ABSTRACT
Vaccinia virus complement control protein (VCP) was one of the first viral molecules demonstrated to have a role in blocking complement and hence in the evasion of host defense. Structurally it is very similar to the human C4b-BP and the other members of complement control protein. Functionally it is most similar to the CR1 protein. VCP blocks both major pathways of complement activation. The crystal structure of VCP was determined a little over a year ago and it is the only known structure of an intact and complete complement control protein. In addition to binding complement, VCP also binds to heparin. These two binding abilities can take place simultaneously and contribute to its many function and to its potential use in several inflammatory diseases, e.g. Alzheimer's disease (AD), CNS injury, xenotransplantation, etc. making it a truly fascinating molecule and potential drug.
Subject(s)
Complement Activation , Complement Inactivator Proteins/chemistry , Complement System Proteins/physiology , Heparin/metabolism , Humans , Immune System/physiology , Protein Binding , Receptors, Complement 3b/metabolism , Vaccinia virus/metabolism , Viral Proteins/chemistryABSTRACT
As alteraçöes na saturaçäo de ácidos graxos de dexoito carbonos de cultura de células foram estudadas após a infecçäo com o vírus Vaccinia. O estudo por cromatografia líquido-gasosa mostrou que o vírus produz uma relativa diminuiçäo na saturaçäo dos ácidos graxos C18. Este efeito foi observado 2 horas após a infecçäo com alta multiplicidade de infecçäo. As alteraçöes nas propriedades de membrana de células hospedeiras causadas pela dessaturaçäo de ácidos graxos, säo discutidas em termos de efeito citopático e permeabilidade celular