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Biomedical subjects

R V Gilden

Publications and source records attributed to R V Gilden.

At least 37 records · Page 2Linked to original sources
PubMed1984

Serological analysis of a subgroup of human T-lymphotropic retroviruses (HTLV-III) associated with AIDS.

The two main subgroups of the family of human T-lymphotropic retroviruses (HTLV) that have previously been characterized are known as HTLV-I and HTLV-II. Both are associated with certain human leukemias and lymphomas. Cell surface antigens (p61 and p65) encoded by HTLV-I are frequently recognized, at low titers, by antibodies in the serum of patients with acquired immunodeficiency syndrome (AIDS) or with signs or symptoms that precede AIDS (pre-AIDS). This suggests an involvement of HTLV in these disorders. Another subgroup of HTLV, designated HTLV-III, has now been isolated from many patients with AIDS and pre-AIDS. In the studies described in this report, virus-associated antigens in T-cell clones permanently producing HTLV-III were subjected to biochemical and immunological analyses. Antigens of HTLV-III, specifically detected by antibodies in serum from AIDS or pre-AIDS patients and revealed by the Western blot technique, are similar in size to those found in other subgroups of HTLV. They include at least three serologically unrelated antigenic groups, one of which is associated with group-specific antigens (p55 and P24) and another with envelope-related (p65) proteins, while the antigens in the third group are of unknown affiliation. The data show that HTLV-III is clearly distinguishable from HTLV-I and HTLV-II but is also significantly related to both viruses. HTLV-III is thus a true member of the HTLV family.

Acquired Immunodeficiency Syndrome↗
PubMed1984

Simian AIDS: isolation of a type D retrovirus and transmission of the disease.

A type D retrovirus related to but distinct from Mason-Pfizer monkey virus was isolated in vitro from the blood of two rhesus monkeys (Macaca mulatta) with simian acquired immunodeficiency syndrome (SAIDS). Three juvenile rhesus monkeys that were injected intravenously with tissue culture fluids containing this virus developed SAIDS after 2 to 4 weeks.

Acquired Immunodeficiency Syndrome↗
PubMed1984

Nucleotide sequence analysis of the long terminal repeat of integrated bovine leukemia provirus DNA and of adjacent viral and host sequences.

The nucleotide sequence of the 3' long terminal repeat and adjacent viral and host sequences was determined for a bovine leukemia provirus cloned from a bovine tumor. The long terminal repeat was found to comprise 535 nucleotides and to harbor at both ends an imperfect inverted repeat of 7 bases. Promoter-like sequences (Hogness box and CAT box), an mRNA capping site, and a core enhancer-related sequence were tentatively located. No kinship was detected between this bovine leukemia proviral fragment and other retroviral long terminal repeats, including that of human T-cell leukemia virus.

Animals↗
PubMed1983

Nucleotide sequence of v-rel: the oncogene of reticuloendotheliosis virus.

The nucleotide sequence of v-rel, the oncogene carried by reticuloendotheliosis virus (REV), has been determined. The defective transforming genome REV arose through the insertion of v-rel (1,415 nucleotides) into the env gene of the helper virus REV-A. The predicted rel protein (503 amino acids) employs the REV-A env initiator and terminates within the p20E region of env. Because there are no natural antisera that detect the REV transforming protein, this nucleotide sequence provides the first step toward its isolation and characterization. The predicted protein is clearly distinct from all other reported transforming proteins but may be very distantly related to members of the src family.

Amino Acid Sequence↗
PubMed1983

Oncogenes.

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Animals↗
PubMed1982

Primary structure analysis of the major internal protein p24 of human type C T-cell leukemia virus.

A human type C retrovirus [human T-cell leukemia (lymphoma) virus; HTLV], recently isolated from young adult patients with cutaneous T-cell lymphoma or leukemia, was not detectably related to other known animal retroviruses in molecular hybridization studies, by comparison of reverse transcriptase and the major core protein p24. The p24 core protein was purified to homogeneity. The amino acid composition, the COOH-terminal amino acid, and the NH(2)-terminal amino acid sequence of the first 25 residues of this major internal structural protein were determined. These results were then compared to the known structure of the internal core protein of other retroviruses. The compositional data reveal that HTLV p24 is chemically distinct from p30-p24 of other animal retroviruses, in agreement with the earlier immunological analyses. However, HTLV p24 shares the common NH(2)-terminal proline and COOH-terminal leucine of all mammalian type C viral p30s. In addition, like bovine leukemia virus (BLV), HTLV lacks the common prolylleucylarginine tripeptide and the larger conserved region found near the NH(2) terminus of the other mammalian type C viral p30s. Alignment of the amino acid sequence of HTLV p24 with previously determined sequences of other retrovirus proteins, including BLV p24, reveals statistically significant sequence homology only to BLV. The results reported here demonstrate that HTLV p24 is related to but chemically distinct from the major core protein of other retroviruses. Similarly, previous results showed that there was no immunological crossreactivity of the p24 protein and reverse transcriptase of HTLV with other retroviruses, including BLV, and no nucleic acid sequence homology. However, the present results, combined with the common size of the p24 and reverse transcriptase, suggest that HTLV may be closer to BLV than any other known retrovirus.

Amino Acid Sequence↗
PubMed1982

Genome of reticuloendotheliosis virus: characterization by use of cloned proviral DNA.

Reticuloendotheliosis virus is an avian type C retrovirus that is capable of transforming fibroblasts and hematopoietic cells both in vivo and in vitro. This virus is highly related to the three other members of the reticuloendotheliosis virus group, including spleen necrosis virus, but it is apparently unrelated to the avian leukosis-sarcoma virus family. Previous studies have shown that it consists of a replication-competent helper virus (designated REV-A) and a defective component (designated REV) that is responsible for transformation. In this study we used restriction endonuclease mapping and heteroduplex analysis to characterize the proviral DNAs of REV-A and REV. Both producer and nonproducer transformed chicken spleen cells were used as sources of REV proviral DNA; this genome was mapped in detail, and fragments of it were cloned in lambdagtWES.lambdaB. The infected canine thymus line Cf2Th(REV-A) was used as a source of REV-A proviral DNA. The restriction maps and heteroduplexes of the REV and REV-A genomes showed that (proceeding from 5' to 3') (i) REV contains a large fraction of the REV-A gag gene (assuming a gene order of gag-pol-env and gene sizes similar to those of other type C viruses), for the two genomes are very similar over a distance of 2.1 kilobases beginning at their 5' termini; (ii) most or all of REV-A pol is deleted in REV; (iii) REV contains a 1.1 kilobase segment derived from the 3' end of REV-A pol or the 5' end of env or both; (iv) this env region in REV is followed by a 1.9-kilobase segment which is unrelated to REV-A; and (v) the helper-unrelated segment of REV extends essentially all of the way to the beginning of the 3' long terminal repeat. Therefore, like avian myeloblastosis virus but unlike the other avian acute leukemia viruses and most mammalian and avian sarcoma viruses, REV appears to be an env gene recombinant. We also found that the REV-specific segment is derived from avian DNA, for a cloned REV fragment was able to hybridize with the DNA from an uninfected chicken. Therefore, like the other acute transforming viruses, REV appears to be the product of recombination between a replication-competent virus and host DNA. Two other defective genomes in virus-producing chicken cells were also cloned and characterized. One was very similar to REV in its presumptive gag and env segments, but instead of a host-derived insertion it contained additional env sequences. The second was similar (but not identical) to the first in its gag and env regions and appeared to contain an additional 1-kilobase inversion of REV-A sequences.

Animals↗
PubMed1982

Molecular cloning, genomic analysis, and biological properties of rat leukemia virus and the onc sequences of Rasheed rat sarcoma virus.

Rasheed rat sarcoma virus (RaSV) has been shown to code for a protein of 29,000 Mr not present in replication-competent rat type C helper virus (RaLV)-infected cells. This protein is a fused gene product consisting of a portion of the RaLV p15 gag protein and the transformation-specific 21,000 Mr (p21) ras protein, which is also found in Harvey murine sarcoma virus. We now report the molecular cloning of both the SD-1 (Sprague-Dawley) strain of RaLV and the transforming ras sequences of RaSV. Heteroduplex analysis of these cloned DNAs demonstrated that the RaSV ras gene (v-Ra-ras) was inserted into the rat type C viral genome with a small deletion of RaLV genetic information in the 5' region of the gag gene and that the v-Ra-ras gene (0.72 kilobase pair) is homologous to and colinear with the p21 ras gene of Harvey murine sarcoma virus (v-Ha-ras). Restriction enzyme mapping confirmed the homology demonstrated by heteroduplex mapping, showing strong site conservation of restriction endonucleases known to cleave v-Ha-ras. Cloned v-Ra-ras DNA transformed NIH 3T3 cells, inducing the synthesis of the p29 RaSVgag-ras protein.

Base Sequence↗
PubMed1981

Baboon endogenous virus genome: molecular cloning and structural characterization of nondefective viral genomes from DNA of a baboon cell strain.

Several heterogeneities in the baboon endogenous virus (BaEV) genomes that are present in the DNA of normal baboon tissues and the baboon cell strain BEF-3 have been described previously. To study these genomes, we cloned BaEV proviruses from BEF-3 cellular DNA into the lambda vector Charon 4A. Of the four full-length clones isolated, one was nondefective as determined by transfection. The sequence of a portion of this clone was found to code for amino acids 61-91 in the p30 region of the gag gene. This identification allowed us to align the restriction map with the BaEV genetic map. One heterogeneity, a BamHI site 2.4 kilobases (kb) from the proviral 5' end, was located close to the gag-pol junction; another, a BamHI site 1.4 kb from the 5' end of the genome, corresponded to the gag p30 coding sequence for amino acids 32-34; and a third, a Xho I site, was near the 3' end of the pol gene. To select the nondefective BaEV genomes from BEF-3 cells, we infected permissive cells with virus produced by BEF-3 cells and also transfected BEF-3 cellular DNA into permissive cells. The BaEV genomes in the permissive recipient cultures were then analyzed by restriction enzyme analysis. These nondefective genomes were found to be heterogeneous with respect to the gag-pol BamHI site and the Xho I site, but all were found to contain the BamHI site 1.4 kb from the 5' end of the genome.

Animals↗
PubMed1981

Chemical and Immunological characterization of the major structural protein (p28) of MMC-1, a rhesus monkey endogenous type C virus: homology with the major structural protein of avian reticuloendotheliosis virus.

The major core protein (p28) of MMC-1, an endogenous type C virus of the rhesus monkey (Macaca mulatta), was purified and subjected to structural and immunological analyses. The NH2-terminal amino acid sequence of MMC-1 p28 showed extensive homology to the sequences of the major structural proteins (p30) of known mammalian type C viruses. Similarly, interspecies antigenic determinants shared by all the above viral proteins were detected in MMC-1 p28. Competition radioimmunoassays together with the results of statistical analysis of the primary structure data provided evidence that MMC-1 p28 is not more closely related to primate type C viruses of the Papio genus than to those isolated from rodents, cats, or New World monkeys. MMC-1 p28 was found to be closely related structurally to the p30 protein of the avian reticuloendotheliosis virus (REV-A), a horizontally transmitted type C virus of putative mammalian origin. In addition, MMC-1 p28 and REV-A p30 shared a specific subset of antigenic determinants not present in any of the other avian or mammalian type C viruses studied. These findings suggest that MMC-1 and REV may have a common evolutionary origin.

Amino Acid Sequence↗
PubMed1981

In vitro host range of equine infectious anemia virus.

Equine infectious anemia virus (EIAV) was successfully inoculated onto cell cultures of canine and feline origin, resulting in chronic infections in these cultures. Infection of equine cell cultures, which were the previous sole in vitro source demonstrated for virus production, was also performed for comparative purposes. Determination of the nature of the virus produced in the heterologous as well as the equine cells was accomplished in several ways. SDS-PAGE of purified virus from the different cell lines indicated very similar protein composition. Immunological identity was observed in gel diffusion tests employing an antiserum to the major core protein (p24) of equine-derived EIAV. Competition radioimmunoassays also indicated similar antigenicity in the viruses derived from the several cell lines. Strong relatedness was further demonstrated by hybridization of viral RNAs to EIAV complementary DNA. These data indicate that EIAV has an amphotropic cell culture host range and that the viruses isolated from the permissive lines were similar.

Animals↗
PubMed1980

The baboon endogenous virus genome. II. Provirus sequence variations in baboon cell DNA.

Restriction analysis of the approximately 100 integrated baboon endogenous virus (BaEV) proviruses in baboon cells and tissues has revealed two major sequence variations, both in the gag gene region of the genome. One, a 150 nucleotide pair insert, is present in a small proportion of the proviral DNAs and some baboons, but is present in the majority of the proviral DNAs of other baboons. The second, a Bam HI recognition sequence located 2.25 kb from the proviral 5' end, is missing or modified in approximately one-half of the integrated genomes. We consider the possibility that accumulation of proviruses not containing the 0.15 kb insert is correlated with viral activation and expression since it is this form that is a replication intermediate in freshly infected permissive cells. It is evident from these initial studies that the organization of the multiple BaEV proviruses in baboon DNA has undergone modification during evolution.

Animals↗