Category Ranking
98%
Total Visits
921
Avg Visit Duration
2 minutes
Citations
20
Article Abstract
An important viromics challenge is associating bacteriophages to hosts. To address this, we developed adsorption sequencing (AdsorpSeq), a readily implementable method to measure phages that are preferentially adsorbed to specific host cell envelopes. AdsorpSeq thus captures the key initial infection cycle step. Phages are added to cell envelopes, adsorbed phages are isolated through gel electrophoresis, after which adsorbed phage DNA is sequenced and compared with the full virome. Here, we show that AdsorpSeq allows for separation of phages based on receptor-adsorbing capabilities. Next, we applied AdsorpSeq to identify phages in a wastewater virome that adsorb to cell envelopes of nine bacteria, including important pathogens. We detected 26 adsorbed phages including common and rare members of the virome, a minority being related to previously characterized phages. We conclude that AdsorpSeq is an effective new tool for rapid characterization of environmental phage adsorption, with a proof-of-principle application to Gram-negative host cell envelopes.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7452251 | PMC |
| http://dx.doi.org/10.1016/j.isci.2020.101439 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Deficient of glycosylation site in the envelop protein attenuated Zika virus replication in mosquito cells.
Front Microbiol
August 2025
College of Life Sciences, Hebei University, Baoding, China.
Introduction: The Zika virus (ZIKV) envelope (E) protein is critical for viral replication and host interactions. Although glycosylation of the E protein is known to influence viral infectivity and immune evasion, the specific functional roles of E protein glycosylation in ZIKV infectivity in mosquito cells remain unclear.
Methods: In this study, we generated a deglycosylation mutant ZIKV with a T156I substitution in the E protein and investigated its effects on viral replication and viral-host interactions in mosquito C6/36 cells.
Structure, function and assembly of nuclear pore complexes.
Nat Rev Mol Cell Biol
September 2025
Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA, USA.
The defining property of eukaryotic cells is the storage of heritable genetic material in a nuclear compartment. For eukaryotic cells to carry out the myriad biochemical processes necessary for their function, macromolecules must be efficiently exchanged between the nucleus and cytoplasm. The nuclear pore complex (NPC) - which is a massive assembly of ~35 different proteins present in multiple copies totalling ~1,000 protein subunits and architecturally conserved across eukaryotes - establishes a size-selective channel for regulated bidirectional transport of folded macromolecules and macromolecular assemblies across the nuclear envelope.
View Article and Find Full Text PDFThe KASH protein UNC-83 differentially regulates kinesin-1 activity to control developmental stage-specific nuclear migration.
Curr Biol
September 2025
Department of Molecular and Cellular Biology, University of California, 1 Shields Avenue, Davis, CA 95616, USA. Electronic address:
Nuclear migration plays a fundamental role in development, requiring precise spatiotemporal control of bidirectional movement through dynein and kinesin motors. Here, we uncover a differential isoform-dependent mechanism for developmental regulation of nuclear migration directionality. The nuclear envelope Klarsicht/ANC-1/Syne homology (KASH) protein UNC-83 in Caenorhabditis elegans exists in multiple isoforms that differentially control motor activity to achieve tissue-specific nuclear positioning.
View Article and Find Full Text PDFTherapeutic potential, antimicrobial activity against acne-causing bacteria, and modes of action of WKK10 and WRR10, novel cationic antimicrobial peptides.
Bioorg Chem
September 2025
School of Cosmetic Science, Mae Fah Luang University, Chiang Rai 57100, Thailand. Electronic address:
Although antimicrobial peptides possess potent antimicrobial activities, the high cost of production, based on amino acid length, has limited their therapeutic and cosmeceutical applications. This study aimed to produce and characterize de novo designed antimicrobial peptides derived from WSKK11 and WSRR11 for efficacy against acne-causing bacteria. Ten designed peptides were evaluated for antimicrobial, hemolytic, and cytotoxic activities, as well as, secondary structures by FTIR and modes of action.
View Article and Find Full Text PDFMatrix Protein 1 (M1) of Influenza A Virus: Structural and Functional Insights.
Emerg Microbes Infect
September 2025
State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases, Key Laboratory for Zoonosis Research of the Ministry of Education, and College of Veterinary Medicine, Jilin University, Changchun 130062, China.
Enveloped viruses rely on matrix proteins for structural integrity and lifecycle progression. Matrix protein 1 (M1) is the most abundant structural protein of influenza A virus (IAV), playing a multifaceted role in viral uncoating, polymerase activity, vRNA transcription and replication, and assembly and budding. The M1 protein not only interacts with host cells but also regulates viral morphogenesis, thereby influencing viral transmissibility and pathogenicity.
View Article and Find Full Text PDF