scholarly journals Mutations Affecting the Sensitivity of the Influenza Virus Neuraminidase to 4-Guanidino-2,4-dideoxy-2,3-dehydro-N-acetylneuraminic Acid

Virology ◽  
1997 ◽  
Vol 238 (2) ◽  
pp. 265-272 ◽  
Author(s):  
Hideo Goto ◽  
Richard C Bethell ◽  
Yoshihiro Kawaoka
Keyword(s):  
Influenza Virus ◽  
Acetylneuraminic Acid ◽  
Influenza Virus Neuraminidase

scholarly journals Salmonella typhimurium neuraminidase acts with inversion of configuration

1993 ◽  
Vol 296 (2) ◽  
pp. 291-292 ◽  
Author(s):  
X Guo ◽  
M L Sinnott
Keyword(s):  
Influenza Virus ◽  
Salmonella Typhimurium ◽  
Mode Of Action ◽  
Time Course ◽  
Optical Rotation ◽  
Acetylneuraminic Acid ◽  
Displacement Mode ◽  
Absorbance Change ◽  
Influenza Virus Neuraminidase ◽  
Hydrolysis Of

When the time course of the hydrolysis of identical solutions of p-nitrophenyl N-acetyl-alpha-D-neuraminide by Salmonella typhimurium neuraminidase is monitored by u.v. and by its optical rotation, the rotation change is synchronous with, or even marginally in advance of, the absorbance change. In experiments under the same conditions with influenza-virus neuraminidase, known to react with retention of configuration [Chong, Pegg, Taylor and von Itzstein (1992) Eur. J. Biochem. 207, 335-343], the rotation change is much slower than the absorbance change. The inverting, presumably single-displacement, mode of action of the S. typhimurium enzyme follows from these observations, and the position (92.5% beta) of the slowly established mutarotational equilibrium of N-acetylneuraminic acid [Friebolin, Kunzelmann, Supp, Brossmer, Keilich and Ziegler (1981) Tetrahedron Lett. 22, 1383-1386].

scholarly journals Novel α- and β-Amino Acid Inhibitors of Influenza Virus Neuraminidase

2001 ◽  
Vol 45 (9) ◽  
pp. 2563-2570 ◽  
Author(s):  
Warren M. Kati ◽  
Debra Montgomery ◽  
Clarence Maring ◽  
Vincent S. Stoll ◽  
Vincent Giranda ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Neuraminidase Inhibitor ◽  
Hydroxyl Group ◽  
Hydroxyl Groups ◽  
Side Chains ◽  
Amino Group ◽  
Amino Groups ◽  
Acetylneuraminic Acid ◽  
Cell Culture Assay ◽  
Influenza Virus Neuraminidase

ABSTRACT In an effort to discover novel, noncarbohydrate inhibitors of influenza virus neuraminidase we hypothesized that compounds which contain positively charged amino groups in an appropriate position to interact with the Asp 152 or Tyr 406 side chains might be bound tightly by the enzyme. Testing of 300 α- and β-amino acids led to the discovery of two novel neuraminidase inhibitors, a phenylglycine and a pyrrolidine, which exhibited K i values in the 50 μM range versus influenza virus A/N2/Tokyo/3/67 neuraminidase but which exhibited weaker activity against influenza virus B/Memphis/3/89 neuraminidase. Limited optimization of the pyrrolidine series resulted in a compound which was about 24-fold more potent than 2-deoxy-2,3-dehydro-N-acetylneuraminic acid in an anti-influenza cell culture assay using A/N2/Victoria/3/75 virus. X-ray structural studies of A/N9 neuraminidase-inhibitor complexes revealed that both classes of inhibitors induced the Glu 278 side chain to undergo a small conformational change, but these compounds did not show time-dependent inhibition. Crystallography also established that the α-amino group of the phenylglycine formed hydrogen bonds to the Asp 152 carboxylate as expected. Likewise, the β-amino group of the pyrrolidine forms an interaction with the Tyr 406 hydroxyl group and represents the first compound known to make an interaction with this absolutely conserved residue. Phenylglycine and pyrrolidine analogs in which the α- or β-amino groups were replaced with hydroxyl groups were 365- and 2,600-fold weaker inhibitors, respectively. These results underscore the importance of the amino group interactions with the Asp 152 and Tyr 406 side chains and have implications for anti-influenza drug design.

scholarly journals Synthesis of novel N-acetylneuraminic acid derivatives as substrates for rapid detection of influenza virus neuraminidase

2012 ◽  
Vol 359 ◽  
pp. 92-96 ◽  
Author(s):  
Wei Yang ◽  
Xiaoyu Liu ◽  
Xiaoxia Peng ◽  
Pei Li ◽  
Tianxin Wang ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Rapid Detection ◽  
Acetylneuraminic Acid ◽  
Influenza Virus Neuraminidase

scholarly journals A cell-free assay for the insertion of a viral glycoprotein into the plasma membrane.

1986 ◽  
Vol 103 (5) ◽  
pp. 1829-1835 ◽  
Author(s):  
P G Woodman ◽  
J M Edwardson
Keyword(s):  
Influenza Virus ◽  
Plasma Membrane ◽  
Trichloroacetic Acid ◽  
Plasma Membranes ◽  
Semliki Forest Virus ◽  
Fusion Reaction ◽  
Viral Glycoprotein ◽  
Acetylneuraminic Acid ◽  
Donor And Acceptor ◽  
A Cell

A cell-free assay has been developed for the delivery of influenza virus neuraminidase to the plasma membrane. Two types of postnuclear supernatant, which acted as donor and acceptor of the enzyme, were prepared from baby hamster kidney cells. Donor preparations were obtained from cells infected with influenza virus and containing neuraminidase en route to the plasma membrane. Acceptor preparations were obtained from cells containing, bound to their plasma membranes, Semliki Forest virus with envelope glycoproteins bearing [3H]N-acetylneuraminic acid. Fusion between vesicles from these two preparations permits access of the enzyme to its substrate, which results in the release of free [3H]N-acetylneuraminic acid. This release was detected through the transfer of radioactivity from a trichloroacetic acid-insoluble to a trichloroacetic acid-soluble fraction. An ATP-dependent component of release was found, which appears to be a consequence of vesicle fusion. This component was enhanced when the donor was prepared from cells in which the enzyme had been concentrated in a compartment between the Golgi complex and the plasma membrane, which indicates that a specific exocytic fusion event has been reconstituted. The extent of fusion is greatly reduced by pre-treatment of donor and acceptor preparations with trypsin, which points to the involvement of proteins in the fusion reaction.

Docking and 3D QSAR study of thiourea analogs as potent inhibitors of influenza virus neuraminidase

2010 ◽  
Vol 16 (12) ◽  
pp. 1809-1818 ◽  
Author(s):  
Jiaying Sun ◽  
Shaoxi Cai ◽  
Hu Mei ◽  
Jian Li ◽  
Ning Yan ◽  
...  
Keyword(s):  
Influenza Virus ◽  
3D Qsar ◽  
Qsar Study ◽  
Influenza Virus Neuraminidase

Influenza Virus Neuraminidase Inhibitory Activity of Phlorotannins from the Edible Brown AlgaEcklonia cava

2011 ◽  
Vol 59 (12) ◽  
pp. 6467-6473 ◽  
Author(s):  
Young Bae Ryu ◽  
Hyung Jae Jeong ◽  
So Young Yoon ◽  
Ji-Young Park ◽  
Young Min Kim ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Inhibitory Activity ◽  
Influenza Virus Neuraminidase

Difluorosialic acids, potent novel influenza virus neuraminidase inhibitors, induce fewer drug resistance-associated neuraminidase mutations than does oseltamivir

2015 ◽  
Vol 210 ◽  
pp. 126-132 ◽  
Author(s):  
S.-H. Sheldon Tai ◽  
Olga Agafitei ◽  
Zhizeng Gao ◽  
Richard Liggins ◽  
Martin Petric ◽  
...  
Keyword(s):  
Drug Resistance ◽  
Influenza Virus ◽  
Neuraminidase Inhibitors ◽  
Influenza Virus Neuraminidase

scholarly journals Induced opening of influenza virus neuraminidase N2 150-loop suggests an important role in inhibitor binding

2013 ◽  
Vol 3 (1) ◽  
Author(s):  
Yan Wu ◽  
Guangrong Qin ◽  
Feng Gao ◽  
Yue Liu ◽  
Christopher J. Vavricka ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Inhibitor Binding ◽  
Influenza Virus Neuraminidase
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