Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0038362 (stomatitis)
 8,852 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Armstrong, D. (The Children's Hospital of Philadelphia, Philadelphia, Pa.), and K. Paucker. Effect of mycoplasma on interferon production and interferon assay in cell cultures. J. Bacteriol. 92:97-101. 1966.-The influence of mycoplasma on the production and action of interferon was studied in cultures of both L and human embryonic kidney (HEK) cells. Mycoplasma hominis 1, the Negroni agent, and the F12 mycoplasma were used for infection of L cells, and M. hominis 1 and M. pneumoniae for inoculation of HEK cells. All strains were capable of multiplication in the culture systems employed. None produced detectable levels of interferon, and responsiveness of the cells to induction of interferon by virus remained unaltered. Infection with mycoplasma did not impair the sensitivity of the cells to the action of interferon, nor was the replication of vesicular stomatitis virus noticeably diminished.
 ...
PMID:Effect of mycoplasma on interferon production and interferon assay in cell cultures. 428 5

Murine cytomegalovirus (MCMV) does not productively infect OTT6050AF1 BrdU, F9, or PCC4 undifferentiated murine teratocarcinoma cell lines, as shown by immunofluorescence assays for viral antigens and by plaque assays for infectious virus. However, these cells were infected by a variety of other viruses. MCMV does productively infect PYS2 and OTT F12 differentiated murine teratocarcinoma cell lines. The replication of MCMV in the pluripotent PCC4 cell line was examined in detail. Undifferentiated PCC4 cells could be differentiated when propagated in the presence of dimethylacetamide, as judged by changes in the expression of H-2 antigens on the cell surface. Several viruses, including lymphocytic choriomeningitis virus, herpes simplex virus type 1, and vesicular stomatitis virus, replicated to a similar extent in differentiated and undifferentiated PCC4 cells. MCMV did productively infect differentiated PCC4 cells. In contrast, MCMV did not produce infectious virus, viral antigens, or substantial viral RNA in undifferentiated PCC4 cells. The molecular block of MCMV replication occurred at the level of MCMV RNA transcription. Undifferentiated PCC4 cells have receptors for MCMV and bind similar amounts of radiolabeled virus as differentiated PCC4 cells. After MCMV binds to its receptors on undifferentiated cells, MCMV penetrates the plasma membrane and is transported to the cells' nuclei. MCMV DNA was present in the cytoplasm, and small amounts of MCMV RNA (less than 17 percent of that found in MCMV-infected differentiated PCC4 cells) were found in the nucleus. However, MCMV RNA was not detected in the cytoplasm of undifferentiated cells. A latent infection was established by infecting undifferentiated PCC4 cells with MCMV, inactivating residual infectivity with antibodies to MCMV, and propagating cells under conditions that maintained the undifferentiated state. These MCMV-infected undifferentiated cells did not produce infectious virus, viral antigens, or viral RNA but did contain viral DNA detectable by DNA-DNA hybridization kinetics. Latency was terminated and infectious virus was made when such undifferentiated cells were induced to differentiate.
 ...
PMID:Cytomegalovirus causes a latent infection in undifferentiated cells and is activated by induction of cell differentiation. 627 94

Murine F9 and PCC4 teratoma cells do not express H-2 major transplantation antigens according to virus-specific T-lymphocyte cytotoxic or serological assays. However, such cells can be infected with and readily replicate many types of viruses (coxsackie B 3, mouse hepatitis, Sindbis, Semliki Forest [SFV], lymphocytic choriomeningitis, Pichinde, vesicular stomatitis, herpes simplex type 1) to the same extent as do murine F12 teratoma cells and mouse embryo fibroblasts, all of which express the H-2 determinants. In contrast, F9 and PCC4 cells are not productively infected with murine cytomegalovirus, whereas F12 and mouse embryo fibroblast cells are. In addition to replicating in H-2-negative murine teratoma cells, SFV replicates in H-2-negative murine lymphoblastoid cells. The ability of SFV to infect cells without H-2 antigens and then to effect viral antigenic expression in the cells' cytoplasm and on their surface with similar kinetics and in equivalent amounts as cells with H-2 antigens indicates that the H-2 receptor is not needed for SFV infection. Daudi cells, which lack HLA antigens, block the replication of SFV. This occurs at some point after receptor binding, as demonstrated by diminished viral mRNA. In addition, a possible membrane defect precludes viral exit in Daudi cells transfected with SFV infectious RNA. These results indicate that a cell's possession of H-2 antigens is not a requirement for SFV infection and that major histocompatibility complex antigens are not specific receptors for this virus.
 ...
PMID:Does the major histocompatibility complex serve as a specific receptor for Semliki Forest virus? 737 8

The extracellular form of vaccinia virus acquires its outer envelope by wrapping with cytoplasmic membranes that contain at least seven virus-encoded proteins, of which four are glycoproteins. We searched for interactions between the vaccinia virus A33 glycoprotein and proteins A34, A36, B5, F12, and F13. First, when myc epitope-tagged A33 was expressed in combination with other envelope proteins, A33 colocalized with B5 and A36, suggesting that direct A33-B5 and A33-A36 interactions occur in the absence of infection. A recombinant vaccinia virus (vA33Rmyc) was constructed by introduction of the myc-tagged A33 version (A33myc) into A33-deficient vaccinia virus. A33myc partially restored plaque formation and colocalized with enveloped virions in infected cells. Coimmunoprecipitation experiments with extracts of vA33Rmyc-infected cells confirmed the existence of a physical association of A33 with A36 and B5. Of these, the A33-B5 interaction is a novel finding, whereas the interaction between A33 and A36 has been previously characterized. A collection of vaccinia viruses expressing mutated versions of the B5 protein was used to investigate the domain(s) of B5 required for interaction with A33. Both the cytoplasmic domain and most of the extracellular domain, but not the transmembrane domain, of the B5 protein were dispensable for binding to A33. Mutations in the extracellular portions of B5 and A33 that enhance extracellular virus release did not affect the interaction between the two. In contrast, substituting the B5 transmembrane domain with that of the vesicular stomatitis virus G glycoprotein prevented the association with A33. Immunofluorescence experiments on virus mutants indicated that B5 is required for efficient targeting of A33 into enveloped virions. These results point to the transmembrane domain of B5 as the major determinant of the A33-B5 interaction and demonstrate that protein-protein interactions are crucial in determining the composition of the virus envelope.
 ...
PMID:Interaction between vaccinia virus extracellular virus envelope A33 and B5 glycoproteins. 1691 23