scholarly journals Rescue of Infectious Rotavirus Reassortants by a Reverse Genetics System Is Restricted by the Receptor-Binding Region of VP4

Viruses ◽  
2021 ◽  
Vol 13 (3) ◽  
pp. 363
Author(s):  
Alexander Falkenhagen ◽  
Marno Huyzers ◽  
Alberdina A. van Dijk ◽  
Reimar Johne
Keyword(s):  
Receptor Binding ◽  
Reverse Genetics ◽  
Genome Segment ◽  
Future Research ◽  
Binding Region ◽  
Virus Propagation ◽  
Virus Rescue ◽  
Plasmid Transfection ◽  
Strain Dependent ◽  
Receptor Binding Region

The rotavirus species A (RVA) capsid contains the spike protein VP4, which interacts with VP6 and VP7 and is involved in cellular receptor binding. The capsid encloses the genome consisting of eleven dsRNA segments. Reassortment events can result in novel strains with changed properties. Using a plasmid-based reverse genetics system based on simian RVA strain SA11, we previously showed that the rescue of viable reassortants containing a heterologous VP4-encoding genome segment was strain-dependent. In order to unravel the reasons for the reassortment restrictions, we designed here a series of plasmids encoding chimeric VP4s. Exchange of the VP4 domains interacting with VP6 and VP7 was not sufficient for rescue of viable viruses. In contrast, the exchange of fragments encoding the receptor-binding region of VP4 resulted in virus rescue. All parent strains and the rescued reassortants replicated efficiently in MA-104 cells used for virus propagation. In contrast, replication in BSR T7/5 cells used for plasmid transfection was only efficient for the SA11 strain, whereas the rescued reassortants replicated slowly, and the parent strains failing to produce reassortants did not replicate. While future research in this area is necessary, replication in BSR T7/5 cells may be one factor that affects the rescue of RVAs.

scholarly journals A Receptor-binding Region inEscherichia coliα-Haemolysin

2003 ◽  
Vol 278 (21) ◽  
pp. 19159-19163 ◽  
Author(s):  
Aitziber L. Cortajarena ◽  
Félix M. Goñi ◽  
Helena Ostolaza
Keyword(s):  
Receptor Binding ◽  
Binding Region ◽  
Receptor Binding Region

The Galactosyl Ceramide/Sulfatide Receptor Binding Region of HIV-1 gp120 Maps to Amino Acids 206-275

1993 ◽  
Vol 9 (2) ◽  
pp. 175-181 ◽  
Author(s):  
SHAMA BHAT ◽  
RICHARD V. METTUS ◽  
E. PREMKUMAR REDDY ◽  
K.E. UGEN ◽  
V. SRIKANTHAN ◽  
...  
Keyword(s):  
Amino Acids ◽  
Receptor Binding ◽  
Binding Region ◽  
Galactosyl Ceramide ◽  
Receptor Binding Region ◽  
Hiv 1

Characterization of a complex glucocorticoid response unit in the phosphoenolpyruvate carboxykinase gene

1990 ◽  
Vol 10 (9) ◽  
pp. 4712-4719
Author(s):  
E Imai ◽  
P E Stromstedt ◽  
P G Quinn ◽  
J Carlstedt-Duke ◽  
J A Gustafsson ◽  
...  
Keyword(s):  
Glucocorticoid Receptor ◽  
Receptor Binding ◽  
Phosphoenolpyruvate Carboxykinase ◽  
Binding Region ◽  
Factor Binding ◽  
Response Unit ◽  
Accessory Factor ◽  
Glucocorticoid Response ◽  
Glucocorticoid Induction ◽  
Receptor Binding Region

The minimal DNA sequence required for glucocorticoid induction of the phosphoenolpyruvate carboxykinase (PEPCK) gene in H4IIE rat hepatoma cells was defined. This novel glucocorticoid response unit (GRU) spans about 110 base pairs (bp) and includes two receptor-binding elements plus two accessory factor-binding elements. Purified glucocorticoid receptor bound to two regions (GR1 and GR2) between -395 and -349 bp relative to the transcription start site. Factors in crude rat liver nuclear extract bound to DNA in the regions -455 to -431 and -420 to -403 bp, which are designated accessory factor 1 (AF1) and accessory factor 2 (AF2) elements, respectively. Gel retardation analysis revealed that at least two proteins bound to AF1 and that they were distinct from the protein(s) that bound to AF2. Various combinations of GR1, GR2, AF1, and AF2 were fused to the chloramphenicol acetyltransferase (CAT) reporter gene and cotransfected with a glucocorticoid receptor expression plasmid (pSVGR1) into H4IIE cells to identify the functional GRU. Neither the glucocorticoid receptor binding region nor the accessory factor binding region alone was sufficient to confer glucocorticoid responsiveness. The two components of the glucocorticoid receptor binding region functioned independently, and each accounted for half of the maximal response, provided the accessory factor elements were present. Similarly, deletion of either AF1 or AF2 diminished glucocorticoid induction of the PEPCK gene to approximately half of the maximum. We propose that the complex PEPCK gene GRU provides the stringent regulation required of this critical enzyme in liver.

Rat relaxin: insulin-like fold predicts a likely receptor binding region

1982 ◽  
Vol 4 (7) ◽  
pp. 399-405 ◽  
Author(s):  
G.G. Dodson ◽  
E.E. Eliopoulos ◽  
N.W. Isaacs ◽  
M.J. McCall ◽  
H.D. Niall ◽  
...  
Keyword(s):  
Receptor Binding ◽  
Binding Region ◽  
Receptor Binding Region

Bioactivities and Secondary Structures of Constrained Analogues of Human Parathyroid Hormone:  Cyclic Lactams of the Receptor Binding Region†

1997 ◽  
Vol 40 (9) ◽  
pp. 1373-1380 ◽  
Author(s):  
Jean-René Barbier ◽  
Witold Neugebauer ◽  
Paul Morley ◽  
Virginia Ross ◽  
Mark Soska ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Receptor Binding ◽  
Secondary Structures ◽  
Human Parathyroid Hormone ◽  
Binding Region ◽  
Receptor Binding Region

Solution structure of a synthetic peptide corresponding to a receptor binding region of FSH (hFSH-β 33–53)

1992 ◽  
Vol 11 (5) ◽  
pp. 495-507 ◽  
Author(s):  
Paul F. Agris ◽  
Richard H. Guenther ◽  
Hanna Sierzputowska-Gracz ◽  
Laura Easter ◽  
Wanda Smith ◽  
...  
Keyword(s):  
Receptor Binding ◽  
Synthetic Peptide ◽  
Solution Structure ◽  
Binding Region ◽  
Receptor Binding Region
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