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Biomedical subjects

A Kundu

Publications and source records attributed to A Kundu.

31 records · Page 2Linked to original sources
PubMed1994

Abortive replication of influenza virus A/WSN/33 in HeLa229 cells: defective viral entry and budding processes.

Since influenza A virus replication is defective in HeLa229 cells but productive in Madin-Darby canine kidney (MDCK) cells, we have investigated the steps in the infectious cycle of A/WSN/33 virus defective in HeLa229 cells. We find that both the entry and exit processes of the infectious cycle were defective in HeLa229 cells. During entry, viral adsorption was apparently normal in HeLa229 cells but a subsequent step(s) involving one or more processes namely the fusion/uncoating and nuclear transport of viral ribonucleoprotein was inefficient and slow compared to those in MDCK cells. Fewer HeLa229 cells were infected at the same multiplicities of infection, resistance to ammonium chloride developed much more slowly and degradation of the incoming virus proteins was delayed when compared to those in MDCK cells. Subsequent to the entry process, there was no significant difference in either the synthesis of viral proteins or the transport, maturation, and membrane insertion of viral glycoproteins although the glycosylation pattern of hemagglutinin was different and the peak protein synthesis was albeit delayed in HeLa229 cells compared to that in MDCK cells. However, there was a major defect in the budding and release of viral particles. In HeLa229 cells, viral bud formation occurred but viral particles remained attached to the plasma membrane and were not released into the medium. This defect in virus release was not due to lack of neuraminidase activity but could be, at least partly, overcome by cytochalasin B treatment, suggesting a possible involvement of microfilaments in virus release. These results indicate that the abortive replication of influenza virus A/WSN/33 in HeLa229 cells appears to be due to multiple defects involving both the entry and release of viral particles and that host cell membrane and microfilaments may be important contributing factors in these processes.

Animals↗
PubMed1994

Analysis of the signals for polarized transport of influenza virus (A/WSN/33) neuraminidase and human transferrin receptor, type II transmembrane proteins.

In polarized MDCK cells influenza virus (A/WSN/33) neuraminidase (NA) and human transferrin receptor (TR), type II glycoproteins, when expressed from cloned cDNAs, were transported and accumulated preferentially on the apical and basolateral surfaces, respectively. We have investigated the signals for polarized sorting by constructing chimeras between NA and TR and by making deletion mutants. NATR delta 90, which contains the cytoplasmic tail and transmembrane domain of NA and the ectodomain of TR, was found to be localized predominantly on the apical membrane, whereas TRNA delta 35, containing the cytoplasmic and transmembrane domains of TR and the ectodomain of NA, was expressed preferentially on the basolateral membrane. TR delta 57, a TR deletion mutant lacking 57 amino acids in the TR cytoplasmic tail, did not exhibit any polarized expression and was present on both apical and basolateral surfaces, whereas a deletion mutant (NA delta 28-35) lacking amino acid residues from 28 to 35 in the transmembrane domain of NA resulted in secretion of the NA ectodomain predominantly from the apical side. These results taken together indicate that the cytoplasmic tail of TR was sufficient for basolateral transport, but influenza virus NA possesses two sorting signals, one in the cytoplasmic or transmembrane domain and the other within the ectodomain, both of which are independently able to transport the protein to the apical plasma membrane.

Amino Acid Sequence↗
PubMed1992

Eating epilepsy: a study of twenty cases.

Twenty cases of eating epilepsy have been studied over a period of 5 years (1985-1989). Males outnumbered females (4:1). Heavy meal comprising conventional Indian diet (viz, rice, vegetables, etc), was found to be the most important provocating factor (14 out of 20 cases). The attacks occurred at lunch time in most cases (15). Thirteen cases had generalised seizures. Electro-encephalogram showed focal changes in 10 cases, generalised changes in 6 cases, while 4 cases had normal electro-encephalogram. Computerised tomography scan was normal in all the cases (7) when it was done.

Adolescent↗
PubMed1991

Cell surface transport, oligomerization, and endocytosis of chimeric type II glycoproteins: role of cytoplasmic and anchor domains.

We investigated the role of cytoplasmic and anchor domains of type II glycoproteins in intracellular transport, oligomerization, and endocytosis by expressing the wild-type and chimeric genes in mammalian cells. Chimeric genes were constructed by exchanging the DNA segments that encode the cytoplasmic and anchor domains between the human influenza virus (A/WSN/33) neuraminidase (NA) and transferrin receptor (TR). The chimeric proteins in which domains were exchanged precisely were productively targeted to the cell surface. However, the proteins appeared to assemble differently in the intracellular compartment. For example, while TR existed predominantly as a dimer, NATR delta 90, containing the cytoplasmic and signal-anchor domains of NA and the ectodomain of TR, was present as a tetramer, a dimer, and a monomer. Similarly, the influenza virus NA existed predominantly as a tetramer but TRNA delta 35, in which the cytoplasmic and signal-anchor domains of TR were joined to the ectodomain of NA, existed predominantly as a dimer, suggesting that the cytoplasmic and anchor domains of type II glycoproteins affect the subunit assembly of heterologous ectodomains. In addition, we analyzed the role of the cytoplasmic domain in endocytosis. NA and NATR delta 90 did not undergo endocytosis, whereas both TR and TRNA delta 35 were internalized efficiently, demonstrating that the NH2 cytoplasmic domain of TR was capable of internalizing a heterologous ectodomain (NA) from the cell surface.

Amino Acid Sequence↗
PubMedDate not supplied

Local segmentation of biomedical images.

In this paper, a new algorithm for local segmentation of biomedical images is presented. First, a relatively small region is selected for segmentation on the basis of dispersion measurement of local gray values. This small region is then segmented using a segmentation algorithm based on quantization approach. While quantizing a signal, the range of input signal is divided into a number of segments. All signal values within a segment are assigned a unique reconstruction value. In segmentation of gray level images, the problem is to classify or code gray values of the pixels into two or more groups. An N-level threshold selection method for segmentation thus becomes the design of an N-level optimal quantizer. This new approach is suitable for a number of biomedical applications where the objects of interest appear as small and localized in the images. Some experimental results are also provided which illustrate the success of the new scheme.

Algorithms↗