Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.27.3 (RNase T1)
 1,228 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A procedure has been developed to map the genetic elements of avian tumor virus RNA, which has a molecular weight of about 3 X 10(6) daltons and a poly(A) sequence at the 3' end. For this purpose, about 30 RNase T1-resistant oligonucleotides were ordered relative to the 3'-poly(A) terminus of the RNA, to construct an oligonucleotide map of viral RNAs. A cluster of seven envelope gene (env)-specific oligonucleotides, identified by their absence from the otherwise very similar oligonucleotide map of an envelope-defective deletion mutant (which lacks the major viral glycoprotein), mapped at a distance of 0.9 to 1.6 X 10(6) daltons from the poly(A) end of sarcoma virus RNA. A cluster of three sarcoma gene (src)-specific oligonucleotides, identified by their absence from the otherwise nearly identical oligonucleotide map of a transformation-defective deletion mutant mapped at a distance of 0.2 to 0.6 X 10(6) daltons from the poly(A) end of sarcoma virus RNA. The oligonucleotide maps of sarcoma viruses and of related deletion mutants were the same from the poly(A) end up to 0.2 X 10(6) daltons and included one terminal oligonucleotide, termed C, which is found in all avian tumor viruses tested so far. Preliminary mapping experiments ordering the src-specific and env-specific oligonucleotides of recombinants, selected for sarcoma and envelope genes of different parents, agree with those obtained by comparing maps of wild type viruses and deletion mutants. A partial genetic map consistent with these results suggests that the src gene maps between the env gene and the 3'-poly(A) end of viral RNA. This map reads: poly(A)-src-env-(pol, gag).
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PMID:Sequences and functions of Rous sarcoma virus RNA. 18 29

Previous results from our laboratory have demonstrated that equine infectious anemia virus displays structural variations in its surface glycoproteins and RNA genome during passage and chronic infections in experimentally infected Shetland ponies (Montelaro et al., J. Biol. Chem. 259:10539-10544, 1984; Payne et al., J. Gen. Virol. 65:1395-1399, 1984). The present study was undertaken to obtain an antigenic and biochemical characterization of equine infectious anemia virus isolates recovered from an experimentally infected pony during sequential disease episodes, each separated by intervals of only 4 to 8 weeks. The virus isolates could be distinguished antigenically by neutralization assays with serum from the infected pony and by Western blot analysis with a monoclonal antibody against the major surface glycoprotein gp90, thus demonstrating that novel antigenic variants of equine infectious anemia virus predominate during each clinical episode. The respective virion glycoproteins displayed different electrophoretic mobilities on sodium dodecyl sulfate-polyacrylamide gels, indicating structural variation. Tryptic peptide and glycopeptide maps of the viral proteins of each virus isolate revealed biochemical alterations involving amino acid sequence and glycosylation patterns in the virion surface glycoproteins gp90 and gp45. In contrast, no structural variation was observed in the internal viral proteins pp15, p26, and p9 from any of the four virus isolates. Oligonucleotide mapping experiments revealed similar but unique RNase T1-resistant oligonucleotide fingerprints of the RNA genomes of each of the virus isolates. Localization of altered oligonucleotides for one virus isolate placed two of three unique oligonucleotides within the predicted env gene region of the genome, perhaps correlating with the structural variation observed in the envelope glycoproteins. Thus these results support the concept that equine infectious anemia virus is indeed capable of relatively rapid genomic variations during replication, some of which result in altered glycoprotein structures and antigenic variants which are responsible for the unique periodic disease nature observed in persistently infected animals. The findings of envelope specific differences in isolates of visna virus and of human T-cell lymphotropic virus III (acquired immune deficiency syndrome-related virus) suggest that this variation may be a common characteristic of the subfamily Lentivirinae.
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PMID:Rapid emergence of novel antigenic and genetic variants of equine infectious anemia virus during persistent infection. 300 67

The amino acid sequence of ribonuclease T2 (RNase T2) from Aspergillus oryzae has been determined. This has been achieved by analyzing peptides obtained by digestions with Achromobacter lyticus protease I, Staphylococcus aureus V8 protease, and alpha-chymotrypsin of two large cyanogen bromide peptides derived from the reduced and S-carboxymethylated or S-aminoethylated protein. Digestion with A. lyticus protease I was successfully used to degrade the N-terminal half of the S-aminoethylated protein at cysteine residues. RNase T2 is a glycoprotein consisting of 239 amino acid residues with a relative molecular mass of 29,155. The sugar content is 7.9% (by mass). Three glycosylation sites were determined at Asns 15, 76 and 239. Apparently RNase T2 has a very low degree of sequence similarity with RNase T1, but a considerable similarity is observed around the amino acid residues involved in substrate recognition and binding in RNase T1. These similar residues may be important for the catalytic activity of RNase T2.
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PMID:Amino-acid sequence of ribonuclease T2 from Aspergillus oryzae. 316 20

We have examined the molecular basis for the observed antigenic differences between isolates of western equine encephalomyelitis (WEE) virus and those of a serologically related alphavirus from the eastern United States designated Highlands J (HJ). The structural proteins of WEE virus isolates have mol. wt. of 55 x 10(3) (E1), 47 x 10(3) (E2) and 33 x 10(3) for the nucleocapsid. The E1 glycoprotein had an isoelectric point (pI) of 6.4 and induced haemagglutination-inhibiting (HI) antibody which was specific for WEE virus. The E2 glycoprotein of WEE virus had a pI of 8.4 and induced antibody which was virus specific by neutralization (PRNT) but cross-reacted with HJ virus in the radioimmune precipitation (RIP) test. Envelope glycoproteins of HJ virus isolates had mol. wt. of 58 x 10(3) (E1) and 49 x 10(3) EW) respectively. The E1 glycoprotein from HJ virus had a pI of 6.8 and induced antibody which reacted specifically in the HI, PRNT and RIP tests. Isolated E2 protein of HJ virus had a pI of 9.1 and induced antibodies which were reactive at equal titre with both WEE and HJ viruses by RIP. Two-dimensional gel electrophoresis of RNase T1 oligonucleotides of WEE virus and HJ virus genome RNase T1 oligonucleotides revealed that the primary structures of the RNAs of these two serologically related alphaviruses were very distant. The fingerprints of the oligonucleotides from 16 WEE viruses from western and central North America, Mexico and South America were similar to each other and easily distinguished from those of the eight HJ viruses isolated in the eastern United States from Massachusetts to Louisiana.
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PMID:A comparison of New World alphaviruses in the western equine encephalomyelitis complex by immunochemical and oligonucleotide fingerprint techniques. 615 28

The 32S RNA of the Friend strain of spleen focus-forming virus (SFFV) contains two sets of sequences: about half is specific to SFFV, and the other half is in common with the sequence of the helper lymphatic leukemia virus. Fingerprinting analysis of RNase T1 oligonucleotides showed that the SFFV-specific sequences were located in two distinct regions: in the 3' half and near the 5' terminus of the genome. Translation of SFFV RNA in a cell-free system yielded three SFFV-specific polypeptides: two main products with molecular weights of about 47,000 (P47) and 16,000 (P16) and a variable amount of a product with a molecular weight of 40,000 (P40). P47 was translated from polyadenylic acid-containing fragments of 1,500 to 3,000 nucleotides with SFFV-specific sequences from the 3' half of the genome, whereas P16, which contained peptides in common with those of P47, was synthesized by smaller RNA. P47 formed in vitro was found to be structurally related to the protein portion of a glycoprotein, gp55, specifically found in SFFV-infected cells in vitro. It is concluded from the results that a defective env gene containing SFFV-specific sequences in the 3' half of the genome codes for SFFV-specific gp55.
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PMID:Analysis of spleen focus-forming virus-specific RNA sequences coding for spleen focus-forming virus-specific glycoprotein with a molecular weight of 55,000 (gp55). 677 6

We reported previously that the antigenicity of the haemagglutinin-esterase (HE) glycoprotein of the human influenza C virus strain C/Nara/1/85 was indistinguishable from that of strain C/Nara/82. However, the ribonuclease T1-oligonucleotide map of total virion RNA of C/Nara/1/85 differed remarkably from the map of C/Nara/82, resembling instead the map of C/Nara/2/85, which has an HE antigenicity dissimilar to C/Nara/82 and C/Nara/1/85. This observation raised the possibility that C/Nara/1/85 might have arisen by reassortment from two viruses closely related to C/Nara/82 and C/Nara/2/85, respectively. Here, we compared the total nucleotide sequence of the HE gene and partial sequences of the other genes of C/Nara/1/85 with those of C/Nara/82 and C/Nara/2/85. The results suggest that C/Nara/1/85 has inherited HE and NP genes from a C/Nara/82-related virus and the PB2, PB1, PA, M and NS genes from a C/Nara/2/85-related virus.
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PMID:Genetic reassortment of influenza C viruses in man. 799 55