Induction and Genomic Analysis of a Lysogenic Phage of Hafnia paralvei

Lingting Pan; Dengfeng Li; Yigang Tong; Wei Lin; Weinan Qin; Lihua Xu; Pingping Zhan

doi:10.1007/s00284-021-02698-0

Characterization of the ELPhiS Prophage from Salmonella enterica Serovar Enteritidis Strain LK5

Applied and Environmental Microbiology ◽

10.1128/aem.07241-11 ◽

2012 ◽

Vol 78 (6) ◽

pp. 1785-1793 ◽

Cited By ~ 17

Author(s):

L. Farris Hanna ◽

T. David Matthews ◽

Elizabeth A. Dinsdale ◽

David Hasty ◽

Robert A. Edwards

Keyword(s):

Salmonella Enterica ◽

Bacterial Pathogens ◽

Genomic Analysis ◽

Bacterial Genomes ◽

Salmonella Enterica Serovar Enteritidis ◽

Content Type ◽

Transfer Genes ◽

Screen Approach ◽

Lysogenic Phage

ABSTRACTPhages are a primary driving force behind the evolution of bacterial pathogens by transferring a variety of virulence genes into their hosts. Similar to other bacterial genomes, theSalmonella entericaserovar Enteritidis LK5 genome contains several regions that are homologous to phages. Although genomic analysis demonstrated the presence of prophages, it was unable to confirm which phage elements within the genome were viable. Genetic markers were used to tag one of the prophages in the genome to allow monitoring of phage induction. Commonly used laboratory strains ofSalmonellawere resistant to phage infection, and therefore a rapid screen was developed to identify susceptible hosts. This approach showed that a genetically tagged prophage, ELPhiS (Enteritidis lysogenic phage S), was capable of infectingSalmonellaserovars that are diverse in host range and virulence and has the potential to laterally transfer genes between these serovars via lysogenic conversion. The rapid screen approach is adaptable to any system with a large collection of isolates and may be used to test the viability of prophages found by sequencing the genomes of various bacterial pathogens.

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Genomic Analysis of the Polyvalent Bacteriophage FP01

10.20944/preprints201907.0169.v1 ◽

2019 ◽

Author(s):

Ignacio Vasquez ◽

Julio Retamales ◽

Barbara Parra ◽

James Robeson ◽

Javier Santander

Keyword(s):

Escherichia Coli ◽

Potential Application ◽

Complete Genome ◽

Phylogenetic Analyses ◽

Genomic Analysis ◽

Host Factors ◽

Coding Sequences ◽

Double Stranded Dna ◽

Host Infection ◽

Lysogenic Phage

Recently the polyvalent bacteriophage FP01, isolated from wastewater in Valparaiso, Chile, was described to have lytic activity across species against Escherichia coli and Salmonella enterica serovars. Due to it polyvalent nature the bacteriophage FP01 could have potential application in food and agri-industry. Also, fundamental aspects of polyvalent bacteriophage biology are not well known. In this study we sequenced and describe the complete genome of the polyvalent phage FP01 (MH745368) using the nanopore technology. The bacteriophage FP01 genome has a 44,900 bp, double-stranded DNA with an average G+C content of 49.41% and 90 coding sequences (CDSs). We found that the phage FP01 critically depends on host factors for replication and transcription. Also, it has a critical lysogenic repressor pseudogene. Phylogenetic analyses indicated that the phage FP01 is closely related to phages lambda and P22. These results suggest that the phage FP01 could be a lytic variant of a lysogenic phage or acquired genes from lysogenic phages during host infection.

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Genomic analysis of C-type lectins

Biochemical Society Symposium ◽

10.1042/bss0690059 ◽

2002 ◽

Vol 69 ◽

pp. 59-72 ◽

Cited By ~ 85

Author(s):

Kurt Drickamer ◽

Andrew J. Fadden

Keyword(s):

Biological Effects ◽

Cell Signalling ◽

Genomic Analysis ◽

Binding Activity ◽

Immunoglobulin Superfamily ◽

Carbohydrate Binding ◽

Carbohydrate Recognition ◽

Calcium Dependent ◽

Binding Domains ◽

Carbohydrate Recognition Domains

Many biological effects of complex carbohydrates are mediated by lectins that contain discrete carbohydrate-recognition domains. At least seven structurally distinct families of carbohydrate-recognition domains are found in lectins that are involved in intracellular trafficking, cell adhesion, cell–cell signalling, glycoprotein turnover and innate immunity. Genome-wide analysis of potential carbohydrate-binding domains is now possible. Two classes of intracellular lectins involved in glycoprotein trafficking are present in yeast, model invertebrates and vertebrates, and two other classes are present in vertebrates only. At the cell surface, calcium-dependent (C-type) lectins and galectins are found in model invertebrates and vertebrates, but not in yeast; immunoglobulin superfamily (I-type) lectins are only found in vertebrates. The evolutionary appearance of different classes of sugar-binding protein modules parallels a development towards more complex oligosaccharides that provide increased opportunities for specific recognition phenomena. An overall picture of the lectins present in humans can now be proposed. Based on our knowledge of the structures of several of the C-type carbohydrate-recognition domains, it is possible to suggest ligand-binding activity that may be associated with novel C-type lectin-like domains identified in a systematic screen of the human genome. Further analysis of the sequences of proteins containing these domains can be used as a basis for proposing potential biological functions.

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