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R N Leamnson

Publications and source records attributed to R N Leamnson.

5 recordsLinked to original sources
PubMed1986

Nucleotide sequence comparison of the 3' regions of avian retroviruses NY203 and NTRE-2.

We have been characterizing molecular clones of two subgroup E avian retroviruses (NTRE-2 and NY203RAV-60) that produce different proliferative diseases after inoculation into susceptable K28 chickens. Both viruses arose by recombination between exogenous and endogenous viral genomes. To further characterize regions of these viruses that are important for the production of disease, we have determined the nucleotide sequence of a 1.2-kb EcoRI fragment extending from the carboxyl end of gp85 through 150 bases of the U3 region of the LTR. From the sequence data it is possible to precisely define one point where recombination occurred between PrRSV-B and RAV-0 to produce NTRE-2. We suggest a hypothesis, based on the core enhancer consensus sequence, for the higher incidence of disease when chickens are infected with viruses bearing the LTR of NY203RAV-60.

Animals↗
PubMed1977

Induction and biological properties of defective interfering particles of rabies virus.

A method for obtaining large quantities of defective interfering (DI) rabies virus particles that fulfill all the criteria delineated by Huang and Baltimore (1970) is described. The purified rabies DI virion was found to be much shorter (60 to 80 nm) than the complete virion (180 nm) and to have a viral genome of about half the size of normal rabies RNA but with all of the structural proteins of standard virions. Rabies DI virions were noninfectious for both cells in culture and for animals. As determined by in vitro and in vivo techniques, interference with the replication of standard virus was specific to rabies virus. The possible role of rabies DI virion in the pathogenicity of rabies virus infection and in the establishment of attenuated strains for use as live rabies vaccines is discussed.

Animals↗
PubMed1976

Subunit structure of the glycoprotein complex of avian tumor virus.

Envelope glycoprotein of avian tumor virus is linked by disulfide bonds in a structure that we have designated VGP to stand for viral glycoprotein. VGP appears to contain one molecule of gp85 and one of gp37. Under nonreducing conditions, VGP is the only glycoprotein component that is stable in the presence of ionic detergent, although in the presence of nonionic detergent two or more VGPs are associated in discrete complexes. The disulfide bonds linking viral glycoprotein are formed before release of virus from infected cells.

Animals↗