Radioimmunoassay of Avian RNA Tumor Virus Group-Specific Antigen

Intervirology ◽  
1973 ◽  
Vol 1 (2) ◽  
pp. 119-126 ◽  
Author(s):  
Jukka Suni ◽  
Antti Vaheri ◽  
Erkki Ruoslahti
Virology ◽  
1966 ◽  
Vol 29 (3) ◽  
pp. 377-384 ◽  
Author(s):  
Gary Kelloff ◽  
Peter K. Vogt

Virology ◽  
1965 ◽  
Vol 27 (2) ◽  
pp. 233-236 ◽  
Author(s):  
Peter K. Vogt ◽  
Padman S. Sarma ◽  
Robert J. Huebner

Nature ◽  
1971 ◽  
Vol 233 (5315) ◽  
pp. 102-103 ◽  
Author(s):  
RAYMOND V. GILDEN ◽  
WADE P. PARKS ◽  
ROBERT J. HUEBNER ◽  
GEORGE J. TODARO

Virology ◽  
1972 ◽  
Vol 50 (1) ◽  
pp. 294-296 ◽  
Author(s):  
Stephen Oroszlan ◽  
Martin M.H. White ◽  
Raymond V. Gilden ◽  
Howard P. Charman
Keyword(s):  

Serological cross-reactions between influenza viruses of the two major types A and B and between the viruses and extracts of host tissue were investigated to elucidate the nature and source of the antigens concerned. The results render untenable the generally accepted view that virus types A and B are totally unrelated antigenically and that any cross-reactivity which occurs must be due to impurities in the virus preparations used. Strong cross-complement fixation reactions were consistently demonstrable with highly purified viruses provided that the antisera were prepared by immunizing rabbits with heat-degraded viruses in which the specific antigens had been destroyed. Cross-reactions between the viruses and chorio-allantoic membrane extracts showed that the virus-group antigens differed from the dominant membrane antigen which is of the Forssman type. The cross-reacting antigens of the two viruses were also found to be distinguishable from each other by their different responses to heat degradation. With the classical strains PR 8 and Lee propagated in embryonated eggs, the virus-group antigen could not be removed by successive cycles of virus purification. The method of purification was adsorption of virus on human group O red cells followed by spontaneous elution effected by the receptor-destroying enzyme of the virus. The ratio of specific antigen to group antigen remained constant through six successive purification cycles. It is suggested that the host-tissue component of the viruses is an integral part of their structure which may be essential for virus synthesis and may have some determinant function in respect of virus behaviour. The possibility of its fortuitous inclusion within the virus matrix without serving any biological purpose has not been excluded, but in such case its presence would point to a replication mechanism different from simple binary fission.


2007 ◽  
Vol 21 (9) ◽  
pp. 2071-2084 ◽  
Author(s):  
Cristina T. Kesler ◽  
Daniel Gioeli ◽  
Mark R. Conaway ◽  
Michael J. Weber ◽  
Bryce M. Paschal

Abstract Although the steady-state distribution of the androgen receptor (AR) is predominantly nuclear in androgen-treated cells, androgen-bound AR shuttles between the nucleus and the cytoplasm. In the present study we have addressed how nucleocytoplasmic shuttling contributes to the regulation of AR. Nuclear transport signal fusions were used to force AR localization to the nucleus or cytoplasm of prostate cancer cells, and the effect of localization on shuttling, transcription, androgen binding, and phosphorylation was determined. Fusing the simian virus 40 nuclear localization signal or c-Abl nuclear export signal to AR resulted in androgen-independent localization to the nucleus or cytoplasm, respectively. AR forced to the nucleus was transcriptionally active on prostate-specific antigen and mouse mammary tumor virus promoters driving reporter genes. AR forced to the cytoplasm was largely inactive on the prostate-specific antigen promoter, but, surprisingly, AR was active on the mouse mammary tumor virus promoter and on two endogenous genes examined. Thus, highly transient nuclear localization of AR is sufficient to activate transcription. Androgen dissociation rates and the dissociation constant (KD) of AR for androgen were similar whether AR was localized to the cytoplasm or the nucleus, suggesting the ligand-binding cycle of AR is not strictly linked to its compartmentalization. Using phosphosite antibodies, we found that compartmentalization influences the phosphorylation state of AR. We show there is a bias for androgen-dependent phosphorylation of Ser81, Ser256, and Ser308 in the nucleus and androgen-independent phosphorylation of Ser94 in the cytoplasm. We propose that one function of nucleocytoplasmic shuttling is to integrate the signaling environment in the cytoplasm with AR activity in the nucleus.


1973 ◽  
Vol 11 (6) ◽  
pp. 893-899 ◽  
Author(s):  
John R. Stephenson ◽  
Roger E. Wilsnack ◽  
Stuart A. Aaronson

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