{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Peng Y"],"funding":["National Natural Science Foundation of China (National Science Foundation of China)"],"pagination":["1772"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12917162"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["17(1)"],"pubmed_abstract":["Siphophages possess a long, flexible, and non-contractile tail that is responsible for host recognition, cell wall perforation, and genome delivery. Although the majority of structurally characterized siphophages target Gram-negative bacteria, those infecting Gram-positive bacteria remain elusive. Moreover, structural information concerning phage infection and genome release events in Gram-positive infecting siphophages is sparse. Here, we present a near-atomic resolution structure of Brochothrix thermosphacta bacteriophage NF5 determined by cryo-electron microscopy (cryo-EM). The structure comprises 11 proteins associated with the head, neck, tail tube, and baseplate, amounting to 643 polypeptides in total. Integration of cellular cryo-electron tomography (cryo-ET) showed the infection pr"],"journal":["Nature communications"],"pubmed_title":["Structure of a Brochothrix thermosphacta bacteriophage reveals cell wall adsorption mechanism in Gram-positive infecting siphophages."],"pmcid":["PMC12917162"],"funding_grant_id":["32200994","12034006","32401014"],"pubmed_authors":["Liu H","Peng Y","Zheng J","Chen W","Xiao H","Pang H","Yang F","Zhou J"],"additional_accession":[]},"is_claimable":false,"name":"Structure of a Brochothrix thermosphacta bacteriophage reveals cell wall adsorption mechanism in Gram-positive infecting siphophages.","description":"Siphophages possess a long, flexible, and non-contractile tail that is responsible for host recognition, cell wall perforation, and genome delivery. Although the majority of structurally characterized siphophages target Gram-negative bacteria, those infecting Gram-positive bacteria remain elusive. Moreover, structural information concerning phage infection and genome release events in Gram-positive infecting siphophages is sparse. Here, we present a near-atomic resolution structure of Brochothrix thermosphacta bacteriophage NF5 determined by cryo-electron microscopy (cryo-EM). The structure comprises 11 proteins associated with the head, neck, tail tube, and baseplate, amounting to 643 polypeptides in total. Integration of cellular cryo-electron tomography (cryo-ET) showed the infection pr","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Jan","modification":"2026-07-16T10:08:26.94Z","creation":"2026-07-09T10:48:11.808Z"},"accession":"S-EPMC12917162","cross_references":{"pubmed":["41540027"],"doi":["10.1038/s41467-026-68477-2"]}}