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At least 37 records · Page 2Linked to original sources
PubMed1975

Treatment of RSV-transformed "poorly" virogenic and non-virogenic mammalian cell lines with inhibitors of protein synthesis: failure to potentiate RSV rescue.

Treatment of the RSV-transformed "poorly" virogenic rat clones LW13-RsK4 and LW13-RsK4 R1 with cycloheximide or puromycin before fusion with chick embryo fibroblasts did not lead to RSV rescue. Neither was RSV rescued from the RSV-transformed non-virogenic mouse line RVP3 treated with 5-bromodeoxyuridine and cycloheximide or puromycin before fusion.

Avian Sarcoma Viruses↗
PubMed1990

Serodiagnosis of respiratory syncytial virus (RSV) infection in children as measured by detection of RSV-specific immunoglobulins G, M, and A with enzyme-linked immunosorbent assay.

The diagnostic value of an enzyme-linked immunosorbent assay for detection of respiratory syncytial virus (RSV)-specific immunoglobulin G (IgG), IgM, and IgA in sera from infants and children with proven RSV infection, from a control group, and from patients with symptoms of viral respiratory disease was analyzed. Compared to virus isolation and RSV antigen detection methods, the sensitivity of this assay was 87% and the specificity was 79%. For IgG alone, these were 45 and 92%, for IgM alone they were 48 and 92%, and for IgA alone they were 74 and 95%, respectively.

Antibodies, Viral↗
PubMed1976

Rescue of Rous sarcoma virus (RSV) from RSV-transformed human embryonic cells by cell fusion with chick embryo fibroblasts using lysolecithin.

Heterokaryon formation and Rous sarcoma virus (RSV)-induction were studied by fusion of RSV-transformed human embryonic cells with chick embryo fibroblasts in the presence of lysolecithin. Heterokaryon formation was observed by autoradiography. RSV-induction was identified by focus formation, electron microscopy and density gradient centrifugation of 3H-uridine-labeled particles. The most effective concentration of lysolecithin for virus induction was 10 mug/10(6) cells/0.1 ml. Efficiency of lysolecithin in virus induction was not less than that of ultraviolet-inactivated Sendai virus (UV-HVJ).

Animals↗
PubMed1977

Presence of ribonucleotide sequences complementary to Rous sarcoma virus (RSV) RNA in chicken cells infected with RSV.

RNA--RNA molecular hybridization between [125I] RNA from Rous sarcoma virus virions and RNAs isolated from various subcellular fractions, i.e. nuclei, mitochondria, free and membrane-bound polyribosomes, from tumors induced by RSV in chickens resulted in the formation of RNAase-resistant hybrids only with the RNA of mitochondria and membrane-bound polysomes. The origin of complementary regions in the RNAs from these organelles is discussed.

Animals↗
PubMed1989

The 1B (NS2), 1C (NS1) and N proteins of human respiratory syncytial virus (RSV) of antigenic subgroups A and B: sequence conservation and divergence within RSV genomic RNA.

A 2330 nucleotide sequence spanning the 1B (NS2), IC (NS1) and N genes and intergenic regions of human respiratory syncytial virus strain 18537, representing antigenic subgroup B, was determined by sequencing cloned cDNAs of intracellular mRNAs. Comparison with the previously reported sequences for strain A2 of subgroup A showed that 1B, 1C and N were highly conserved at the nucleotide level (78, 78 and 86% identity, respectively) and at the amino acid level (92, 87 and 96% identity, respectively). The gene-start signals were exactly conserved between subgroups, and the gene-end signals contained only a single nucleotide substitution each in 1B and N. In most cases intergenic and non-coding gene sequences that were not part of presumed transcriptive signals were much less well conserved (generally 50 to 71%) than sequences that were part of translational open reading frames (82 to 86%). The nucleotide and deduced amino acid sequences of the N gene and protein of the Long strain of subgroup A were determined by sequencing cDNA clones of intracellular mRNA; the nucleotide sequence (representing all but the first 10 nucleotides of the gene) contained 15 differences from that of the A2 strain, but the deduced amino acid sequences were identical.

Amino Acid Sequence↗
PubMed2026

Systematic review of the mutations in the active antigenic site Ø of the prefusion F protein of the Respiratory Syncytial Virus (RSV) following the implementation of monoclonal antibody prophylaxis.

BACKGROUND: Monoclonal antibody (mAb) nirsevimab, which targets the antigenic site &#xd8; of the prefusion F protein (pre-F) of RSV, was introduced for RSV prophylaxis in several countries. METHODS: A systematic search was conducted between January 1, 2022, and July 31, 2026 for studies analyzing substitutions within the epitope of pre-F RSV protein, which is the target of nirsevimab, after the implementation of the mAb. We searched across PubMed, Scopus, Web of Science and ClinicalTrial.gov for studies involving children with confirmed RSV infection, that conducted genomic analysis. RESULTS: Seven studies (five observational and two randomized controlled trials) including 2156 RSV-positive samples (RSV-A: 1347, RSV-B: 809) were analyzed. RSV-A strains showed limited variability within antigenic site &#xd8;, with K65R being the most common substitution and K209E being the only intermediate-resistance RSV-A substitution. RSV-B strains demonstrated substantially higher substitution frequencies, particularly involving I206M, Q209R, and S211N. Most identified substitutions appeared to represent naturally occurring polymorphisms and retained susceptibility to nirsevimab, while multiple RSV-B substitutions and combinations involving residues 64-68 and 204-208 demonstrated reduced susceptibility or high-level resistance. Resistance-associated variants were detected in 28 of 2156 (1.3%) RSV-positive samples and exclusively among nirsevimab breakthrough infections. In a sub-analysis restricted to nirsevimab-treated individuals, resistance-associated variants were significantly more frequent among RSV-B than RSV-A (9.8% vs 0.5%; p&#xa0;<&#xa0;0.001). CONCLUSION: Most substitutions that were detected within the nirsevimab antigenic site reflect ongoing natural RSV evolution and do not significantly affect nirsevimab susceptibility. However, detection of resistance-associated variants highlights the importance of continuous genomic and phenotypic surveillance.

Humans↗
PubMed1991

Comparison of class and subclass antibody response to live and UV-inactivated RSV administered intranasally in mice.

To determine the effect of viral dose and replication on the subclass antibody response to RSV, mice were immunized intranasally with different doses of live RSV (10(4)-10(6) pfu) and compared to mice given an immunizing regimen of UV-inactivated RSV. Mice given the 10(6) pfu dose of live RSV and mice given the 40 micrograms dose of UV-inactivated RSV had comparable class specific antibody responses to whole RSV in serum and respiratory secretions. Serum from these two groups of mice were then compared for IgG subclass response to whole RSV. A predominance of IgG2a subclass antibody was found for both immunizing regimens, and no significant differences in subclass proportions were noted between regimens. These two regimens were then compared for serum total IgG response to RSV surface glycoproteins F and G. The serum IgG response to these glycoproteins was lower after immunization with UV-inactivated RSV than after live-RSV immunization (F: P = 0.03; G: P less than 0.05), even though the serum IgG response of the two groups to whole RSV was comparable. The IgG subclass response to surface glycoproteins was evaluated for live RSV immunization. The proportions of subclass antibody responses to glycoprotein F were comparable to the subclass response proportions to whole RSV and were not characteristic of a T-dependent response pattern. The subclass profile for glycoprotein G was not comparable to that of whole RSV but was suggestive of a T-independent response pattern.

Administration, Intranasal↗
PubMed1985

Transformation of erythroid cells by Rous sarcoma virus (RSV).

RSV transforms several nonhematopoietic cell types and as reported here also has the capacity to transform hematopoietic cells of the erythroid lineage. In vitro, the three RSV isolates tested induced erythroblast-like colonies in infected bone marrow cells that were distinguishable by size and cell arrangement from those induced by avian erythroblastosis virus (AEV). Also in contrast to AEV-transformed erythroblast cultures, isolated cell colonies induced by RSV required complex growth conditions in liquid medium similar to the in vitro conditions necessary for erythroblasts transformed by the acute leukemia virus E26. Temperature-shift experiments using temperature-sensitive (ts) NY68 RSV revealed that when grown at the nonpermissive temperature (42 degrees), mutant-infected cells became benzidine positive and partially differentiated into erythrocytes. Wild-type (wt) RSV-transformed cells did not undergo similar changes. However, both wt RSV-, and to a greater extent, ts RSV-transformed cultures at the permissive temperature (37 degrees) did contain populations of spontaneously differentiating erythroid cells signifying that the transforming activity of the virus did not fully arrest erythroid maturation. In addition, the RSV-transformed cells did express tyrosine kinase activity. When injected intravenously into birds, RSV induced an erythroblastosis-like disease similar to AEV but also caused fibrosarcomas and leg paralysis. These results show that RSV can alter the pattern of erythroid differentiation in a manner similar to, but distinct from, AEV and indicate that the tyrosine-specific pp60src kinase is involved in erythroid cell transformation. Since the src and erb B proteins share a significant amino acid homology, these data suggest that both may also share a common functional homology.

Alpharetrovirus↗
PubMed1976

Interactions of concanavalin A with chick embryo fibroblasts transformed by Rous sarcoma virus. Study with an RSV mutant thermosensitive for transformation.

The interactions between concanavalin A and chick embryo fibroblasts, normal and infected with Rous sarcoma virus (RSV-BH) or its thermosensitive mutant RSV-BH-Ta, have been studied. Normal chick embryo cells and RSV-BH transformed cells showed at 4 and 25 degrees C a similar number of concanavalin A receptors per cell. Analysis of the binding data by the Scatchard relation showed that apparent changes in binding as a function of temperature are due to the thermodynamic properties of the process and not to endocytosis. The lectin receptors on the cell surface of normal and RSV-BH infected cells showed homogeneity in their binding properties. Chick cells infected with RSV-BH-Ta showed a lectin binding behavior that was dependent on the temperature at which the cells were grown. At the permissive temperature for transformation (37 degrees C), the binding process was similar to that observed for normal and RSV-BH infected cells. At the nonpermissive temperature (41 degrees C), the cells showed at least two sets of concanavalin A receptors. The new set of receptors on the cell surface had a lower lectin affinity than those observed in the same cells at 37 degrees C. Chick cells infected with RSV-BH showed an enhanced agglutinability by concanavalin A, as compared with normal cells. Cells infected with RSV-BH-Ta showed a reversal of the correlation between increased concanavalin A agglutinability and the transformed state. At the permissive temperature for transformation, the cells were not agglutinable, whereas at the nonpermissive temperature they presented agglutinability indexes as high as those observed with RSV-BH infected cells. This enhanced agglutinability observed with cells maintained at the nonpermissive temperature for transformation may be related to the new set of low affinity receptors present at 41 degrees C.

Agglutination Tests↗