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Construction And Characterization Of A Chimeric Virus (Biv/Hiv-1) Carrying The Bovine Immunodeficiency Virus Gag-Pol Gene: Research Letters, Guomin Chen, Shuhui Wang, Kun Xiong, Jinzhong Wang, Tao Ye, Wenping Dong, Qi Wang, Qimin Chen, Yunqi Geng, Charles Wood, Yi Zeng Jan 2002

Construction And Characterization Of A Chimeric Virus (Biv/Hiv-1) Carrying The Bovine Immunodeficiency Virus Gag-Pol Gene: Research Letters, Guomin Chen, Shuhui Wang, Kun Xiong, Jinzhong Wang, Tao Ye, Wenping Dong, Qi Wang, Qimin Chen, Yunqi Geng, Charles Wood, Yi Zeng

Nebraska Center for Virology: Faculty Publications

HIV-1HXB2 5′LTR region, most of BIVR29 gag-pol segment and HIV-1HXB2 pol IN-3′LTR region were respectively amplified. A chimeric clone, designated as pHBIV3753, was constructed by cloning three fragments sequentially into pUC18. MT4 cells were transfected with pHBIV3753. The replication and expressions of the chimeric virus (HBIV3753) were monitored by RT activity and IFA. The results firstly demonstrated that it is possible to generate a new type of the BIV/HIV-1 chimeric virus containing BIV gag-pol gene.


Small Glutamine-Rich Protein/Viral Protein U–Binding Protein Is A Novel Cochaperone That Affects Heat Shock Protein 70 Activity, Peter C. Angeletti, Doriann Walker, Antonito T. Panganiban Jan 2002

Small Glutamine-Rich Protein/Viral Protein U–Binding Protein Is A Novel Cochaperone That Affects Heat Shock Protein 70 Activity, Peter C. Angeletti, Doriann Walker, Antonito T. Panganiban

Nebraska Center for Virology: Faculty Publications

Molecular chaperone complexes containing heat shock protein (Hsp) 70 and Hsp90 are regulated by cochaperones, including a subclass of regulators, such as Hsp70 interacting protein (Hip), C-terminus of Hsp70 interacting protein (CHIP), and Hsp70-Hsp90 organizing factor (Hop), that contain tetratricopeptide repeats (TPRs), where Hsp70 refers to Hsp70 and its nearly identical constitutive counterpart, Hsc70, together. These proteins interact with the Hsp70 to regulate adenosine triphosphatase (ATPase) and folding activities or to generate the chaperone complex. Here we provide evidence that small glutamine-rich protein/viral protein U–binding protein (SGT/UBP) is a cochaperone that negatively regulates Hsp70. By “Far-Western” and pull-down assays, SGT/UBP …