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Biomedical subjects

D Blaas

Publications and source records attributed to D Blaas.

81 records · Page 5Linked to original sources
PubMed1985

Human rhinovirus 2: complete nucleotide sequence and proteolytic processing signals in the capsid protein region.

cDNA clones representing the entire genome of human rhinovirus 2 have been obtained and used to determine the complete nucleotide sequence. The genome consists of 7102 nucleotides and possesses a long open reading frame of 6450 nucleotides; this reading frame is initiated 611 nucleotides from the 5' end and stops 42 nucleotides from the polyA tract. The N-terminal sequences of three of the viral capsid proteins have been elucidated, thus defining the positions of three cleavage sites on the polyprotein. The extensive amino acid sequence homology with poliovirus and human rhinovirus 14 enabled the other cleavage sites to be predicted. Cleavages in the 3' half of the molecule appear to take place predominantly at Gln-Gly pairs, whereas those in the 5' half (including the capsid proteins) are more heterogeneous.

Amino Acid Sequence↗
PubMed1984

Relationship of human rhinovirus strain 2 and poliovirus as indicated by comparison of the polymerase gene regions.

cDNA clones representing the 3'-terminal region of the human rhinovirus strain 2 genome have been obtained. The sequence of 1425 nucleotides adjacent to the poly(A) tract is presented and contains an open reading frame of 1383 nucleotides. The derived amino acid sequence corresponding to the putative RNA polymerase-coding region is compared to those of poliovirus type 1 (Mahoney) and foot-and-mouth disease virus A12. A high degree of homology between human rhinovirus strain 2 and poliovirus type 1 (Mahoney) was found within the coding sequence but not within the 3'-untranslated region.

Amino Acid Sequence↗
PubMed1983

CAP binding proteins associated with the nucleus.

Cap binding proteins of HeLa cells were identified by photo-affinity labelling using the cap analogue gamma-[32P]-[4-(benzoyl-phenyl)methylamido]-7-methylguanosine-5'- triphosphate. Photoreaction with whole cell homogenates resulted in specific labelling of five major polypeptides. The small molecular weight polypeptide appeared to be identical to the 24 000 to 26 000 dalton cap binding protein previously identified in initiation factors. A cap binding protein of 37 000 dalton was found in initiation factors as well as in preparations of crude nuclei. It was released from nuclei by washing with buffer of moderate salt concentration. Three high molecular weight cap binding proteins (approximately 120 000, approximately 89 000, approximately 80 000 dalton) were found in the nuclear fraction and were only partly released upon nuclease digestion and high salt extraction.

Affinity Labels↗
PubMed1982

Identification of the cap binding protein of influenza virus.

The presence of a cap binding protein in influenza virus PR8 has recently been demonstrated by photoaffinity labelling with the cap-analogue (gamma [3 2P]-[4-(benzoylphenyl)methylamido]-7-methylguanosine 5'-triphosphate). This paper describes the identification of the labelled protein using two-dimensional gel electrophoresis. The protein is shown to be PB2, the smaller of the two basic P proteins in the polymerase complex.

Carrier Proteins↗
PubMed1982

Identification of the cap-binding protein of two strains of influenza A/FPV.

We have identified the cap-recognizing protein of two strains of influenza A fowl plague virus (FPV) by photoaffinity labelling of virion proteins with a photoreactive analogue of the 5'-methyl cap structure of messenger RNA. The cap-recognizing protein of influenza A/FPV/Rostock/34 is the P2 polypeptide, and that of influenza A/FPV/Dutch/27 (Dobson) is the P3 polypeptide. In each case the cap-recognizing protein is the product of RNA segment 1.

Affinity Labels↗
PubMed1978

Use of trypsin for rapid and efficient purification of murine sarcoma and leukemia virus.

A method is described for purification of MSV-MuLV from culture supernatant of chronically infected 78A,1 rat embryo cell line. This method involves direct polyethylene glycol-NaCl precipitation of the low speed supernatant of culture fluid followed by digestion of the pellet with trypsin. This procedure efficiently disrupts large aggregates which normally entrap most of the virus. Highly purified virus can be obtained in very good yield by a combination of sedimentation velocity and isopycnic centrifugation : yields up to 100 A280 units (17 mg of protein) of purified virus per liter of culture fluid can be observed. This procedure appears well suited for large scale isolation of virion associated enzymatic activities.

Animals↗
PubMed1977

[Evidence of protein kinase activity in 2 murine oncornaviruses].

A protein kinase activity has been detected in two strains of murine Oncornaviruses, MSV/MLV and EFV. This activity phosphorylates not only endogenous viral proteins but also exogenous substrates (histones and phosvitin). The stimulation of enzyme activity by detergents along with the increase of specific activity in viruses treated with trypsin during purification suggest that the enzyme is located in the viral particle.

Gammaretrovirus↗