Abstract The single-stranded, negative-sense, viral genomic RNA (vRNA) of influenza A virus is encapsidated by nucleoproteins (NPs) and an polymerase to form a ribonucleoprotein complex (vRNP) with helical, rod-shaped structure. vRNP responsible for transcription replication the vRNA. However, conformation during synthesis not well understood. Here, using high-speed atomic force microscopy cryo...

Previous data indicate that immune mechanisms may be involved in developing capillary leakage during Sin Nombre virus (SNV) infection. Therefore, we investigated production of tumor necrosis factor alpha (TNF-alpha) by human alveolar macrophages and human umbilical vein endothelial cells (HUVEC) after infection with SNV. In addition, we examined the effect of TNF-alpha on HUVEC monolayer leakag...

Formaldehyde fixation of simian virus 40 (SV40)-infected CV-1 cells at appropriate times after infection permits us to isolate crosslinked complexes of SV40 minichromosomes during the time of DNA replication and during packaging with viral proteins. Such crosslinked complexes can be separated on the basis of density on CsCl/guanidine . HCl density gradients. During the course of these studies w...

Influenza A virus is an enveloped virus with a segmented, single-strand, negative-sense RNA genome. Its virions show spherical or filamentous shapes of about 100 nm in diameter and occasionally irregular morphology, which exemplifies the pleomorphic nature of these virions. Each viral RNA segment forms a ribonucleoprotein complex (RNP), along with an RNA-dependent RNA polymerase complex and mul...

In a study of the role of cathepsins in nuclear metabolism (1) these intracellular proteinases were found to hydrolyze thymus nucleoproteins and render dialyzable the desoxyribonucleic acid. Further characterization of this nuclease activity of the cathepsin preparations revealed pH optima in the acid range for both desoxyribonucleic acid (DNA) and ribonucleic acid (RNA). This was in contrast t...