source records attributed to A K Banerjee.

At least 289 records · Page 16Linked to original sources
PubMed1988

Ribonuclease activity is associated with subviral particles isolated from interferon-treated vesicular stomatitis virus-infected cells.

Previously we have shown that inhibition of replication of vesicular stomatitis virus in interferon-treated JLSV-11 cells is at least partly caused by impaired viral primary transcription. Here we report that subviral particles isolated from interferon-treated infected cells were deficient in mRNA synthesis in vitro compared with the particles isolated from untreated cells. This was due to the presence of an associated ribonuclease activity which hydrolyzed not only newly synthesized viral mRNAs but also exogenously added viral transcripts.

Cell Line↗
PubMed1988

Resolution of multiple complexes of phosphoprotein NS with nucleocapsid protein N of vesicular stomatitis virus.

The interaction of the nucleocapsid protein N and the phosphoprotein NS of vesicular stomatitis virus (VSV) was studied, free of other viral proteins, by transcription from SP6 vectors, followed by translation in a rabbit reticulocyte lysate. N-NS complex formation depended strongly on cotranslation of the two proteins; when N and NS were mixed following separate translation of each, very little complex formation occurred. Conditions were found under which at least six N-NS complexes were separated from each other by electrophoresis in a nondenaturing gel system, and the following findings were made. (i) These complexes fell into two groups; complexes 1 through 5 all had a stoichiometry of two molecules of N to one molecule of NS, whereas N-NS complex 6 had an equimolar ratio of the two proteins. (ii) N-NS complexes 1 through 5 predominated at lower concentrations of NS relative to N, but N-NS complex 6 was the major or sole product when NS was equimolar to or in excess of N. (iii) The two sets of complexes were formed by two distinct types of interactions of NS with N. The formation of N-NS complexes 1 through 5 was abolished by the removal of as few as 11 amino acid residues from the basic, highly conserved carboxy-terminal domain of NS, which is essential for the binding of NS to the N-RNA template of VSV. In contrast, formation of complex 6 was unaffected by removal of as many as 62 of the carboxy-terminal amino acids of NS, a region encompassing both the terminal basic domain and an adjacent domain which is required for VSV RNA polymerase function. The significance of these observations for the mechanism of VSV genome replication is discussed.

Capsid↗
PubMed1988

Complex formation with vesicular stomatitis virus phosphoprotein NS prevents binding of nucleocapsid protein N to nonspecific RNA.

The interactions between the nucleocapsid protein N and either RNA or the phosphoprotein NS of vesicular stomatitis virus (VSV) were studied by the transcription of N and NS mRNAs from SP6 vectors, followed by translation in a rabbit reticulocyte lysate. Nascent N protein bound tightly to added labeled RNA, as well as to endogenous RNA in the reticulocyte lysate. This binding was demonstrated by three independent techniques. First, labeled N protein and labeled RNA migrated identically as a series of sharp, closely spaced bands in a nondenaturing gel system. Second, translated N protein behaved as a stable ribonucleoprotein complex in CsCl gradients and sedimented to the same density as the authentic N-RNA template of VSV. Third, translated N protein protected a series of labeled RNA fragments from digestion by RNase A. None of the three RNA-binding criteria was satisfied by either translated NS protein or two deletion mutants of N protein or by other components of the reticulocyte lysate. The evidence suggests that the observed binding of RNA by nascent N was not RNA sequence specific, in contrast to the encapsidation process during VSV replication. Moreover, the prior formation of N-NS complexes totally abolished the observed binding of RNA by N. Thus, we propose that NS may be responsible for conferring the sequence specificity of the RNA binding that occurs during VSV genome replication.

Capsid↗
PubMed1988

Crohn's or poisoning?

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Anti-Inflammatory Agents, Non-Steroidal↗
PubMed1988

Aprotinin reduces hypothermic mortality--an experimental model.

In order to test the postulate that post-hypothermic damage may be caused by protease activation, the effect of the administration of aprotinin on hypothermic mortality was investigated in anaesthetized rabbits. A group of 6 animals received 40.000 KIU aprotinin intravenously prior to the induction of hypothermia by surface cooling and this was followed by a further 35.000 KIU each hour for 5 h. The animals were cooled to 29 degrees C and then rewarmed. A control group received equal volumes of physiological saline. The aprotinin treated animals survived, whereas all the control group died within 7 days, 5 of them within 24 h. The haemodynamic, biochemical and haematological changes in the two groups are reported.

Animals↗
PubMed1988

Marfan's syndrome associated with Wolff-Parkinson-White syndrome type B.

A case of Marfan's syndrome associated with Wolff-Parkinson-White (WPW) syndrome is described and a discussion follows on the possible relationship of the two conditions. Isolated cases of such an association have been previously reported. It is possible that the association is more common than was previously recognized and the two conditions may share a common pathological basis. Moreover, WPW syndrome may contribute to the cardiac morbidity of Marfan's syndrome.

Adult↗
PubMed1988

A finite deformation model of infantile hydrocephalus.

Clinical data obtained about intracranial pressure volume experiments abound in the literature. However, what is lacking is a proper interpretation of the data. A nonlinear hyperelastic model is proposed in this paper which is more realistic and simulates successfully the various states and stages of infantile hydrocephalus which have hitherto been considered puzzling. Strain energy function incorporating two and three constants have been employed to develop the constitutive equations and pressure-volume curves have been plotted for arbitrary values of the constants. The available clinical data can be employed through the proposed model to evaluate the status of hydrocephalus and also to arrive at suitable measures to relieve the intracranial pressure and ventricular dilatation.

Algorithms↗
PubMed1988

Role of immune complexes in cerebral malaria.

To investigate the involvement of immune complexes in the pathogenesis of cerebral malaria, a comparative study between Plasmodium berghei infected Swiss albino mice and BALB/c mice was conducted. Rise in parasitemia was found to be same with differences in manifestation of disease and mortality, level of immune complexes and histopathology. Increased parasitized red cells with swelling of endothelial cells in the brain capillaries along with increased levels of circulating immune complexes were observed in the BALB/c mice.

Animals↗
PubMed1987

Phosphorylation within a specific domain of the phosphoprotein of vesicular stomatitis virus regulates transcription in vitro.

We have investigated the functional significance of phosphoserine residues that lie in the L protein-binding domain between amino acids 213 and 247 of the phosphoprotein (NS) of vesicular stomatitis virus. A series of mutant NS proteins were made by cell-free translation of mRNAs transcribed from the cloned gene. Site-directed substitution of alanine for both serine 236 and serine 242 essentially abolished RNA synthesis catalyzed by the NS-L complex. Substitution of either of these serines reduced RNA synthesis by 75%. Serine 218 played no major role in RNA synthesis. Phosphorylation of NS by the L protein was abrogated by substitution of either serine 236 or serine 242. These results indicate that phosphorylation of serines 236 and 242 in the NS protein regulates its binding with the L protein and the N-RNA template and is essential for activation of viral RNA synthesis.

Amino Acid Sequence↗