Background: Increasing the quantity and detail of bacteriophage genomic data is critical to broadening our understanding of how bacteriophages operate to allow us to harness their unique properties for biotechnology advancements. Here we present the complete sequence of phage SV76's assembled and annotated genome (Accession OM339528). SV76 has previously been classified as a T4-like bacteriophage belonging to the genus within the family of contractile tailed bacteriophages.
Materials And Methods: Whole genome sequencing, assembly, and annotation was performed on SV76. Double-agar spot assays were utilized to determine SV76's host range against a panel of 72 isolates meant to represent the diversity of , as well as a series of knockouts designed to identify required receptor binding proteins. The genome and host range were compared to the closely related phage, T2.
Results: Spot assays revealed that SV76 could plaque on 10 of the 72 strains (13.9 %) and nine of the nine K12 single gene knockout of known phage receptors (100%). SV76 did not plate on a indicating suggesting a requirement as a receptor binding protein.
Conclusions: SV76 is closely related to T2 with similar host ranges within ECOR. This study presents novel host range and genomic data on SV76 phage, providing a foundation for future studies to further characterize SV76 to understand more about SV76 and other T4-like phages that can be applied to create novel biotechnologies.
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http://dx.doi.org/10.1089/phage.2022.0005 | DOI Listing |
Anim Microbiome
January 2025
Genomics & Bioanalytics, Los Alamos National Laboratory, Los Alamos, NM, 87506, USA.
Background: African buffalo (Syncerus caffer) is a significant reservoir host for many zoonotic and parasitic infections in Africa. These include a range of viruses and pathogenic bacteria, such as tick-borne rickettsial organisms. Despite the considerations of mammalian blood as a sterile environment, blood microbiome sequencing could become crucial for agnostic biosurveillance.
View Article and Find Full Text PDFCell Mol Biol (Noisy-le-grand)
January 2025
Plant Protection Department, College of Food and Agriculture Sciences, King Saud University, P.O. Box 2460, Riyadh, 11451, Saudi Arabia.
Forty-four samples of garlic plants showing virus-like symptoms were collected, during the growing season (2021-2022) from different locations in Qassim province, Saudi Arabia. These samples were analyzed by ELISA against the important Allium allexiviruses including garlic virus A (GarV-A), garlic virus B (GarV-B), garlic virus C (GarV-C), and Shallot virus X (ShVX). The obtained results showed that 22/44 (50%) samples were found to be infected with one of the tested viruses.
View Article and Find Full Text PDFBiotechnol Bioeng
January 2025
Chair of Technical Biochemistry, Technische Universität Dresden, Dresden, Saxony, Germany.
Ikarugamycin is a member of the natural product family of the polycyclic tetramate macrolactams (PoTeMs). The compound exhibits a diverse range of biological activities, including antimicrobial, antiprotozoal, anti-leukemic, and anti-inflammatory properties. In addition, it interferes with several crucial cellular functions, such as oxidized low-density lipoprotein uptake in macrophages, Nef-induced CD4 cell surface downregulation, and mechanisms of endocytosis.
View Article and Find Full Text PDFFEMS Microbiol Lett
January 2025
Department of Bioscience and Biotechnology, Indian Institute of Technology Kharagpur, Kharagpur-721302, West Bengal, India.
Verona-integron-metallo-β-lactamase (VIM-2) is one of the most widespread class B β-lactamase responsible for β-lactam resistance. Although active-site residues help in metal binding, the residues nearing the active-site possess functional importance. Here, to decipher the role of such residues in the activity and stability of VIM-2, the residues E146, D182, N210, S207, and D213 were selected through in-silico analyses and substituted with alanine using site-directed mutagenesis.
View Article and Find Full Text PDFJ Biol Chem
January 2025
Developmental Therapeutics Branch, Center for Cancer Research, National Cancer Institute, Bethesda, MD, USA; Department of Oncology, Division of Oncology Research, Mayo Clinic, Rochester, MN, USA; Department of Molecular Pharmacology and Experimental Therapeutics, Mayo Clinic, Rochester, MN, USA. Electronic address:
The host-range mutant of rabbitpox virus (RPXV) with a deletion in the gene encoding the serpin serine protease inhibitor 1 (SPI-1) fails to replicate efficiently in restrictive host cells. Depletion of the host cell serine protease FAM111A restores viral replication in these cells, suggesting that SPI-1 targets FAM111A to facilitate infection. However, direct evidence of SPI-1 inhibiting FAM111A has been lacking.
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