These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Characterization of two recombination-complementation groups of Uukuniemi virus temperature-sensitive mutants.
    Author: Gahmberg N.
    Journal: J Gen Virol; 1984 Jun; 65 ( Pt 6)():1079-90. PubMed ID: 6726186.
    Abstract:
    With the aim of isolating temperature-sensitive (ts) mutants defective in virus maturation or glycoprotein transport, Uukuniemi virus, a bunyavirus, was mutagenized with N-methyl-N'-nitro-N-nitrosoguanidine. Out of 13 initial clones unable to grow at 39 degrees C (non-permissive temperature), five mutants which grew to titres above 10(7) p.f.u./ml at 32 degrees C (permissive temperature) were selected for further studies. The mutants fell into two coinciding recombination-complementation groups. Three group I mutants ( ts7 , 8 and 12) and two group II mutants ( ts6 and 11) synthesized all three RNA segments and were able to form the corresponding nucleoproteins at 39 degrees C. Thus, members of these two recombination groups had a RNA-positive phenotype. All five mutants showed immunofluorescence when cells were stained at 39 degrees C using a double-staining technique employing monoclonal antibodies against the glycoproteins G1 or G2, and polyclonal antibodies against the nucleoprotein, N. We have previously shown that in cells infected with wild-type virus both the G1/G2 and the N proteins accumulate in the Golgi complex, the site of virus maturation. In cells infected with ts12 , accumulation of G1 and G2, but not N protein, was observed in the Golgi complex at 39 degrees C. The N protein was found evenly scattered in the cytoplasm, suggesting lack of interaction between the G1/G2 and N proteins. With ts6 and 11, G1 and G2 appeared to accumulate and aggregate in the endoplasmic reticulum (ER) at 39 degrees C. The location of the N protein coincided with that of the aggregated glycoproteins, suggesting that the N protein interacted with G1/G2 already in the ER. Thus, these mutants may prove valuable tools in studying the mechanism of Uukuniemi virus maturation.
    [Abstract] [Full Text] [Related] [New Search]