Oligomeric Structure of Retroviral Envelope Glycoproteins

1990 ◽  
pp. 335-343
Author(s):  
David A. Einfeld ◽  
Eric Hunter
Keyword(s):  
Envelope Glycoproteins ◽  
Oligomeric Structure

Modified Envelope Glycoproteins to Retarget Retroviral Vectors

2003 ◽  
Vol 3 (5) ◽  
pp. 405-410 ◽  
Author(s):  
Catherine Haynes ◽  
Otto Erlwein ◽  
Barbara Schnierle
Keyword(s):  
Retroviral Vectors ◽  
Envelope Glycoproteins

Role of HIV-1 Envelope Glycoproteins Conformation and Accessory Proteins on ADCC Responses

2015 ◽  
Vol 14 (1) ◽  
pp. 9-23 ◽  
Author(s):  
Maxime Veillette ◽  
Jonathan Richard ◽  
Marzena Pazgier ◽  
George K. Lewis ◽  
Matthew S. Parsons ◽  
...  
Keyword(s):  
Envelope Glycoproteins ◽  
Accessory Proteins ◽  
Hiv 1

scholarly journals Heme Binding to HupZ with a C-Terminal Tag from Group A Streptococcus

Molecules ◽  
2021 ◽  
Vol 26 (3) ◽  
pp. 549
Author(s):  
Ephrahime S. Traore ◽  
Jiasong Li ◽  
Tapiwa Chiura ◽  
Jiafeng Geng ◽  
Ankita J. Sachla ◽  
...  
Keyword(s):  
Quaternary Structure ◽  
Group A Streptococcus ◽  
Heme Binding ◽  
Oligomeric Structure ◽  
Heme Degradation ◽  
Group A ◽  
Degradation Activity ◽  
Ferric Heme ◽  
Epr Signal ◽  
Utilization Pathway

HupZ is an expected heme degrading enzyme in the heme acquisition and utilization pathway in Group A Streptococcus. The isolated HupZ protein containing a C-terminal V5-His6 tag exhibits a weak heme degradation activity. Here, we revisited and characterized the HupZ-V5-His6 protein via biochemical, mutagenesis, protein quaternary structure, UV–vis, EPR, and resonance Raman spectroscopies. The results show that the ferric heme-protein complex did not display an expected ferric EPR signal and that heme binding to HupZ triggered the formation of higher oligomeric states. We found that heme binding to HupZ was an O2-dependent process. The single histidine residue in the HupZ sequence, His111, did not bind to the ferric heme, nor was it involved with the weak heme-degradation activity. Our results do not favor the heme oxygenase assignment because of the slow binding of heme and the newly discovered association of the weak heme degradation activity with the His6-tag. Altogether, the data suggest that the protein binds heme by its His6-tag, resulting in a heme-induced higher-order oligomeric structure and heme stacking. This work emphasizes the importance of considering exogenous tags when interpreting experimental observations during the study of heme utilization proteins.

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