title: Membrane dynamics and interactions in measles virus dendritic cell infections.
abstract: Viral entry, compartmentalization and transmission depend on the formation of membrane lipid/protein microdomains concentrating receptors and signalosomes. Dendritic cells (DCs) are prime targets for measles virus (MV) infection, and this interaction promotes immune activation and generalized immunosuppression, yet also MV transport to secondary lymphatics where transmission to T cells occurs. In addition to MV trapping, DC-SIGN interaction can enhance MV uptake by activating cellular sphingomyelinases and, thereby, vertical surface transport of its entry receptor CD150. To exploit DCs as Trojan horses for transport, MV promotes DC maturation accompanied by mobilization, and restrictions of viral replication in these cells may support this process. MV-infected DCs are unable to support formation of functional immune synapses with conjugating T cells and signalling via viral glycoproteins or repulsive ligands (such as semaphorins) plays a key role in the induction of T-cell paralysis. In the absence of antigen recognition, MV transmission from infected DCs to T cells most likely involves formation of polyconjugates which concentrate viral structural proteins, viral receptors and with components enhancing either viral uptake or conjugate stability. Because DCs barely support production of infectious MV particles, these organized interfaces are likely to represent virological synapses essential for MV transmission.
authors.affiliation: Institute for Virology and Immunobiology, University of Wuerzburg, Versbacher Str. 7, 97878 Wuerzburg, Germany.
authors.forename: Elita
authors.initials: E
authors.lastname: Avota
authors.forename: Susanne
authors.initials: S
authors.lastname: Koethe
authors.forename: Sibylle
authors.initials: S
authors.lastname: Schneider-Schaulies
mesh_terms: D015703:Antigens, CD / Q000235:genetics / Q000378:metabolism; D015815:Cell Adhesion Molecules / Q000235:genetics / Q000378:metabolism; D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism* / Q000821:virology; D003713:Dendritic Cells / Q000276:immunology / Q000378:metabolism* / Q000821:virology; D005786:Gene Expression Regulation; D054884:Host-Pathogen Interactions; D006801:Humans; D037181:Lectins, C-Type / Q000235:genetics / Q000378:metabolism; D008457:Measles / Q000276:immunology / Q000378:metabolism* / Q000635:transmission / Q000821:virology; D008459:Measles virus / Q000276:immunology / Q000378:metabolism*; D011956:Receptors, Cell Surface / Q000235:genetics / Q000378:metabolism; D011991:Receptors, Virus / Q000235:genetics / Q000378:metabolism; D015398:Signal Transduction; D000071177:Signaling Lymphocytic Activation Molecule Family Member 1; D013108:Sphingomyelin Phosphodiesterase / Q000378:metabolism; D013601:T-Lymphocytes / Q000473:pathology / Q000821:virology; D015678:Viral Structural Proteins / Q000235:genetics / Q000378:metabolism; D014779:Virus Replication; D000099215:DC-Specific ICAM-3 Grabbing Nonintegrin
chemical_list: D015703:Antigens, CD; D015815:Cell Adhesion Molecules; D037181:Lectins, C-Type; D011956:Receptors, Cell Surface; D011991:Receptors, Virus; D000071177:Signaling Lymphocytic Activation Molecule Family Member 1; D013108:Sphingomyelin Phosphodiesterase; D015678:Viral Structural Proteins; D000099215:DC-Specific ICAM-3 Grabbing Nonintegrin; C000604059:SLAMF1 protein, human