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Complement, viruses, and virus-infected cells

The attachment of specific antibody to viral glycoproteins and other structures on the surface of a virus or virus-infected cell has a number of potential consequences to the virus or virus-infected cell. Antibody is multivalent and thus able to redistribute or patch surface viral proteins or virus-...

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Detalles Bibliográficos
Autores principales: Cooper, Neil R., Nemerow, Glen R.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer-Verlag 1983
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7087538/
https://www.ncbi.nlm.nih.gov/pubmed/6364429
http://dx.doi.org/10.1007/BF02116278
Descripción
Sumario:The attachment of specific antibody to viral glycoproteins and other structures on the surface of a virus or virus-infected cell has a number of potential consequences to the virus or virus-infected cell. Antibody is multivalent and thus able to redistribute or patch surface viral proteins or virus-encoded structures within the lipid bilayer of the viral envelope or the cell membrane. In certain instances, antibody may agglutinate viruses or virus-infected cells. The physical presence of antibody molecules on the virus surface may interfere with the ability of the virus to infect potentially susceptible cells. Antibody on the surface of virus-infected cells may prevent the maturation and release of virus particles; antibody also can alter certain normal cell functions. The Fc portions of antibody molecules bound to virus-infected cells facilitate interactions with effector cells bearing Fc receptors. In the case of lymphocytes and perhaps phagocytic cells, this interaction may lead to antibody-dependent cellular cytotoxicity (ADCC) [51, 58]. The exposed Fc regions may also facilitate attempts at ingestion by monocytes, macrophages, and polymorphonuclear leukocytes.