PubMed Health⌕ Search

Biomedical subjects

R Usha

Publications and source records attributed to R Usha.

At least 19 recordsLinked to original sources

Differential roles of C4 and betaC1 in mediating suppression of post-transcriptional gene silencing: evidence for transactivation by the C2 of Bhendi yellow vein mosaic virus, a monopartite begomovirus.

Bhendi yellow vein mosaic disease (BYVMD) is caused by the association of a DNA beta satellite with a begomovirus component. The begomovirus component has two promoters, one in the virion sense (V-sense) and the other in the complementary sense (C-sense) in the intergenic region (IR). To study the promoter activities of V-sense and C-sense promoters, mGFP gene fusion was made downstream to the promoters. Transient and stable expressions in N. benthamiana leaves showed significant GFP expression under C-sense promoter whereas the expression under the V-sense promoter was very weak in the absence of the transactivator C2. Untransformed N. benthamiana plants were agroinfiltrated with binary vector constructs containing V-sense-GFP alone or along with C1, C2, C4, V1, V2 or betaC1 (in both sense and antisense orientations) to understand the roles of these gene products in transactivation and/or suppression of post-transcriptional gene silencing (PTGS). The results showed strong suppression of gene silencing activities for C4 and betaC1 but a weak activity for C2. The suppression activities were also confirmed using gfp-silenced GFP16c/GFPi plants by agroinfiltration and agroinoculation. The expression of C4 and betaC1 as transgenes produced abnormal phenotypic growth compared to the other viral genes mentioned above, further supporting their suppressor function.

Begomovirus↗

Protein-protein interactions and nuclear trafficking of coat protein and betaC1 protein associated with Bhendi yellow vein mosaic disease.

Bhendi yellow vein mosaic disease (BYVMD) is caused by a complex consisting of a monopartite begomovirus BYVMV and a satellite DNA beta component. BYVMV represents a new member of the emerging group of monopartite begomoviruses requiring a satellite component for symptom induction. Here we report the results of the transient expression of green fluorescent protein (GFP) fused with the betaC1 and coat protein (CP) coding regions, in the epidermal cells of Nicotiana benthamiana. GFPCP was found to be targeted into the nucleus whereas GFPbetaC1 was localized towards the periphery of the cell. The sub-cellular localization of the betaC1 protein has been compared with that of the CP in yeast cells using a genetic system for detection of protein nuclear import and export. Expression of betaC1 ORF in transgenic N. benthamiana under the control of the Cauliflower mosaic virus 35S promoter produced severe developmental abnormalities in the plant, like distorted stem, leaves and stunting of the plant. We also present the results on the interaction of CP and betaC1 proteins using yeast two hybrid analysis, suggesting a collaborative role in the inter- and intracellular dynamics of BYVMD.

Active Transport, Cell Nucleus↗

Refolding, purification and characterization of replication-initiator protein from soybean-infecting geminivirus.

The replication-initiator protein (Rep) from a soybean-infecting geminivirus was overexpressed in E. coli as a fusion protein with maltose binding protein (MBP). In spite of the presence of the highly soluble MBP as the fusion partner, the overexpressed MBP-Rep fusion protein formed insoluble inclusion bodies. The protein was solubilized from the inclusion bodies and refolded. The refolded MBP-Rep protein was purified using ion exchange and amylose affinity chromatography. The activity of the purified MBP-Rep was assessed using an in vitro cleavage assay. Soluble and stable MBP-Rep protein was obtained in high abundance, providing the feasibility of large-scale production of active Rep protein for functional characterization and X-ray crystallographic structure determination.

Chromatography, Affinity↗

Structural influence of mono and polyhydric alcohols on the stabilization of collagen.

In the present study, solvents effects on the structure of collagen have been examined by circular dichroism and their interfacial tension at glass/liquid and Teflon/liquid. Changes in the conformations of the protein have been analyzed after equilibration with aqueous solutions of monohydric and polyhydric alcohols like methanol, ethanol, n-propanol, propane-2-diol and glycerol. The results from viscosity and Circular dichroism (CD) spectra suggest a clear distinction in the structural changes for collagen with monohydric alcohols as against polyhydric ones. The surface tension and interfacial tension at glass (high surface energy, HFSE) and Teflon (Low surface energy, LSFE) reflect similar differences between the monohydric and polyhydric alcohols. Studies on the interfacial energy of the adsorbed protein at glass/solution interface compared to that of Teflon/solution interface show that the water structure near glass gets perturbed leading to an increase in the average free energy of the bulk water phase and a reduction in hydrophobic effect near the glass. The results suggest that the different solvents alter the hydrophobic effect on the hydrated protein to different extent and thus influence folding equilibrium of the protein without directly interacting with it. Polyhydric alcohols seem to favor the native collagen structure while monohydric alcohols enhance it.

Acetates↗

Structure and conformation of intramolecularly cross-linked collagen.

This work reports the effects of cross-linking agent like formaldehyde (HCHO) and glutaraldehyde (GA) on monomeric collagen and its conformational stability using circular dichroism. The nature of the bonds formed and the stability of the cross-links introduced vary with the aldehyde. The amount of HCHO required is four times greater than GA to induce similar changes in the molar ellipticity. This is due to the structural changes of collagen-aldehyde reaction. The change in the molar ellipticity and Rpn ratio for HCHO and GA treated collagen suggest possible aggregation of collagen molecule. The relative viscosity of native and aldehyde treated collagen was measured and correlated to the changes seen in the CD spectra. The small amount of aldehydes are needed to induce changes in the conformational stability of collagen. This can be applied to the biomaterial and biomedical application.

Animals↗

Molecular characterization of two soybean-infecting begomoviruses from India and evidence for recombination among legume-infecting begomoviruses from South [corrected] South-East Asia.

The complete nucleotide sequences of two soybean-infecting begomoviruses have been determined from central and southern parts of India. Sequence analyses show that the isolate from central India is a strain of Mungbean yellow mosaic India virus (MYMIV) and the southern Indian isolate is a strain of Mungbean yellow mosaic virus (MYMV). Multiple DNA B components could be detected with the soybean strain of Mungbean yellow mosaic virus species. The nucleotide sequence similarity between the DNA A components of the two isolates is higher (82%) than that between the corresponding DNA B components (71%). Analyses of the common region of the genomic components of these two virus isolates indicate considerable divergence in the origin of replication (ori), which did not impair their infectivity as demonstrated for the central Indian isolate by agroinfection with partial tandem repeats (PTRs) of the genomic components. Detailed sequence and phylogenetic analyses reveal the distribution and possible recombination events among legume-infecting begomoviruses from South-East Asia.

Base Sequence↗

High genetic diversity in the coat protein and 3 untranslated regions among geographical isolates of Cardamom mosaic virus from south India.

A survey was conducted to study the biological and genetic diversity of Cardamom mosaic virus (CdMV) that causes the most widespread disease in the cardamom growing area in the Western Ghats of south India. Six distinct subgroups were derived based on their symptomatology and host range from the sixty isolates collected. The serological variability between the virus isolates was analysed by ELISA and Western blotting. The 3 terminal region consisting of the coat protein (CP) coding sequence and 3 untranslated region (3 UTR) was cloned and sequenced from seven isolates. Sequence comparisons revealed considerable genetic diversity among the isolates in their CP and 3 UTR, making CdMV one of the highly variable members of Potyviridae. The possible occurrence of recombination between the isolates and the movement of the virus in the cardamom tract of south India are discussed.

3' Untranslated Regions↗

Expression of Cardamom mosaic virus coat protein in Escherichia coli and its assembly into filamentous aggregates.

Cardamom mosaic virus (CdMV), a member of the genus Macluravirus of Potyviridae, causes a mosaic disease in cardamom. A polyclonal antiserum was raised against the purified virus and IgG was prepared. Electron microscopic studies on the purified virus showed flexuous filamentous particles of approximately 800 nm in length, typical of members of Potyviridae. The coat protein (CP) encoding sequence of the virus was expressed in Escherichia coli and the protein purified by affinity chromatography under denaturing conditions. The viral nature of the expressed CP was confirmed by positive reaction with anti CdMV IgG in a Western blot. The expressed CP aggregated irreversibly upon renaturation at concentrations above 0.07 mg/ml. The expression of the CP led to the formation of filamentous aggregates in E. coli as observed by immuno-gold electron microscopy. The filamentous aggregates were of 100-150 nm in length. Immuno-capture RT-PCR confirmed the absence of coat protein mRNA in the filamentous aggregates. Deletion mutations, which were expected to inhibit virus assembly, were introduced in the core region of the coat protein. However, these mutations did not improve the solubility of the CP in non-denaturing buffers.

Blotting, Western↗

3'-Terminal sequence analysis of the RNA genome of the Indian isolate of cardamom mosaic virus: a new member of genus Macluravirus of potyviridae.

Cardamom mosaic virus, a possible member of the family Potyviridae has been associated with the mosaic disease (Katte disease) of small cardamom in India. A virus isolated from the symptomatic cardamom leaves was positive in ELISA only with antiserum to the Guatemalan isolate of cardamom mosaic virus and not with a number of other potyviruses. The size of the viral RNA (8.5 kb) and the molecular weight of the coat protein (CP) (38 kDa) were determined. A 1.8-kb product containing the partial nuclear inclusion body (NIb) gene, the entire coat protein gene and the 3' untranslated region (UTR) was amplified by reverse transcription (RT) and polymerase chain reaction (PCR), cloned and sequenced. The viral origin of the clone was confirmed by Northern hybridization with viral RNA. The experimentally determined N-terminal sequence of the CP matched with the deduced amino acid sequence of the CP gene. Sequence analysis of the clone suggests that the cardamom mosaic virus is a member of the Maclurvirus genus of the family Potyviridae.

3' Untranslated Regions↗

Molecular modelling of epitope presentation using membrane protein OmpC.

Three-dimensional models of the chimeric S. typhi OmpC protein carrying an epitope from rotavirus VP4 capsid protein on either of two exposed loops (fourth and sixth) were constructed separately, using computer-aided homology modelling. The theoretical model of S. typhi OmpC was used as a template. The monomers were initially energy minimized. The trimers were generated for both the chimeric S. typhi OmpC proteins and the structures were optimized after several cycles of minimization. The surface accessibility calculations for the resulting models show that epitope recognition should be more effective in the fourth loop than in the sixth loop, in accordance with the experimental results on the immunogenic nature of the rotaviral epitope inserted into the two putative loops of S. typhi OmpC.

Amino Acid Sequence↗

Region-specific attenuation of a trypsin-like protease in substantia nigra following dopaminergic neurotoxicity by 1-methyl-4-phenyl-1,2, 3,6-tetrahydropyridine.

We analysed apoptosis, caspase-1 and -3, and trypsin-like protease activity in the nigrostriatal pathway during 1-methyl-4-phenyl-1,2,3, 6-tetrahydropyridine (MPTP)-induced neurotoxicity. MPTP injected (30 mg/kg, i.p., twice, 16 h apart) mice were sacrificed on 1, 2 and 7 days. DNA extracted from nucleus caudatus putamen (NCP) and substantia nigra (SN) was subjected to agarose gel electrophoresis. Typical apoptotic-like DNA cleavage was absent in SN or NCP after this dose of MPTP. A trypsin-like protease activity was significantly decreased in SN and not in NCP. While caspase-3 activity in the whole brain was increased significantly, caspase-1 activity was unaffected. Striatal dopamine content was decreased to 75% by 7 days. The absence of typical DNA 'ladder' when there was severe striatal dopamine depletion suggests that in vivo MPTP-mediated dopaminergic neurotoxicity may not involve apoptotic cell death, and explains why in mice MPTP-induced dopamine depletion is transient. The region-specific decrease in trypsin-like protease activity and absence of caspase-3 activation in SN signify the importance of trypsin-like protease in the regulation of apoptosis in MPTP-neurotoxicity in mice.

1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine↗

Empty sella syndrome presenting as galactorrhoea.

A prolactin secreting tumour is the commonest cause of the amenorrhoea-galactorrhoea syndrome. Galactorrhoea is a rare presentation of an empty sella syndrome. The empty sella syndrome commonly presents with headache and visual impairment and occasionally with endocrine disturbances in hypertensive middle aged women. The authors present a case of hyperprolactinemia resulting in galactorrhoea in a middle aged lady associated with a primary empty sella syndrome.

Empty Sella Syndrome↗

The refined crystal structure of cowpea mosaic virus at 2.8 A resolution.

Comoviruses are a group of plant viruses in the picornavirus superfamily. The type member of comoviruses, cowpea mosaic virus (CPMV), was crystallized in the cubic space group I23, a = 317 A and the hexagonal space group P6(1)22, a = 451 A, c = 1038 A. Structures of three closely similar nucleoprotein particles were determined in the cubic form. The roughly 300-A capsid was similar to the picornavirus capsid displaying a pseudo T = 3 (P = 3) surface lattice. The three beta-sandwich domains adopt two orientations, one with the long axis radial and the other two with the long axes tangential in reference to the capsid sphere. T = 3 viruses display one or the other of these two orientations. The CPMV capsid was permeable to cesium ions, leading to a disturbance of the beta-annulus inside a channel-like structure, suggesting an ion channel. The hexagonal crystal form diffracted X rays to 3 A resolution, despite the large unit cell. The large ( approximately 200 A) solvent channels in the lattice allow exchange of CPMV cognate Fab fragments. As an initial step in the structure determination of the CPMV/Fab complex, the P6(1)22 crystal structure was solved by molecular replacement with the CPMV model determined in the cubic cell.

Amino Acid Sequence↗

Purification of a multicatalytic protease complex from developing winged bean seeds by indirect immunoaffinity chromatography.

Many protease inhibitors have been characterized from leguminous seeds but very little is known about seed proteases which are supposedly regulated by these inhibitors. We have developed an indirect immunoaffinity chromatography system for the purification of cognate proteases from the same source, based on preferential high salt elution of the enzyme from a ternary complex of the protease, the inhibitor, and the anti-inhibitor IgG. Using anti-winged bean chymotrypsin inhibitor (WbCI) IgG as an affinity ligand, a multicatalytic protease complex has been purified from developing winged bean (Psophocarpus tetragonolobus) seeds. The purified preparation resolves into two large proteolytically active components when subjected to gel permeation chromatography under nondenaturing conditions, while SDS/PAGE analysis shows the presence of approximately 15 polypeptide chains in the 20- to 115-kDa range. The preparation cleaves known synthetic peptide substrates of trypsin, chymotrypsin, and V8 protease and it is only partially inhibited by a number of class-specific protease inhibitors. Western blot analysis shows the presence of WbCI in the purified preparation even after its extensive removal by the IgG-Sepharose column. The versatility of the indirect immunoaffinity chromatography system is attested by its extension to the soybean seeds.

Adenosine Triphosphatases↗

Kenny-Caffey syndrome in six Bedouin sibships: autosomal recessive inheritance is confirmed.

We are reporting on 16 children, in 6 unrelated sibships, born to healthy, consanguineous parents of Bedouin ancestry. Eleven of them were assessed clinically. All presented with marked growth retardation, craniofacial anomalies, small hands and feet, hypocalcemia, hypoparathyroidism, radiological evidence of cortical thickening of long bones with medullary stenosis, and absent diploic space in the skull. There was a history of 6 affected sibs dying in infancy with hypocalcemic convulsions. All cases show absence of macrocephaly and early psychomotor retardation. The present cases confirm the presence of clinical variability and co firm autosomal recessive inheritance of Kenny-Caffey syndrome.

Abnormalities, Multiple↗

Proteases of germinating winged-bean (Psophocarpus tetragonolobus) seeds: purification and characterization of an acidic protease.

Two major classes of protease are shown to occur in germinating winged-bean (Psophocarpus tetragonolobus) seeds, by assaying extracts at pH 8.0 and pH 5.1 with [14C]gelatin as substrate. At pH 8.0, the activity profile of the enzyme shows a steady rise throughout the period of germination, whereas the activity at the acidic pH is very low up to day 5 and then increases sharply reaching a peak on day 11, followed by an equally sharp decline. The winged-bean acidic protease (WbAP) has been purified to apparent homogeneity, as attested by a single protein band on both PAGE and SDS/PAGE. WbAP is a monomeric enzyme with a molecular mass of 35 kDa and a pH optimum of 6.0. It is a thiol protease that does not belong to the papain family and it has tightly bound Ca2+ as shown by 45Ca(2+)-exchange studies. Besides gelatin and casein, it hydrolyses a 29 kDa winged-bean protein, indicating a prospective physiological role for it in storage-protein mobilization. Immunoblot analysis shows that it occurs only in the seeds and sprouting tubers of this plant and also that it is synthesized in developing seeds just before desiccation. It appears that the newly synthesized enzyme is inactive, and activation takes place around day 6 of germination. However, neither the mechanism of activation nor the signal that triggers it is clearly understood.

Calcium↗

The primary structure of sheep liver cytosolic serine hydroxymethyltransferase and an analysis of the evolutionary relationships among serine hydroxymethyltransferases.

The complete amino-acid sequence of sheep liver cytosolic serine hydroxymethyltransferase was determined from an analysis of tryptic, chymotryptic, CNBr and hydroxylamine peptides. Each subunit of sheep liver serine hydroxymethyltransferase consisted of 483 amino-acid residues. A comparison of this sequence with 8 other serine hydroxymethyltransferases revealed that a possible gene duplication event could have occurred after the divergence of animals and fungi. This analysis also showed independent duplication of SHMT genes in Neurospora crassa. At the secondary structural level, all the serine hydroxymethyltransferases belong to the alpha/beta category of proteins. The predicted secondary structure of sheep liver serine hydroxymethyltransferase was similar to that of the observed structure of tryptophan synthase, another pyridoxal 5'-phosphate containing enzyme, suggesting that sheep liver serine hydroxymethyltransferase might have a similar pyridoxal 5'-phosphate binding domain. In addition, a conserved glycine rich region, G L Q G G P, was identified in all the serine hydroxymethyltransferases and could be important in pyridoxal 5'-phosphate binding. A comparison of the cytosolic serine hydroxymethyltransferases from rabbit and sheep liver with other proteins sequenced from both these sources showed that serine hydroxymethyltransferase was a highly conserved protein. It was slightly less conserved than cytochrome c but better conserved than myoglobin, both of which are well known evolutionary markers. C67 and C203 were specifically protected by pyridoxal 5'-phosphate against modification with [14C]iodoacetic acid, while C247 and C261 were buried in the native serine hydroxymethyltransferase. However, the cysteines are not conserved among the various serine hydroxymethyltransferases. The exact role of the cysteines in the reaction catalyzed by serine hydroxymethyltransferase remains to be elucidated.

Amino Acid Sequence↗