Anders Nørgaard Sørensen

This study identifies a dUTPase from Mosigvirus AV110 that inhibits E. coli growth by disrupting DNA replication and cell division, revealing functional and evolutionary diversity among phage-encoded dUTP/dCTPases.

This study identifies Htm, a phage-encoded protein that reprograms the transcriptome of ESBL-E. coli to support phage replication by altering gene expression and metabolic pathways.

The paper identifies an antibacterial peptide from a phage that inhibits E. coli growth by disrupting Mre-dependent peptidoglycan synthesis.

This study shows Ackermannviridae phages can acquire new tail spike proteins to expand their branched receptor complex, enabling adaptation to new hosts.

The paper isolates and characterizes 28 unique bacteriophages against ESBL/AmpC E. coli, showing they can form broad host range cocktails effective in inhibiting bacterial growth in vitro.

Agtrevirus phage AV101 expresses four unique tail spike proteins that recognize different O-antigens of Extended Spectrum β-lactamase-producing E. coli.

The paper genetically engineers phages to produce Tailocins, which kill their native hosts, expanding antimicrobial options.

The paper identifies a hybrid receptor binding protein in phage F341 that enables infection of Campylobacter by binding to flagella and lipooligosaccharides, revealing potential for phage resistance mechanisms.