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The role of proteolytic processing in the morphogenesis of virus particles

Proteinases are encoded by many RNA viruses, all retroviruses and several DNA viruses. They play essential roles at various stages in viral replication, including the coordinated assembly and maturation of virions. Most of these enzymes belong to one of three (Ser, Cys or Asp) of the four major clas...

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Detalles Bibliográficos
Autores principales: Hellen, C. U. T., Wimmer, E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Birkhäuser-Verlag 1992
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7087542/
https://www.ncbi.nlm.nih.gov/pubmed/1740191
http://dx.doi.org/10.1007/BF01923512
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author Hellen, C. U. T.
Wimmer, E.
author_facet Hellen, C. U. T.
Wimmer, E.
author_sort Hellen, C. U. T.
collection PubMed
description Proteinases are encoded by many RNA viruses, all retroviruses and several DNA viruses. They play essential roles at various stages in viral replication, including the coordinated assembly and maturation of virions. Most of these enzymes belong to one of three (Ser, Cys or Asp) of the four major classes of proteinases, and have highly substrate-selective and cleavage specific activities. They can be thought of as playing one of two general roles in viral morphogenesis. Structural proteins are encoded by retroviruses and many RNA viruses as part of large polyproteins. Their proteolytic release is a prerequisite to particle assembly; consequent structural rearrangement of the capsid domains serves to regulate and direct association and assembly of capsid subunits. The second general role of proteolysis is in assembly-dependent maturation of virus particles, which is accompanied by the acquisition of infectivity.
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spelling pubmed-70875422020-03-23 The role of proteolytic processing in the morphogenesis of virus particles Hellen, C. U. T. Wimmer, E. Experientia Multi-Author Review Proteinases are encoded by many RNA viruses, all retroviruses and several DNA viruses. They play essential roles at various stages in viral replication, including the coordinated assembly and maturation of virions. Most of these enzymes belong to one of three (Ser, Cys or Asp) of the four major classes of proteinases, and have highly substrate-selective and cleavage specific activities. They can be thought of as playing one of two general roles in viral morphogenesis. Structural proteins are encoded by retroviruses and many RNA viruses as part of large polyproteins. Their proteolytic release is a prerequisite to particle assembly; consequent structural rearrangement of the capsid domains serves to regulate and direct association and assembly of capsid subunits. The second general role of proteolysis is in assembly-dependent maturation of virus particles, which is accompanied by the acquisition of infectivity. Birkhäuser-Verlag 1992 /pmc/articles/PMC7087542/ /pubmed/1740191 http://dx.doi.org/10.1007/BF01923512 Text en © Birkhäuser Verlag 1992 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic.
spellingShingle Multi-Author Review
Hellen, C. U. T.
Wimmer, E.
The role of proteolytic processing in the morphogenesis of virus particles
title The role of proteolytic processing in the morphogenesis of virus particles
title_full The role of proteolytic processing in the morphogenesis of virus particles
title_fullStr The role of proteolytic processing in the morphogenesis of virus particles
title_full_unstemmed The role of proteolytic processing in the morphogenesis of virus particles
title_short The role of proteolytic processing in the morphogenesis of virus particles
title_sort role of proteolytic processing in the morphogenesis of virus particles
topic Multi-Author Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7087542/
https://www.ncbi.nlm.nih.gov/pubmed/1740191
http://dx.doi.org/10.1007/BF01923512
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