Isolation and characterization of a Chinese hamster ovary mutant cell line with altered sensitivity to vaccinia virus killing.

1996 ◽  
Vol 70 (7) ◽  
pp. 4655-4666 ◽  
Author(s):  
C H Bair ◽  
C S Chung ◽  
I A Vasilevskaya ◽  
W Chang
1981 ◽  
Vol 7 (5) ◽  
pp. 507-521 ◽  
Author(s):  
Michihiko Kuwano ◽  
Toshiko Tabuki ◽  
Shin-ichi Akiyama ◽  
Kumato Mifune ◽  
Akira Takatsuki ◽  
...  

2001 ◽  
Vol 69 (9) ◽  
pp. 5899-5904 ◽  
Author(s):  
Reynaldo A. Carabeo ◽  
Ted Hackstadt

ABSTRACT Host factors involved in Chlamydia trachomatispathogenesis were investigated by random chemical mutagenesis of Chinese hamster ovary (CHO-K1) cells followed by selection for clones resistant to chlamydial infection. A clonal mutant cell line, D4.1–3, refractory to infection by the C. trachomatis L2 serovar was isolated. The D4.1–3 cell line appears to be lacking in a previously undescribed temperature-dependent and heparin-resistant binding step that occurs subsequent to engagement of cell surface heparan sulfate by L2 elementary bodies. This novel binding step differentiates the lymphogranuloma venereum (LGV) serovar from other serovars and may contribute the different pathologies associated with LGV and non-LGV strains.


2002 ◽  
Vol 43 (8) ◽  
pp. 1341-1347 ◽  
Author(s):  
Jonathan C. Cruz ◽  
Matthew Thomas ◽  
Edmund Wong ◽  
Nobutaka Ohgami ◽  
Shigeki Sugii ◽  
...  

We report the chemical synthesis of a new photoactivatable cholesterol analog 7,7-azocholestanol (AC) and its linoleate ester (ACL). We also examined the biochemical properties of the sterol and its ester by employing several different mutant Chinese hamster ovary (CHO) cell lines with defined abnormalities in cholesterol metabolism as tools. AC mimics cholesterol in supporting the growth of a mutant cell line (M19) that requires cholesterol for growth. In normal cells, tritiated ACL present in low-density lipoprotein (LDL) was hydrolyzed and reesterified in a manner similar to tritiated cholesteryl linoleate (CL) in LDL. Also, in the mutant cell line (AC29) lacking the enzyme acyl-coenzyme A:cholesterol acyltransferase or in the mutant cell line (CT60) defective in the Niemann-Pick type C1 protein, the hydrolysis of ACL in LDL was normal, but the reesterification of the liberated AC was defective. Therefore, the metabolism of ACL in LDL is very similar to that of CL in LDL. Tritium-labeled AC delivered to intact CHO cells as a cyclodextrin complex was shown to photoaffinity label several discrete polypeptides, including caveolin-1.These results demonstrate AC as an effective reagent for studying cholesterol-protein interactions involved in intracellular cholesterol trafficking.


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