Structural basis of cell surface receptor recognition by botulinum neurotoxin B

Nature ◽  
2006 ◽  
Vol 444 (7122) ◽  
pp. 1096-1100 ◽  
Author(s):  
Qing Chai ◽  
Joseph W. Arndt ◽  
Min Dong ◽  
William H. Tepp ◽  
Eric A. Johnson ◽  
...  
Keyword(s):  
Cell Surface ◽  
Botulinum Neurotoxin ◽  
Cell Surface Receptor ◽  
Structural Basis ◽  
Receptor Recognition ◽  
Surface Receptor ◽  
Botulinum Neurotoxin B

Structural basis of Nipah and Hendra virus attachment to their cell-surface receptor ephrin-B2

2008 ◽  
Vol 15 (6) ◽  
pp. 567-572 ◽  
Author(s):  
Thomas A Bowden ◽  
A Radu Aricescu ◽  
Robert J C Gilbert ◽  
Jonathan M Grimes ◽  
E Yvonne Jones ◽  
...  
Keyword(s):  
Cell Surface ◽  
Hendra Virus ◽  
Cell Surface Receptor ◽  
Structural Basis ◽  
Virus Attachment ◽  
Surface Receptor

scholarly journals Structural basis for HCMV Pentamer recognition by antibodies and neuropilin 2

2021 ◽  
Author(s):  
Daniel Wrapp ◽  
Xiaohua Ye ◽  
Zhiqiang Ku ◽  
Hang Su ◽  
Harrison G Jones ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Cell Surface ◽  
Neutralizing Antibodies ◽  
Cell Surface Receptor ◽  
Structural Basis ◽  
Calcium Dependent ◽  
High Affinity ◽  
Molecular Determinants ◽  
Surface Receptor ◽  
Affinity Interaction

Human cytomegalovirus (HCMV) encodes for multiple surface glycoproteins and glycoprotein complexes. One of these complexes, the HCMV Pentamer (gH, gL, UL128, UL130 and UL131), mediates tropism to both epithelial and endothelial cells by interacting with the cell surface receptor neuropilin 2 (NRP2). Despite the critical nature of this interaction, the molecular determinants that govern NRP2 recognition remain unclear. Here we describe the cryo-EM structure of NRP2 bound to the HCMV Pentamer. The high-affinity interaction between these proteins is calcium-dependent and differs from the canonical C-terminal arginine (CendR) binding that NRP2 typically utilizes. The interaction is primarily mediated by NRP2 domains a2 and b2, which interact with UL128 and UL131. We also determine the structures of four human-derived neutralizing antibodies in complex with the HCMV Pentamer to define susceptible epitopes. The two most potent antibodies recognize a novel epitope yet do not compete with NRP2 binding. Collectively, these findings provide a structural basis for HCMV tropism and antibody-mediated neutralization, and serve as a guide for the development of HCMV treatments and vaccines.

Expression, function, and localization of the REG cell surface receptor

2001 ◽  
Vol 120 (5) ◽  
pp. A18-A19
Author(s):  
B DIECKGRAEFE ◽  
C HOUCHEN ◽  
H ZHANG
Keyword(s):  
Cell Surface ◽  
Cell Surface Receptor ◽  
Surface Receptor

Inhibition of rat ventricular automaticity by adenosine

1985 ◽  
Vol 248 (6) ◽  
pp. H907-H913 ◽  
Author(s):  
L. J. Heller ◽  
R. A. Olsson
Keyword(s):  
Cell Surface ◽  
Cell Surface Receptor ◽  
Chronotropic Effect ◽  
Surface Receptors ◽  
Adenosine Concentration ◽  
Surface Receptor ◽  
Ventricular Automaticity ◽  
Beating Rate ◽  
Chronotropic Effects ◽  
Developed Pressure

This study was designed to characterize adenosine's negative chronotropic effect on ventricular pacemakers. The spontaneous beating rate of isolated, isovolumic rat ventricular preparations perfused with Krebs-Henseleit solution decreased as the adenosine concentration was increased [log M effective concentration 50% (EC50) = -5.22 +/- 0.17]. The lack of effect of propranolol or atropine on this adenosine response eliminates the involvement of endogenous neurotransmitters. Support for the involvement of an external cell surface receptor was provided by findings that theophylline and 8-(4-sulfophenyl)theophylline, an analogue thought to act solely at the cell surface, significantly increased the adenosine log M EC50 to -3.94 +/- 0.22 and -3.61 +/- 0.22, respectively. An increase in spontaneous beating rate induced by theophylline, but not by its analogue, was blocked by the addition of propranolol. The relative chronotropic potency of the adenosine analogues R-PIA, S-PIA, and NECA suggests that the cell surface receptors may be of the Ri type. The negative chronotropic effects of adenosine and its analogues occurred at concentrations that had no effect on the developed pressure of the paced preparation. Electrocardiographic evaluations indicate that at high agonist concentrations, there was an abrupt alteration in electrical properties of the preparation, which could be blocked by theophylline and its analogue.

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