Viral Vaccines

Schleiss, Mark R.

doi:10.1016/b978-0-12-818731-9.00225-1

Cited by 4 publications

(3 citation statements)

References 61 publications

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“…As such, GPs dictate host and cellular tropism, providing a direct link to viral emergence and pathogenesis. Viral GPs are also highly visible to the immune system and comprise the principal targets of neutralizing antibodies [1][2][3] . Consequently, these show high rates of evolution due to pressures of escaping host immunity [4][5][6] .…”

Section: Introductionmentioning

confidence: 99%

“…Consequently, these show high rates of evolution due to pressures of escaping host immunity [4][5][6] . Vaccines inducing immunity to viral GPs have proven effective in reducing disease burden for multiple viruses, highlighting their potential as therapeutic targets 1,3,7 . Hence, methods that facilitate the study of viral GP function can help illuminate basic processes of viral infection, evolution, or immunity and facilitate the development of novel therapies.…”

Section: Introductionmentioning

confidence: 99%

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An efficient plasmid-based system for the recovery of recombinant vesicular stomatitis virus encoding foreign glycoproteins

Marqués,

Andreu-Moreno,

Sanjuán

et al. 2023

Preprint

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Viral glycoproteins mediate entry into host cells, thereby dictating host range and pathogenesis. In addition, they constitute the principal target of neutralizing antibody responses, making them important antigens in vaccine development. Recombinant vesicular stomatitis virus (VSV) encoding foreign glycoproteins can provide a convenient and safe surrogate system to interrogate the function, evolution, and antigenicity of viral glycoproteins from viruses that are difficult to manipulate or those requiring high biosafety levels containment. However, the production of recombinant VSV can be technically challenging. In this work, we present an efficient and robust plasmid-based system for the production of recombinant VSV encoding foreign glycoproteins. We validate the system using glycoproteins from different viral families, including arenaviruses, coronaviruses, and hantaviruses and highlight their utility for studying the effects of mutations on viral fitness. Overall, the methods described herein can facilitate the study of both native as well as recombinant VSV encoding foreign glycoproteins and can serve as the basis for the production of VSV-based vaccines.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

An efficient plasmid-based system for the recovery of recombinant vesicular stomatitis virus encoding foreign glycoproteins

Marqués,

Andreu-Moreno,

Sanjuán

et al. 2023

Preprint

View full text Add to dashboard Cite

show abstract

mentioning

confidence: 99%

An efficient plasmid-based system for the recovery of recombinant vesicular stomatitis virus encoding foreign glycoproteins

Marqués,

Andreu-Moreno,

Sanjuán

et al. 2024

Sci Rep

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Viral glycoproteins mediate entry into host cells, thereby dictating host range and pathogenesis. In addition, they constitute the principal target of neutralizing antibody responses, making them important antigens in vaccine development. Recombinant vesicular stomatitis virus (VSV) encoding foreign glycoproteins can provide a convenient and safe surrogate system to interrogate the function, evolution, and antigenicity of viral glycoproteins from viruses that are difficult to manipulate or those requiring high biosafety level containment. However, the production of recombinant VSV can be technically challenging. In this work, we present an efficient and robust plasmid-based system for the production of recombinant VSV encoding foreign glycoproteins. We validate the system using glycoproteins from different viral families, including arenaviruses, coronaviruses, and hantaviruses, as well as highlight their utility for studying the effects of mutations on viral fitness. Overall, the methods described herein can facilitate the study of both native and recombinant VSV encoding foreign glycoproteins and can serve as the basis for the production of VSV-based vaccines.

show abstract