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P K Chanda

Publications and source records attributed to P K Chanda.

46 records · Page 3Linked to original sources

Inactivation of influenza and vesicular stomatitis virion RNA polymerase activities by photoreaction with 4'-substituted psoralens.

Irradiation of purified influenza virus and vesicular stomatitis virus (VSV) with long-wavelength UV light in the presence of 4'-substituted psoralens inactivated the virion-associated RNA polymerase activity. Inactivation was apparently due to psoralen modification of the viral genome RNAs, since cations that decrease psoralen binding to nucleic acids had a protective effect, and reconstitution of VSV RNA polymerase activity was inhibited by photoreaction of nucleoprotein cores but not by pretreatment of soluble fraction from dissociated virions. Partially inactivated viral particles synthesized reduced amounts of full-length RNA products in vitro without an increase in prematurely terminated transcripts. VSV leader RNA formation was relatively resistant to psoralen photoinactivation, and sequential transcription was maintained by photoreacted VSV. The all-or-none psoralen effect on virion-associated RNA polymerase activities may be due to a differential photosensitivity of promoter sites or to structural changes in modified viral genome RNAs that prevent formation of new mRNA chains.

DNA-Directed RNA Polymerases↗

Characteristics of a cholera phage.

The basic physical, chemical and physiological properties of a group II cholera phage belonging to Mukerjee's classification has been described.

Adsorption↗

Photoreactivating property of the Vibrio cholerae cell system.

Ultraviolet-inactivated chlora phage PL163/10 underwent a maximum of abot 36% of photoreactivation within the host V. cholerae cells. UV-inactivated but non-infected V. cholerae cells also underwent the same degree of photoreactivation.

Bacteriophages↗

Molecular weight analysis of the polypeptides of cholera phage PL 163/10 by polyacrylamide gel electrophoresis.

Cholera phage PL 163/10, belonging to Mukerjee's Group I, was purified by alternate cycles of low and high speed centrifugation. Gel electrophoresis revealed the presence of four polypeptide chains of respective molecular weights of 10,370+/-515 (A), 30,000+/-1,303 (B), 40,000+/-1,049(C) and 64,000+/-2,433 (D) daltons. Electrophoresis of the sample alkylated with iodoacetic acid resolved the presence of only one polypeptide chain of an average molecular weight of 10,310+/-565 daltons. The polypeptides B, C and D could be interpreted as trimer, tetramer and hexamer respectively of the polypeptide A, which was the basic structural protein of this phage.

Bacteriophages↗

Properties of the cholera phage PL 163/10.

Vibrio cholerae phage PL 163/10, belonging to Mukherjee's group I, gave clear plaques with surrounding halos of overall diameters varying between 1 to 4 mm when plated on a lawn of host V. cholerae OGAWA 154. It was fairly stable in the PH range 6-11. Its thermal inactivation was characterised by half lives of 39, 12, 4.5 and 1.0 minutes at 55, 60, 65 and 70 degree C respectively. The thermodynamic parameters deltaH, deltaF and deltaS were determined at these temperatures. The phange was resistant in vitro to sodium deoxycholate, trytrypsin, chloroform, robonuclease, deoxyribonuclease, Tris, Tris + EDTA, Tris + lysozyme and phosphate buffer but rapidly inactivated by sodium lauryl sulfate. Adsorption of this phage was biphasic. Intracelllular growth of the PL 163/10 phage was characterised by an eclipse period of 13 minutes, latent period of 31 minutes, rise period of 29 minutes and an average burst size of about 10 PFU/cell. This phage possessed a hexagonal head 106 plus or minus 18 x x 740 plus or minus 27 A without any tail structure.

Adsorption↗

An HTLV-III peptide produced by recombinant DNA is immunoreactive with sera from patients with AIDS.

Human T-cell lymphotropic retrovirus type III (HTLV-III), also called lymphadenopathy-associated virus (LAV), has been identified as the aetiological agent of acquired immune deficiency syndrome (AIDS). The sera of most patients with AIDS or AIDS-related complexes, and of asymptomatic individuals infected with HTLV-III, contain antibodies against antigens of HTLV-III. The characterization of these antibodies and their corresponding viral antigens is important not only for understanding immunity against HTLV-III and the pathology of AIDS, but also for the development of diagnostic methods and preventive vaccine for AIDS. Following the successful establishment of a long-term T-cell line permissive for HTLV-III replication, large quantities of virus have been produced, facilitating the purification of viral proteins and the development of mouse monoclonal antibodies against several viral antigens. More recently, the structure of HTLV-III proviral DNA has been elucidated. We now report the production, by genetic engineering methods, of a peptide encoded by a gene segment of HTLV-III. A 1.1-kilobase (kb) EcoRI DNA segment from an isolate of HTLV-III was inserted into a lpp and lac promoter-coupled expression vector, pIN-III-ompA. Escherichia coli transformants of this plasmid produced a peptide of relative molecular mass (Mr) 15,000 (15K) which was strongly immunoreactive with anti-HTLV-III antibodies present in sera from AIDS patients. Lysates of the clones expressing this 15K peptide inhibited the reactivity of the p31 virion protein with AIDS sera, suggesting that it is a fragment of the viral p31 protein. The peptide reacted with sera from all 20 AIDS patients but none of the 8 normal controls tested. These results suggest that the peptide may be useful for detecting anti-HTLV-III antibodies in blood samples.

Acquired Immunodeficiency Syndrome↗