Resumo

ACOSTA L, Orlando; CALDERON, Martha N; MORENO, Liz P  e  GUERRERO, Carlos A. A model for the mechanism of entry of rotaviruses into the host cell. rev.fac.med. [online]. 2009, vol.57, n.2, pp.114-148. ISSN 0120-0011.

Background. Rotavirus infection is the leading single cause of severe acute gastroenteritis in children under five years of age. The outermost layer of the triple-layered protein capsid of the non-enveloped virus particle has been involved in initial interactions between virus and host cell surface. The rotavirus mechanism for cell attachment and entry seems to be a multistep process in which outermost layer virus proteins VP4 and VP7 interact with different cell surface molecules. Objective. To propose a mechanism for rotavirus entry to the host cell incorporating the protein disulfide isomerase (PDI) activity. Materials and methods. A systematic search for original and review literature published from 1990 to 2009 on rotavirus and cell surface molecules participating in virus entry process was conducted through the use of electronic Databases. The analysis of the published results emphasized the molecular and cellular bases of time and space interactions between virus proteins and cell surface attachment and receptor molecules. Results. We found molecular and cellular bases for incorporating PDI within a coherent mechanism involving sequential or alternative paths previous to virus penetration. A mechanism is proposed in which virus proteins VP4, VP6 and VP7, and cell surface sialico acid, integrins, Hsc70, and PDI interact as part of a caveola/ raft-mediated endocytic process that is characterized by its caveolin and clathrin independence, dynamin dependence, and sensitivity to cholesterol depletion. Conclusions. The rotavirus entry mechanism appears to be a complex multistep process in which the path using PDI could be a potential target for antiviral agents reacting with thiol/disulfide groups.

Palavras-chave : rotavirus; integrins; heat-shock cognate protein 70; disulfides; isomerases.

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