Perspectives in Drug Discovery and Design

, Volume 6, Issue 1, pp 64–86

Viral cysteine proteinases

  • Alexander E. Gorbalenya
  • Eric J. Snijder

DOI: 10.1007/BF02174046

Cite this article as:
Gorbalenya, A.E. & Snijder, E.J. Perspectives in Drug Discovery and Design (1996) 6: 64. doi:10.1007/BF02174046


Dozens of novel cysteine proteinases have been identified in positive single-stranded RNA viruses and, for the first time, in large double-stranded DNA viruses. The majority of these proteins are distantly related to papain or chymotrypsin and may be direct descendants of primordial proteolytic enzymes. Virus genome synthesis and expression, virion formation, virion entry into the host cell, as well as cellular architecture and functioning can be under the control of viral cysteine proteinases during infection. RNA virus proteinases mediate their liberation from giant multidomain precursors in which they tend to occupy conserved positions. These proteinases possess a narrow substrate specificity, can cleave in cis and in trans, and may also have additional, nonproteolytic functions. The mechanisms of catalysis, substrate recognition and RNA binding were highlighted by the recent analysis of the three-dimensional structure of the chymotrypsin-like cysteine proteinases of two RNA viruses.

Copyright information

© ESCOM Science Publishers B.V 1996

Authors and Affiliations

  • Alexander E. Gorbalenya
    • 1
    • 2
  • Eric J. Snijder
    • 3
  1. 1.M.P. Chumakov Institute of Poliomyelitis and Viral EncephalitidesRussian Academy of Medical SciencesMoscow Region
  2. 2.A.N. Belozersky Institute of Physico-Chemical BiologyMoscow State UniversityMoscowRussia
  3. 3.Department of Virology, Institute of Medical MicrobiologyLeiden UniversityLeidenThe Netherlands