Autographa californica multiple nucleopolyhedrovirus (AcMNPV) odv-e66 is a core gene and encodes an occlusion-derived virus (ODV)-specific envelope protein, ODV-E66. The N-terminal 23 amino acid of the envelope protein ODV-E66 are sufficient to direct native and fusion proteins to induced membrane microvesicles and the viral envelope during infection with AcMNPV. In this study, an odv-e66-knockout bacmid can not express N-terminal hydrophobic domains was constructed via homologous recombination in Escherichia coli. The odv-e66 deletion had no effect on budded virus (BV) production and viral DNA replication in infected Sf9 cells. Larval bioassays demonstrated that injection of odv-e66 deletion BV into the hemocoel could kill P. xylostella larvae as efficiently as repaired and control viruses; however, odv-e66 deletion mutant resulted in a 50% lethal dose that was 10(3) higher than that of the repaired and control viruses when inoculated per os. These results indicated that ODV-E66 envelope protein most likely played an important role in the oral infectivity of AcMNPV, but is not essential for virus replication.
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http://dx.doi.org/10.1016/j.virusres.2011.03.012 | DOI Listing |
Appl Environ Microbiol
December 2024
Biology Department, San Diego State University, San Diego, California, USA.
Unlabelled: Many species of proteobacterial methane-consuming bacteria (methanotrophs) form a hauberk-like envelope represented by a surface (S-) layer protein (SLP) matrix. While several proteins were predicted to be associated with the cell surface, the composition and function of the hauberk matrix remained elusive. Here, we report the identification of the genes encoding the hauberk-forming proteins in two gamma-proteobacterial (Type I) methanotrophs, 5GB1 (EQU24_15540) and 20Z (MEALZ_0971 and MEALZ_0972).
View Article and Find Full Text PDFInfect Immun
December 2024
Laboratory of Intracellular Bacterial Pathogens, National Centre for Biotechnology (CNB-CSIC), Madrid, Spain.
Type III protein secretion systems (T3SSs) function as multiprotein devices that span the envelope of Gram-negative bacteria using the peptidoglycan (PG) layer as scaffold. This spatial arrangement explains why modifications in PG structure can alter T3SS activity. In incorporation of non-canonical D-amino acids in the PG was shown to decrease the activity of the T3SS encoded by the pathogenicity island-1 (SPI-1) without affecting other T3SS, like the flagellum apparatus.
View Article and Find Full Text PDFJ Med Virol
January 2025
Department of Microbiology, Howard University College of Medicine, Washington, District of Columbia, USA.
SARS-CoV-2 Envelope (E) protein is critical in viral assembly, release, and virulence. E gene was considered highly conserved and evolving slowly. Pan-sarbecoviruses-conserved regions in the E gene have been used as targets for various RT-PCR assays to detect SARS-CoV-2.
View Article and Find Full Text PDFJ Phys Chem Lett
December 2024
Molecular Ocean Lab, Institute for Advanced Chemistry of Catalonia, IQAC-CSIC, Carrer de Jordi Girona 18-26, 08034 Barcelona, Spain.
Protein-bound ligands can adopt a range of different conformations, collectively defining a ligand envelope that has proven to be crucial for the design of potent and selective drugs. Yet, the cryptic nature of this ligand envelope makes it difficult to visualize, characterize, and ultimately exploit for drug design. Using enhanced molecular dynamics simulations, here, we provide a general framework to reconstruct the cryptic ligand envelope that is dynamically accessible by protein-bound small molecules in solution.
View Article and Find Full Text PDFVet Med Sci
January 2025
Chongqing Three Gouges Vocational College, College of Animal Science & Technology, Wanzhou, China.
Peste des petits ruminants virus (PPRV), a single-stranded negative-sense RNA virus with an envelope, belongs to the Morbillivirus in the Paramyxoviridae family and is prevalent worldwide. PPRV infection causes fever, stomatitis, diarrhoea, pneumonia, abortion and other symptoms in small ruminants, with a high mortality rate that poses a significant threat to the sustainability and productivity of the small ruminant livestock sector. The PPRV virus particles have a diameter of approximately 400-500 nm and are composed of six structural proteins: nucleocapsid protein (N), phosphoprotein (P), envelope matrix protein (M), fusion protein (F), haemagglutinin protein (H) and large protein (L).
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