The Lister Strain of Vaccinia Virus as an Anticancer Therapeutic Agent

2014 ◽  
pp. 225-238
Author(s):  
Jahangir Ahmed ◽  
Ming Yuan ◽  
Ghassan Alusi ◽  
Nicholas R. Lemoine ◽  
Yaohe Wang
Immunotherapy ◽  
2015 ◽  
Vol 7 (12) ◽  
pp. 1249-1258 ◽  
Author(s):  
Chadwan Al Yaghchi ◽  
Zhongxian Zhang ◽  
Ghassan Alusi ◽  
Nicholas R Lemoine ◽  
Yaohe Wang

2008 ◽  
Vol 16 (4) ◽  
pp. 320-328 ◽  
Author(s):  
I Gentschev ◽  
J Stritzker ◽  
E Hofmann ◽  
S Weibel ◽  
Y A Yu ◽  
...  

2014 ◽  
Vol 21 (2) ◽  
pp. 405-416 ◽  
Author(s):  
Louisa S. Chard ◽  
Eleni Maniati ◽  
Pengju Wang ◽  
Zhongxian Zhang ◽  
Dongling Gao ◽  
...  

Marine Drugs ◽  
2019 ◽  
Vol 17 (6) ◽  
pp. 363 ◽  
Author(s):  
Tao Wu ◽  
Yulin Xiang ◽  
Tingting Liu ◽  
Xue Wang ◽  
Xiaoyuan Ren ◽  
...  

Lectins display a variety of biological functions including insecticidal, antimicrobial, as well as antitumor activities. In this report, a gene encoding Aphrocallistes vastus lectin (AVL), a C-type lectin, was inserted into an oncolytic vaccinia virus vector (oncoVV) to form a recombinant virus oncoVV-AVL, which showed significant in vitro antiproliferative activity in a variety of cancer cell lines. Further investigations revealed that oncoVV-AVL replicated faster than oncoVV significantly in cancer cells. Intracellular signaling elements including NF-κB2, NIK, as well as ERK were determined to be altered by oncoVV-AVL. Virus replication upregulated by AVL was completely dependent on ERK activity. Furthermore, in vivo studies showed that oncoVV-AVL elicited significant antitumor effect in colorectal cancer and liver cancer mouse models. Our study might provide insights into a novel way of the utilization of marine lectin AVL in oncolytic viral therapies.


2020 ◽  
Vol 134 (19) ◽  
pp. 2581-2595
Author(s):  
Qiuhong Li ◽  
Maria B. Grant ◽  
Elaine M. Richards ◽  
Mohan K. Raizada

Abstract The angiotensin-converting enzyme 2 (ACE2) has emerged as a critical regulator of the renin–angiotensin system (RAS), which plays important roles in cardiovascular homeostasis by regulating vascular tone, fluid and electrolyte balance. ACE2 functions as a carboxymonopeptidase hydrolyzing the cleavage of a single C-terminal residue from Angiotensin-II (Ang-II), the key peptide hormone of RAS, to form Angiotensin-(1-7) (Ang-(1-7)), which binds to the G-protein–coupled Mas receptor and activates signaling pathways that counteract the pathways activated by Ang-II. ACE2 is expressed in a variety of tissues and overwhelming evidence substantiates the beneficial effects of enhancing ACE2/Ang-(1-7)/Mas axis under many pathological conditions in these tissues in experimental models. This review will provide a succinct overview on current strategies to enhance ACE2 as therapeutic agent, and discuss limitations and future challenges. ACE2 also has other functions, such as acting as a co-factor for amino acid transport and being exploited by the severe acute respiratory syndrome coronaviruses (SARS-CoVs) as cellular entry receptor, the implications of these functions in development of ACE2-based therapeutics will also be discussed.


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