In alternative embodiments, provided are products of manufacture and kits, and methods, to enrich for and/or isolate microbes such as viruses and/or phages capable of targeting, e.g., binding to, targeting, and/or killing or otherwise making non-viable or non-pathogenic, specific or desired microbes such as bacteria. In alternative embodiments, provided are products of manufacture comprising: a virus and/or a phage (a bacteriophage). In alternative embodiments, provided are products of manufacture and kits containing a virus and/or a phage (a bacteriophage) enriched for, selected for or isolated by a method as provided herein, or a microbe containing a virus and/or a phage (a bacteriophage) enriched, selected for and/or isolated by a method as provided herein.

Described is an artificial virus (AV) programmed with biomolecules that can enter human cells and carry out precise human genome modification. The AVs comprise: at least one viral vector, such as bacteriophage T4; at least one therapeutic molecule, such as DNA, RNA, protein and their complex; and a lipid coating. Also described is a method of human genome modification, using such an AV, and a method of program such an AV.

The present invention provides new bacteriophages, their selection, compositions, cocktails and formulations thereof, and their administration for the prevention of opportunistic infections in livestock, such as Avian Pathogenic E. Coli (APEC) infections in poultry.

Disclosed is a broad-spectrum phage for efficiently lysing Cronobacter, a bactericide, and use thereof. Also provided is a Cronobacter phage vB_CsaM_CBT2, where the phage has a deposit number of CCTCC NO: M 2023524. The phage only specifically lyses Cronobacter, has a broad lysis spectrum, and can cover four species of Cronobacter (including multi-drug-resistant bacteria). The phage shows a desirable stability at a pH value of 3 to 11 and 25 C. to 70 C., and has a bactericidal effect of 80.55% to 99.97% within 12 h in a milk powder sample. Moreover, the phage does not carry any virulence and antibiotic resistance genes, and meets the safety requirements in practical applications. Therefore, the phage provides a new strategy and resource guarantee for the control of Cronobacter contamination in powdered infant formula (PIF) and its industrial chain and environment, as well as the development of bactericides.

Systems and methods for editing bacteriophages are described herein.

The present disclosure relates to compositions including or obtained from genetically modified bacterial host cells (e.g., E. coli) and methods for using the same for cell-free bacteriophage synthesis (CFBS). In particular, the present technology relates to genetically modified E. coli that overexpress one or more of translation initiation factor IF-3 (infC), OxyS and CyaR and/or repress RecC subunit exonuclease RecBCD, and methods for using the same to obtain improved CFBS yields.

This invention provides a robust fermentation process for the expression of a capsid protein of a bacteriophage which is forming a VLP by self-assembly, wherein the process is scalable to a commercial production scale and wherein the expression rate of the capsid protein is controlled to obtain improved yield of soluble capsid protein. This is achieved by combining the advantages of fed-batch culture and of lactose induced expression systems with specific process parameters providing improved repression of the promoter during the growth phase and high plasmid retention throughout the process.

Embodiments of the present disclosure provide novel compositions and methods for making and using thermostable bacteriophage or bacteriophage-derived phage-like-particle (PLP)-containing formulations. In certain embodiments, compositions and methods are disclosed for embedding, decorating and/or associating at least one antigen or agent, or bioactive molecule on the surface of the bacteriophage or PLPs. In accordance with these embodiments, bacteriophage or PLPs harboring one or more antigen or agent, or bioactive molecule can further be thermostabilized and/or coated with one or more atomic layer deposition applied coating layer for control or timed release of the one or more antigen or agent when administered to a subject.

The present invention relates to multi-peptide structures comprising at least one heterogenous functional site wherein the at least one heterogenous functional site is composed of at least two homologous peptides, which differ by at least one amino acid, a method for providing such multi-peptide structures, compositions comprising such multi-peptide structures as well as the use of such multi-peptide structures and compositions as an universal anti-microbial agent, in particular in medicine, chemistry, biotechnology, agriculture and/or food industry.

Described herein is a protein display selection method which uncouples a protein of interest (POI) library from the display selection system. Display of the POI can be achieved by forming a covalent bond between the POI and the anchor protein post expression either by enzymatic protein ligation (e.g. SpyLigase, SnoopLigase, sortase, butelase, peptiligase etc.) or by spontaneous covalent bond formation (e.g. SpyTag/SpyCatcher, SnoopTag/SnoopCatcher, etc.). The POI library is fused to a tethering sequence, for example SpyTag, at the C-terminus of the POI which then forms a covalent bond to a capture sequence found on an anchor protein, for example, the SpyCatcher-fused anchor protein, e.g., a SpyCatcher-geneIII protein (SpyCatcher-pIII) fusion, for the most common form of phage display. Nucleic acid constructs, host cell systems and methods of producing the protein display systems are also provided.