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Biomedical subjects

M A McCrae

Publications and source records attributed to M A McCrae.

62 records · Page 4Linked to original sources
PubMed1981

Terminal structure of reovirus RNAs.

S1 nuclease analysis and 3' terminal sequencing of the reovirus genome double-stranded RNAs and in vitro produced viral mRNAs has been used to establish the viral mRNA is a full length copy of the genome template. Sequence determination at the 3' end of the genome minus strand has by transposition allowed determination of the 5' terminal sequences of the viral mRNAs. In all but one case an AUG codon which could function in initiation of protein synthesis has been found within the determined sequence. The 3' ends of the plus strands from all genome segments were found to have a common sequence. The implications of these results on the mechanism of virus replication are discussed.

Base Sequence↗
PubMed1981

Molecular biology of rotaviruses. I. Characterization of basic growth parameters and pattern of macromolecular synthesis.

The United Kingdom tissue-adapted bovine rotavirus growing in African green monkey kidney (BSC-1) cells was selected as a model system with which to study the detailed molecular virology of rotavirus replication. Study of the kinetics of infectious virus production revealed a fairly rapid replication cycle, with maximum yield of virus after 10 to 12 h at 37 degrees C. Progeny genome synthesis was first detected during the virus latent period at 2 to 3 h postinfection. Study of the kinetics of viral polypeptide synthesis showed that virus rapidly inhibited cellular polypeptide synthesis such that by 4 h postinfection, only virus-induced polypeptides, 15 of which were detected, were being synthesized. No qualitative changes in the pattern of viral polypeptide synthesis were observed during infection, although, based on kinetic synthesis, three quantitative classes of polypeptides were defined. Pulse-chase analysis revealed three post-translational changes in viral proteins, two of which were shown to be due to glycosylation. Tunicamycin inhibition studies were used to identify the putative non-glycosylated precursors of the two glycoproteins. Comparison of the infected-cell polypeptides with those present in purified virions revealed that mot of the virus-induced proteins were incorporated into virions, with only VP9 being a truly nonstructural protein. Some localization of the various polypeptides within the purified virion was achieved by producing viral cores.

Animals↗
PubMed1978

Specific secretion of polypeptides from cells infected with vaccinia virus.

The pattern of polypeptides specifically secreted by cells after infection with vaccinia virus has been analyzed. A complex pattern of apparently virus-specified polypeptides exhibiting temporal control of the type seen with intracellular polypeptides after virus infection was observed. Some of the specifically secreted polypeptides were shown to be modified by glycosylation and sulfation. The possible significance of these results is discussed.

Cell Line↗
PubMed1977

Processing of a pseudorabies virus-induced protein which is glycosylated, sulphated and excreted.

Cells infected with pseudorabies virus excrete large amounts of a glycosylated sulphated protein, mol. wt. 89000, into the extracellular fluid. This paper reports the results of studies on the processing of this protein. Glycosylation occurs during, or very soon after, synthesis of the polypeptide chain. After a delay of several minutes the glycoprotein is sulphated; inhibition of glycosylation by high concentrations of glucosamine does not interfere with this process. The glycosylated sulphated polypeptide is then reduced in size from mol. wt. 99000 to 89000, possibly by proteolytic cleavage, and is excreted. Inhibition of glycosylation does not interfere with the excretion of this polypeptide, which is an energy-requiring process.

Azides↗
PubMed1977

Bunyamwera virus-induced polypeptide synthesis.

Bunyamwera virus-induced polypeptide synthesis in BSC-1 cell has been studied using polyacrylamide gel electrophoresis and autoradiography. Four virus-induced polypeptides were identified. Their molecular weights were 200 X 10(6) (L), 128 X 10(6) (G1), 31 X 10(6) (G2), and 23 X 10(6) (N). Pulse-chase experiments, short labeling experiments, and experiments using amino acid analogs failed to show evidence of polypeptides processing by proteolytic cleavage. Analysis of the kinetics of synthesis of these polypeptides showed that a clear division into early and late categories could be made, the onset of synthesis of polypeptide N and L rapidly reached a peak and then declined. Polypeptides G1 and G2 were made for several hours; their rate of synthesis then declined. All four polypeptides then continued to be made in relatively small amounts for many hours.

Arboviruses↗