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Biomedical subjects

B K Rima

Publications and source records attributed to B K Rima.

At least 91 records · Page 5Linked to original sources
PubMed1983

An immunological study of infection of hamsters with large and small plaque canine distemper viruses.

The small plaque virus (SPV), derived from the Onderstepoort strain of canine distemper virus (CDV) does not cause a lethal encephalitis in weanling hamsters. When we immunosuppressed hamsters infected with this virus they developed an acute disease, similar to that produced by the large plaque virus (LPV). Passive transfer of maternal antibody from SPV infected mothers to their offspring was effective in preventing acute disease following LPV infection. Co-infection of animals with both LPV and SPV resulted in increased hamster survival, associated with high titres of serum antibody. Similarly, heat inactivated SPV, present during infection with LPV, increased the survival rate. Heat inactivated LPV did not inhibit acute disease, although hamsters had high titres of neutralizing antibody. A small number of animals developed a delayed or recurring paralysis after immunosuppression, exposure to maternal antibody or co-infection. It would appear that the neurovirulence of CDV for hamsters can be modified by altering the levels of circulating antibody early in infection.

Animals↗
PubMed1983

Comparison of morbillivirus proteins by limited proteolysis.

Proteins of a number of measles and SSPE virus strains have been compared by limited proteolysis and they appear to be largely conserved amongst the various strains. Viruses derived from SSPE cannot be distinguished from other measles viruses by this technique. Small differences in the digest patterns of the M proteins have been observed between the Edmonston and other measles virus strains. Furthermore, in some strains where the M proteins migrate slower in SDS-PAGE the limited proteolysis patterns are slightly different from those in other MV and SSPE virus strains. The limited proteolysis pattern of some canine distemper virus (CDV) proteins have been determined and nucleocapsid breakdown products have been identified in infected cells. Comparisons of proteins of four strains of CDV have shown that these, too, are largely conserved, although the digest of proteins of CDV appear to show more pronounced differences than those present in the MV and SSPE virus group. Limited proteolysis can be used readily to distinguish MV from CDV isolates.

Chemical Phenomena↗
PubMed1983

A simple method for the removal of mycoplasma contamination from paramyxovirus stocks.

A simple and quick method of detecting mycoplasmas in virus stocks using the fluorochrome Hoechst 33258 is described. Different methods of removal of mycoplasmas from stocks are discussed. The simple but effective method using gentamicin (0.2 mg/ml) or chloramphenicol (5 micrograms/ml) is demonstrated and chosen as the most efficient as judged using both the Hoechst stain and the direct assessment of mycoplasma RNA species labelled with [5-3H]uridine.

Animals↗
PubMed1981

A study of phosphorylation of the measles membrane protein.

A polypeptide (designated X) which migrates with a mobility similar to the membrane protein (M) of measles virus has been found in virus-infected cells. This polypeptide appears to be phosphorylated. However, limited proteolysis has shown that this protein is not a phosphorylated form of the M protein, but appears related to the P protein of measles virus.

Animals↗
PubMed1980

Polypeptide synthesis i mumps virus-infected cells.

The synthesis of polypeptides in infected Vero cells has been studied with two tissue culture adapted strains of mumps virus. Minor differences between the strains are found in the mobilities of the virus-specific polypeptides in SDS-PAGE. Eight virus-induced polypeptides have been identified with mol. wt. of 180K, 80K, 71K, 69K, 45 K, 39K, 23K and 17K. These may correspond to the L, HN, N, Fo, P, M, C and S polypeptides identified in other paramyxoviruses. The 69K F0 glycoprotein is probably a precursor for glycopolypeptides F1 and F2 with mol. wt. 61K and 14K, respectively.

Animals↗
PubMed1980

A comparison of measles and canine distemper virus polypeptides.

The polypeptides induced by canine distemper virus (CDV) strains have been characterized by polyacrylamide slab gel electrophoresis of infected cell lysates labelled with 35S-methionine, 14C-amino acids, 3H-glucosamine and 3H-mannose, or 32P-orthophosphate. Seven virus-induced polypeptides have been asigned the following nomenclature and mol. wt.: a large polypeptide L (180,000); a large glycoprotein G (77,000); a nucleocapsid-associated protein P (73,000); the nucleocapsid protein N (60,000); the smaller glycoprotein F0 (59,000); a membrane protein M (35,000) and a small polypeptide S (15,000). During pulse-chase experiments with 3H-glucosamine and 14C-amino acids the intensity of the F0 band decreases and that of the F1 and F2 bands increases; the H polypeptide band becomes more diffuse and the S-protein disappears. The N- and P- but not the M-proteins have been found to be phosphorylated. The polypeptide pattern of the Onderstepoort strain of CDV has been compared with that of two other CDV and with 17 measles and subactue sclerosing panencephalitis (SSPE) strains. Differences in the mobilities of various polypeptides have been observed between CDV and measles and SSPE strains; however, the only consistent difference is the mol. wt. of the M-protein of CDV strains which is smaller by 2000 than that of MV and this may be a biochemical marker to distinguish CDV from measles and SSPE virus strains.

Animals↗
PubMed1979

A comparison of polypeptides in measles and SSPE virus strains.

The polypeptide patterns of twelve subacute sclerosing panencephalitis (SSPE) and measles viruses have been compared by slab gel electrophoresis. The polypeptide patterns of nine strains of SSPE and measles virus were identical. Differences in the NP protein and the HA protein of the Oddo strain, the P protein of the large plaque variant of the Lec strain of SSPE and in the M protein of the Hu 2 measles strain could not be correlated with biological characteristics such as plaque morphology, origin or haemagglutination properties.

Electrophoresis, Polyacrylamide Gel↗
PubMed1979

Effect of undiluted passage on the polypeptides of measles virus.

Measles virus induces a large polypeptide (L; mol. wt. 180 K), a large glycopolypeptide (H; mol. wt. 80 K), a nucleocapsid associated polypeptide (P; mol. wt. 70 K), a nucleocapsid polypeptide (N; mol. wt. 60 K), a second glycopolypeptide (F0; mol. wt. 60 K), a matrix or membrane polypeptide (M; mol. wt. 37 K) and a small polypeptide (S; mol. wt. 15 K). The second glycopolypeptide (F0) appears to be cleaved in purified measles virus. Defective interfering particles accumulate during passage of measles virus leading to a decrease in the amounts of virus-specific protein synthesized in infected cells. Even in the best preparations of purified measles virus, host proteins are always detected and these become more predominant in preparations with low infectivity.

Carcinoma, Squamous Cell↗
PubMed1978

Deoxyribonucleoside-requiring mutants of Bacillus subtilis.

A number of deoxyribonucleoside-requiring mutants (dns) of Bacillus subtilis were isolated and their growth characteristics and ribonucleotide reductase activities were compared with those of the wild type and of a dna mutant (tsA13). Both tsA13 and dns mutants required the presence of a mixture of deoxyribonucleosides for growth at 45 degrees C but not at 25 degrees C. All the mutant strains tested contained ribonucleotide reductase activity which showed heat sensitivity similar to that of the enzyme from a wild-type strain. The reductase in B. subtilis seemed to reduce ribonucleoside triphosphates in a similar manner to the enzyme in Lactobacillus leichmannii.

Bacillus subtilis↗
PubMed1978

Synthesis of thymidine nucleotides in Bacillus subtilis.

To investigate the synthesis of thymidine nucleotides in Bacillus subtilis, mutants that carried various combinations of thyA, thyB, and other mutations affecting pyrimidine metabolism were isolated. It was found that exogenously supplied deoxycytidine was converted to thymidine nucleotides. The present data suggest that deoxycytidine nucleotides are first deaminated to yield deoxyuridine nucleotides which can serve as substrates for both thyA- and thyB-coded synthetases. A deaminase activity for dCDP was found in crude extracts of B. subtilis. A mutant lacking the deaminase activity was unable to convert deoxycytidine nucleotides to thymidine nucleotides.

Bacillus subtilis↗
PubMed1977

The role of defective interfering particles in persistent infection of Vero cells by measles virus.

Persistent infections by measles virus were rapidly established in the majority of Vero cells when monolayers were infected with virus stocks that had been passed three to five times from an undiluted inoculum. These virus stocks had low infectivity titres but normal haemagglutinin titres and were able to cause interference. The ability of such virus stocks to establish persistent infections seems to be due to the presence of defective interfering particles rather than of virus mutants. Measles virus released from a persistently infected Vero cell line at the 93rd passage had properties similar to the undiluted passage virus that generated persistent infections.

Animals↗
PubMed1977

Metabolism of pyrimidine bases and nucleosides in Bacillus subtilis.

In Bacillus subtilis, uracil (Ura), uridine (Urd), and deoxyuridine (dUrd) are metabolized through pathways similar to those of enteric bacteria. Ura is probably converted to uridine 5'-monophosphate by uridine 5'-monophosphate pyrophosphorylase. More than 95% of dUrd added to cultures is converted to Ura and deoxyribose-1-phosphate. Although dUrd kinase activity is detectable in vitro, this enzyme does not seem to play an important role in the metabolism of dUrd. The metabolism of cytosine (Cyt), cytidine (Cyd), and deoxycytidine (dCyd) in B. subtilis appears to be different from that in enteric bacteria. Cytosine cannot be used by Ura-requiring mutants as pyrimidine source. dCyd is deaminated by dCyd-Cyd deaminase or phosphorylated to dCyd nucleotides by dCyd kinase. Cyd is deaminated by dCyd-Cyd deaminase of phosphorylated by Cyd kinase. This Cyd kinase activity has never been reported for B. subtilis.

Bacillus subtilis↗