VSV-G

Last update 08 May 2025

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100 Clinical Results associated with VSV-G

100 Translational Medicine associated with VSV-G

0 Patents (Medical) associated with VSV-G

464

Literatures (Medical) associated with VSV-G

01 Apr 2025·Journal of General Virology

Myosin IXB protects immune cells from virus infection

Article

Author: Camargo, Felippe E. C. ; Forti, Fábio Luis ; da S. Souza, Kamilla B. ; Matozo, Taís ; Kogachi, Leticia ; de Alencar, Bruna Cunha ; Magalhães, Yuli Thamires ; Janoni Bayerlein, Marina ; Braga, Tania Carolina

Actin-associated proteins have been implicated in several stages of virus infection. However, the role of myosins, which are actin-dependent molecular motors, during virus infection and pathogenesis is poorly understood. Myosin IXB (Myo9b) is a member of the myosin family abundantly expressed in immune cells. Myo9b displays a RhoGTPase-activating protein domain capable of modulating actin dynamics by inhibiting RhoGTPase activity. To enquire upon Myo9b participation in virus infections, we have silenced Myo9b in U937 and Jurkat cells and infected them with vesicular stomatitis virus glycoprotein (VSV-G)-pseudotyped HIV-1. Myo9b-silenced U937 showed a remarkable increase of above ten times more HIV-VSV-G infection than control cells. We observed a similar pattern in Jurkat cell infection with both WT Env and VSV-G-pseudotyped HIV, albeit to a lesser extent. Myo9b-silenced U937 cells presented elevated levels of phosphorylated cofilin, but lower levels of polymerized actin. The use of a RhoA, B and C inhibitor, as well as a Rac1 inhibitor, reduced virus infection. Finally, we have also observed an increment in virus internalization and fusion in cells knockdown for Myo9b, which may explain the increase in virus infection. Taken together, our data suggests that Myo9b might hinder viral entry and infection by controlling the activity of RhoGTPases in immune cells.

01 Apr 2025·Advanced Healthcare Materials

pH‐Responsive Engineered Exosomes Enhance Endogenous Hyaluronan Production by Reprogramming Chondrocytes for Cartilage Repair

Article

Author: Wang, Yifan ; Lan, Ziyang ; Zhang, Xin ; Liu, Xulong ; Wang, Jianglin ; Zhong, Zhenyu ; Wu, Xiaodan ; Du, Yingying ; Li, Jiaqi ; Zhang, Shengmin ; Tian, Yaping ; Zhang, Bin ; Wang, Jianwei ; Tao, Weiyong

AbstractTrauma or inflammation‐caused cartilage injury leads to joint dysfunction and pain. Exogenous hyaluronic acid (HA) injection is a well‐established treatment, but it has a short duration in vivo and requires multiple injections. Here, a new strategy for in situ reprogramming chondrocytes to continuously produce endogenous high molecular weight HA is developed. This involves a pH‐responsive engineered exosome decorated with vesicular stomatitis virus glycoprotein (VSV‐G) and hyaluronan synthase type 2 (HAS2). Such engineered exosomes successfully deliver HAS2 to the chondrocyte membranes via VSV‐G‐mediated membrane fusion triggered by low pH, rather than being degraded in lysosomes. This results in the generation of HAS2‐chondrocytes, which are characterized to produce high molecular weight HA in vitro and in vivo. With increased endogenous HA, the injected engineered exosomes enhance cartilage regeneration and inhibit osteoarthritis (OA) progression. Notably, one‐shot administration of engineered exosomes drastically increases the intra‐articular concentration of high molecular weight HA to 145% of the exogenous HA injection group. Importantly, such endogenous HA is sustained for 4 weeks, whereas the injected exogenous HA rapidly decreases within 2 weeks. The findings demonstrate that pH‐responsive engineered exosomes capable of generating endogenous HA hold great potential to replace the treatment of multiple injections of exogenous HA for cartilage repair.

01 Mar 2025·Biochemical and Biophysical Research Communications

Development and application of a high-titer VSV-based HCoV-NL63 pseudovirus system via C-terminal 14 amino acid truncation of spike

Article

Author: Zhang, Xin ; Wang, Ming-Ming ; Li, Tian ; Wang, Sheng-Qi ; Wang, Xue-Jun ; Shao, Li-Ting ; Li, Wei-Guo ; Wang, Fei ; Wang, Yi-Ming ; Xin, Jie-Rong

To provide efficient tools for the development of novel antiviral drugs and vaccines of HCoV-NL63, it is urgently necessary to establish a safe, widely applicable, and high-titer NL63 pseudotyped particles (NL63pp) production system. In this research, we conducted a comparative analysis of several NL63pps, each with a truncated spike (S) protein missing part of its C-terminal amino acids. We discovered that deleting the C-terminal 14 amino acid sequence of the S protein (D14) led to a remarkable approximately 10-fold increase in the infection titer of VSV-based NL63pp. This value is higher than the titers of NL63pp packaged with S proteins having deletions of 18 or 24 amino acids at the C-terminus. Moreover, adding the VSV-G tag to the D14 C-terminus (D14V) resulted in an additional 30 % increase. We then constructed the recent prevalent HCoV-NL63 subgenotype C3 dual-reporter pseudovirus system C3-D14V, and found that C3-D14V had a higher infection efficiency. Utilizing this system, we investigated the susceptibility of several cell lines and observed that cells derived from liver (Huh7.5.1), small intestine (Caco-2) and lung (Calu-3) exhibited higher susceptibility. Furthermore, we applied this system to assess several bis-benzylisoquinoline alkaloids, notably, Cepharanthine demonstrated the highest inhibitory efficiency against NL63pp infection with EC₅₀ 0.61 μM. In conclusion, we have identified that S protein with a 14 amino acids deletion at the C-terminus significantly enhances the infection titer of HCoV-NL63 pseudovirus and provides an efficient VSV-based HCoV-NL63 dual-reporter (mCherry and luciferase2) pseudovirus system for various applications such as drug screening and antibody development in the future.

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