Zhu et al. show that pp2 prophage of LpNC8, a Drosophila symbiont, promotes bacterial lysis and the recovery of extracellular vesicles containing lipoteichoic acids, supporting juvenile growth under nutritional stress. The copper cell region of the fly midgut promotes prophage activity in vivo, linking intestinal physiology to bacterial lysis and symbiotic function.

Zhu et al. show that pp2 prophage of LpNC8, a Drosophila symbiont, promotes bacterial lysis and the recovery of extracellular vesicles containing lipoteichoic acids, supporting juvenile growth under n...

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Toxin/antitoxin systems (TAs) are stress-response loci most-closely linked to stabilizing mobile genetic elements such as plasmids and inhibiting phage infection. In contrast to the phage inhibition p...

Wedd and colleagues present a physiology-resolved view of bacteriophage infection by tracking individual T7 infections in single E. coli cells from genome injection to lysis. Resolving successive infection stages reveals where timing variability emerges and links infection dynamics to the physiological state of individual host cells.

The RNA Lysis Buffer Market was valued at USD 1.2 billion in 2025 and is poised to grow from USD 1.

by Yalu Ji, Meimei Zhang, Liran Song, Hui Ning, Li Wang, Cao Qiu, Jingmin Gu Streptococcus suis (S. suis) is an encapsulated zoonotic pathogen that can form recalcitrant biofilms. Bacteriophage-derived endolysins and depolymerases represent promising antibiofilm agents, but currently, no report has described protein which displays both of lytic and capsule degradation activities simultaneously. Here, we mined the porcine gut virome and identified Lys33795, a dual-activity antibacterial protein that degrades both capsule and peptidoglycan of S. suis. Lys33795 consists of an N-terminal GH25_muramidase domain and a C-terminal cell wall binding domain (CBD). However, translational reinitiation at an internal start codon (M217) in the Lys33795 sequence generates an additional CBD that may assembles with the full-length protein to form an oligomeric complex. Interestingly, the GH25 muramidase truncation fragment of Lys33795 not only retains its classical function as a peptidoglycan hydrolase for degrading bacterial cell walls but also exhibits degradation activity towards capsule. This discovery contrasts sharply with the traditional functional understanding of the GH25 family. In addition, the CBD alone has a stable dimer and, as a nonstandard depolymerase without any classical polysaccharide-degrading catalytic domains, retains its degradation activity against S. suis capsule. We elucidated the molecular mechanism of Lys33795 exhibiting dual activity by combining mutagenesis, lysis, and capsule degradation activity assays. In addition, the results of in vitro and in vivo experiments showed that Lys33795 can effectively prevent and clear S. suis biofilms, and is more effective than single active mutants, and has a enhance effect when used in combination with antibiotics. This study describes the first multimeric bacteriophage protein with dual activities of lysis and capsule degradation against S. suis, encoded by a single gene. These findings provide valuable insights for designing potent antibacterial proteins targeting encapsulated pathogens.