A comparative study of high molecular virus-specific proteins in cells infected with flaviviruses from 5 serological subgroups was carried out. Proteins NV5, NV4, and V3 were found to have similar electrophoretic mobility in viruses of the tick-borne encephalitis (TBE) complex with the exception of Powassan virus protein. Proteins NV5 and NV4 of mosquito-borne flaviviruses differ in electrophoretic mobility both from the corresponding proteins of the TBE complex viruses and from each other. Protein NV4 1/2 is formed only in cells infected with TBE complex viruses. Varying electrophoretic mobility of protein NV3 in different flaviviruses attests to its virus-specific nature.
Download full-text PDF |
Source |
|---|
Publication Analysis
Top Keywords
Similar Publications
LACCASE35 Enhances Lignification and Resistance Against Pseudomonas syringae pv. actinidiae Infection in Kiwifruit.
Plant Physiol
January 2025
Anhui Key Laboratory for Horticultural Crop Quality Biology, School of Horticulture, Anhui Agricultural University, Hefei, 230036, P.R. China.
Kiwifruit bacterial canker, a highly destructive disease caused by Pseudomonas syringae pv. actinidiae (Psa), seriously affects kiwifruit (Actinidia spp.) production.
View Article and Find Full Text PDFNeutral lipids restrict the mobility of broken DNA molecules during comet assays.
Biol Cell
January 2025
Centre de Recherche en Biologie cellulaire de Montpellier (CRBM), Université de Montpellier, Centre National de la Recherche Scientifique, Montpellier, France.
One widespread technique to assess in relative terms the amount of broken DNA present in the genome of individual cells consists of immobilizing the cell's nucleus under an agarose pad (called the nucleoid) and subjecting the whole genome to electrophoresis to force broken DNA molecules out of it. Since the migrating broken DNA molecules create a tail behind the nucleoid, this technique is named the comet assay. While performing comet assays regularly, we systematically observed circular regions devoid of DNA within the nucleoid region.
View Article and Find Full Text PDFGenetic predisposition to Behcet's disease mediated by a IL10RA enhancer polymorphism.
Heliyon
January 2025
The First Affiliated Hospital of Chongqing Medical University, Chongqing Branch (Municipality Division) of National Clinical Research Center for Ocular Diseases, Chongqing, PR China.
Background: Several studies suggested the genetic association between IL10RA variants and susceptibility to Behcet's disease (BD). However, the precise mechanism of the association is still unknown. The purpose of this study was to investigate the mechanism underlying the genetic associations between IL10RA polymorphisms and the risk of BD.
View Article and Find Full Text PDFReinvestigation into the role of lipopolysaccharide Glycosyltransferases in protein glycosylation.
Gut Microbes
December 2025
Center of Infectious Diseases, West China Hospital of Sichuan University, Chengdu, China.
Protein glycosylation has been considered as a fundamental phenomenon shared by all domains of life. In , glycosylation of flagellins A and B with pseudaminic acid have been rigorously confirmed and shown to be essential for flagella assembly and bacterial colonization. In addition to flagellins, several other proteins including RecA, AlpA/B, and BabA/B in have also been reported to be glycosylated and to be dependent on the lipopolysaccharide (LPS) biosynthetic pathway.
View Article and Find Full Text PDFFunctional analysis of the type II toxin-antitoxin system ParDE in Streptococcus suis serotype 2.
BMC Vet Res
January 2025
College of Veterinary Medicine, Nanjing Agricultural University, Nanjing, 210095, China.
Streptococcus suis (S. suis) is a major pathogen in swine and poses a potential zoonotic threat, which may cause serious diseases. Many toxin-antitoxin (TA) systems have been discovered in S.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!