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1.
Rev. bras. pesqui. méd. biol ; Braz. j. med. biol. res;38(6): 813-823, June 2005. ilus, tab
Article in English | LILACS | ID: lil-402669

ABSTRACT

Enveloped viruses always gain entry into the cytoplasm by fusion of their lipid envelope with a cell membrane. Some enveloped viruses fuse directly with the host cell plasma membrane after virus binding to the cell receptor. Other enveloped viruses enter the cells by the endocytic pathway, and fusion depends on the acidification of the endosomal compartment. In both cases, virus-induced membrane fusion is triggered by conformational changes in viral envelope glycoproteins. Two different classes of viral fusion proteins have been described on the basis of their molecular architecture. Several structural data permitted the elucidation of the mechanisms of membrane fusion mediated by class I and class II fusion proteins. In this article, we review a number of results obtained by our laboratory and by others that suggest that the mechanisms involved in rhabdovirus fusion are different from those used by the two well-studied classes of viral glycoproteins. We focus our discussion on the electrostatic nature of virus binding and interaction with membranes, especially through phosphatidylserine, and on the reversibility of the conformational changes of the rhabdovirus glycoprotein involved in fusion. Taken together, these data suggest the existence of a third class of fusion proteins and support the idea that new insights should emerge from studies of membrane fusion mediated by the G protein of rhabdoviruses. In particular, the elucidation of the three-dimensional structure of the G protein or even of the fusion peptide at different pH's might provide valuable information for understanding the fusion mechanism of this new class of fusion proteins.


Subject(s)
Animals , Humans , Glycoproteins/physiology , Membrane Fusion/physiology , Rhabdoviridae/physiology , Viral Fusion Proteins/physiology , GTP-Binding Proteins/physiology , Histidine/physiology , Membrane Glycoproteins/physiology , Phosphatidylserines/physiology
2.
J. pediatr. (Rio J.) ; J. pediatr. (Rio J.);56(5): 279-88, passim, 1984.
Article in Portuguese | LILACS | ID: lil-23071

ABSTRACT

Os autores apresentam 17 casos de complicacao de miningite bacteriana, avaliados atraves da tomografia axial computadorizada do encefalo, exaltando o valor e a importancia deste exame tanto na precisao diagnostica como na evolucao e criterio de cura. As complicacoes de meningite bacteriana mais frequentes foram: abscesso cerebral; colecao subdural; hidrocefalia e cerebrite


Subject(s)
Infant , Child, Preschool , Humans , Male , Female , Meningitis , Tomography, X-Ray Computed
3.
Rev. paul. med ; 100(2): 8-10, 1982.
Article in Portuguese | LILACS | ID: lil-10930

ABSTRACT

Foi estudada em caes a acao antiarritmica de metoclopramida (Plasil) em arritmias experimentais causadas por doses toxicas de desacetil-lanatosideo C e de digitoxina Foi realizada comparacao entre a metoclopramida e a fenil-hidantoina em arritmias causadas pela digitoxina. Os resultados mostram que a metoclopramida antagonizou com eficacia as arritmias causadas pelo desacetil-lanatosideo C e reverteu temporariamente, na maioria das experienicas, aquelas decorrentes da administracao de digitoxinas. Ja a definil-hidantoina nao exerceu acao antiarritmica na maioria dos caes estudados


Subject(s)
Animals , Dogs , Arrhythmias, Cardiac , Deslanoside , Digitoxin , Metoclopramide , Phenytoin
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