scholarly journals Effects of Basic Amino Acids and Their Derivatives on SARS-CoV-2 and Influenza-A Virus Infection

Viruses ◽  
2021 ◽  
Vol 13 (7) ◽  
pp. 1301
Author(s):  
Ivonne Melano ◽  
Li-Lan Kuo ◽  
Yan-Chung Lo ◽  
Po-Wei Sung ◽  
Ni Tien ◽  
...  
Keyword(s):  
Amino Acids ◽  
Virus Infection ◽  
Influenza A Virus ◽  
Influenza A ◽  
Enveloped Viruses ◽  
Virus Attachment ◽  
Basic Amino Acids ◽  
Ester Derivative ◽  
Endosomal Acidification

Amino acids have been implicated with virus infection and replication. Here, we demonstrate the effects of two basic amino acids, arginine and lysine, and their ester derivatives on infection of two enveloped viruses, SARS-CoV-2, and influenza A virus. We found that lysine and its ester derivative can efficiently block infection of both viruses in vitro. Furthermore, the arginine ester derivative caused a significant boost in virus infection. Studies on their mechanism of action revealed that the compounds potentially disturb virus uncoating rather than virus attachment and endosomal acidification. Our findings suggest that lysine supplementation and the reduction of arginine-rich food intake can be considered as prophylactic and therapeutic regimens against these viruses while also providing a paradigm for the development of broad-spectrum antivirals.

scholarly journals Influenza A Virus Infection Induces Apical Redistribution of Na+, K+-ATPase in Lung Epithelial Cells In Vitro and In Vivo

2019 ◽  
Vol 61 (3) ◽  
pp. 395-398
Author(s):  
Christin Peteranderl ◽  
Irina Kuznetsova ◽  
Jessica Schulze ◽  
Martin Hardt ◽  
Emilia Lecuona ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Virus Infection ◽  
Influenza A Virus ◽  
Influenza A ◽  
Lung Epithelial Cells ◽  
Lung Epithelial ◽  
Influenza A Virus Infection

scholarly journals Cross-Protection of Influenza A Virus Infection by a DNA Aptamer Targeting the PA Endonuclease Domain

2015 ◽  
Vol 59 (7) ◽  
pp. 4082-4093 ◽  
Author(s):  
Shuofeng Yuan ◽  
Naru Zhang ◽  
Kailash Singh ◽  
Huiping Shuai ◽  
Hin Chu ◽  
...  
Keyword(s):  
Virus Infection ◽  
Influenza A Virus ◽  
Influenza A ◽  
H5n1 Virus ◽  
Influenza Viruses ◽  
Cross Protection ◽  
Dna Aptamer ◽  
Endonuclease Activity ◽  
Endonuclease Domain

ABSTRACTAmino acid residues in the N-terminal of the PA subunit (PAN) of the influenza A virus polymerase play critical roles in endonuclease activity, protein stability, and viral RNA (vRNA) promoter binding. In addition, PANis highly conserved among different subtypes of influenza virus, which suggests PANto be a desired target in the development of anti-influenza agents. We selected DNA aptamers targeting the intact PA protein or the PANdomain of an H5N1 virus strain using systematic evolution of ligands by exponential enrichment (SELEX). The binding affinities of selected aptamers were measured, followed by an evaluation ofin vitroendonuclease inhibitory activity. Next, the antiviral effects of enriched aptamers against influenza A virus infections were examined. A total of three aptamers targeting PA and six aptamers targeting PANwere selected. Our data demonstrated that all three PA-selected aptamers neither inhibited endonuclease activity nor exhibited antiviral efficacy, whereas four of the six PAN-selected aptamers inhibited both endonuclease activity and H5N1 virus infection. Among the four effective aptamers, one exhibited cross-protection against infections of H1N1, H5N1, H7N7, and H7N9 influenza viruses, with a 50% inhibitory concentration (IC50) of around 10 nM. Notably, this aptamer was identified at the 5th round but disappeared after the 10th round of selection, suggesting that the identification and evaluation of aptamers at early rounds of selection may be highly helpful for screening effective aptamers. Overall, our study provides novel insights for screening and developing effective aptamers for use as anti-influenza drugs.

In Vitro Characterization of Influenza A Virus Attachment in the Upper and Lower Respiratory Tracts of Pigs

2012 ◽  
Vol 50 (4) ◽  
pp. 648-658 ◽  
Author(s):  
S. E. Detmer ◽  
M. R. Gramer ◽  
S. M. Goyal ◽  
M. Torremorell
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
Virus Attachment ◽  
In Vitro Characterization

scholarly journals Inhibitory Effects of Polycations on the Replication of Enveloped Viruses (HIV, HSV, CMV, RSV, Influenza A Virus and Togaviruses)in vitro

1991 ◽  
Vol 2 (4) ◽  
pp. 243-248 ◽  
Author(s):  
M. Hosoya ◽  
J. Neyts ◽  
N. Yamamoto ◽  
D. Schols ◽  
R. Smoeck ◽  
...  
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
Inhibitory Effects ◽  
Enveloped Viruses

Inhibition of Influenza A Virus Infection in Vitro by Saliphenylhalamide-Loaded Porous Silicon Nanoparticles

ACS Nano ◽  
2013 ◽  
Vol 7 (8) ◽  
pp. 6884-6893 ◽  
Author(s):  
Luis M. Bimbo ◽  
Oxana V. Denisova ◽  
Ermei Mäkilä ◽  
Martti Kaasalainen ◽  
Jef K. De Brabander ◽  
...  
Keyword(s):  
Porous Silicon ◽  
Virus Infection ◽  
Influenza A Virus ◽  
Influenza A ◽  
Silicon Nanoparticles ◽  
Porous Silicon Nanoparticles ◽  
Influenza A Virus Infection

Protective efficacy of in vitro synthesized, specific mRNA vaccines against influenza A virus infection

2012 ◽  
Vol 30 (12) ◽  
pp. 1210-1216 ◽  
Author(s):  
Benjamin Petsch ◽  
Margit Schnee ◽  
Annette B Vogel ◽  
Elke Lange ◽  
Bernd Hoffmann ◽  
...  
Keyword(s):  
Virus Infection ◽  
Influenza A Virus ◽  
Influenza A ◽  
Protective Efficacy ◽  
Influenza A Virus Infection ◽  
Specific Mrna

scholarly journals Role of neuromedin B and its receptor in the innate immune responses against influenza A virus infection in vitro and in vivo

2019 ◽  
Vol 50 (1) ◽  
Author(s):  
Guihong Yang ◽  
Huipeng Huang ◽  
Mengyao Tang ◽  
Zifeng Cai ◽  
Cuiqin Huang ◽  
...  
Keyword(s):  
Virus Infection ◽  
Influenza A Virus ◽  
Influenza A ◽  
A549 Cells ◽  
Virus Challenge ◽  
Neuromedin B ◽  
Influenza A Virus Infection

Abstract The peptide neuromedin B (NMB) and its receptor (NMBR) represent a system (NMB/NMBR) of neuromodulation. Here, it was demonstrated that the expression of NMBR in cells or murine lung tissues was clearly upregulated in response to H1N1/PR8 influenza A virus infection. Furthermore, the in vitro and in vivo activities of NMB/NMBR during PR8 infection were investigated. It was observed that A549 cells lacking endogenous NMBR were more susceptible to virus infection than control cells, as evidenced by the increased virus production in the cells. Interestingly, a significant decrease in IFN-α and increased IL-6 expression were observed in these cells. The role of this system in innate immunity against PR8 infection was probed by treating mice with NMB. The NMB-treated mice were less susceptible to virus challenge, as evidenced by increased survival, increased body weight, and decreased viral NP expression compared with the control animals. Additionally, the results showed that exogenous NMB not only enhanced IFN-α expression but also appeared to inhibit the expression of NP and IL-6 in PR8-infected cells and animals. As expected, opposing effects were observed in the NMBR antagonist-treated cells and mice, which further confirmed the effects of NMB. Together, these data suggest that NMB/NMBR may be an important component of the host defence against influenza A virus infection. Thus, these proteins may serve as promising candidates for the development of novel antiviral drugs.

scholarly journals Amino acids 473V and 598P of PB1 from an avian-origin influenza A virus contribute to polymerase activity, especially in mammalian cells

2012 ◽  
Vol 93 (3) ◽  
pp. 531-540 ◽  
Author(s):  
Chen Xu ◽  
Wei-Bin Hu ◽  
Ke Xu ◽  
Yun-Xia He ◽  
Tong-Yan Wang ◽  
...  
Keyword(s):  
Amino Acids ◽  
Influenza A Virus ◽  
Mammalian Cells ◽  
Influenza A ◽  
Polymerase Activity ◽  
Amino Acid Residues ◽  
Lower Growth ◽  
Efficient Replication ◽  
Avian Origin

It has been reported that the avian-origin influenza A virus PB1 protein (avian PB1) enhances influenza A virus polymerase activity in mammalian cells when it replaces the human-origin PB1 protein (human PB1). Characterization of the amino acid residues that contribute to this enhancement is needed. In this study, it was found that PB1 from an avian-origin influenza A virus [A/Cambodia/P0322095/2005, H5N1 (Cam)] could enhance the polymerase activity of an attenuated human isolated virus, A/WSN/33, carrying the PB2 K627E mutation (WSN627E) in vitro. Furthermore, 473V and 598P in the Cam PB1 were identified as the residues responsible for this enhanced activity. The results from recombinant virus experiments demonstrated the contribution of PB1 amino acids 473V and 598P to polymerase activity in mammalian cells and in mice. Interestingly, 473V is conserved in pH1N1 viruses from the 2009 pandemic. Substitution of 473V by leucine in pH1N1 PB1 led to a decreased viral polymerase activity and a lower growth rate in mammalian cells, suggesting that the PB1 473V also plays a role in maintaining efficient virus replication of the pH1N1 virus. Thus, it was concluded that two amino acids in avian-origin PB1, 473V and 598P, contribute to the polymerase activity of the H5N1 virus, especially in mammalian cells, and that 473V in PB1 also contributes to efficient replication of the pH1N1 strain.

Influenza A Virus Infection of Human Schwann Cells In Vitro

2003 ◽  
Vol 123 (1) ◽  
pp. 41-45 ◽  
Author(s):  
Joshua Levine ◽  
Craig A. Buchman ◽  
Nevis Fregien
Keyword(s):  
Virus Infection ◽  
Schwann Cells ◽  
Influenza A Virus ◽  
Influenza A ◽  
Influenza A Virus Infection
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